메뉴 건너뛰기




Volumn 74, Issue 17, 2017, Pages 3091-3118

How order and disorder within paramyxoviral nucleoproteins and phosphoproteins orchestrate the molecular interplay of transcription and replication

Author keywords

Antiviral approaches; Fuzzy complexes; Induced folding; Intrinsic structural disorder; Nucleoprotein; Paramyxoviruses; Phosphoprotein; Protein protein interactions

Indexed keywords

ANTIVIRUS AGENT; GLYCINE DEHYDROGENASE (DECARBOXYLATING); GUANINE NUCLEOTIDE BINDING PROTEIN; INTRINSICALLY DISORDERED PROTEIN; NUCLEOCAPSID PROTEIN; PHOSPHOPROTEIN; VIRUS NUCLEOPROTEIN; CHAPERONE; NUCLEOPROTEIN; VIRAL PROTEIN; VIRUS RNA;

EID: 85020622279     PISSN: 1420682X     EISSN: 14209071     Source Type: Journal    
DOI: 10.1007/s00018-017-2556-3     Document Type: Review
Times cited : (31)

References (236)
  • 1
    • 84974668337 scopus 로고    scopus 로고
    • Paramyxoviridae
    • Knipe DM, Howley PM, (eds), Lippincott Williams & Wilkins, Philadelphia
    • Lamb RA, Parks GD (2013) Paramyxoviridae. In: Knipe DM, Howley PM (eds) Fields virology. Lippincott Williams & Wilkins, Philadelphia, pp 957–995
    • (2013) Fields virology , pp. 957-995
    • Lamb, R.A.1    Parks, G.D.2
  • 3
    • 34548504622 scopus 로고    scopus 로고
    • Henipaviruses
    • Fields BN, Knipe DM, Howley PM, (eds), Lippincott-Raven, Philadelphia
    • Eaton BT, Mackenzie JS, Wang LF (2007) Henipaviruses. In: Fields BN, Knipe DM, Howley PM (eds) Fields virology, 5th edn. Lippincott-Raven, Philadelphia, pp 1587–1600
    • (2007) Fields virology , pp. 1587-1600
    • Eaton, B.T.1    Mackenzie, J.S.2    Wang, L.F.3
  • 4
    • 0033779914 scopus 로고    scopus 로고
    • The exceptionally large genome of Hendra virus: support for creation of a new genus within the family Paramyxoviridae
    • COI: 1:CAS:528:DC%2BD3cXnsFOlt7s%3D, PID: 11024125
    • Wang LF, Yu M, Hansson E, Pritchard LI, Shiell B, Michalski WP, Eaton BT (2000) The exceptionally large genome of Hendra virus: support for creation of a new genus within the family Paramyxoviridae. J Virol 74:9972–9979
    • (2000) J Virol , vol.74 , pp. 9972-9979
    • Wang, L.F.1    Yu, M.2    Hansson, E.3    Pritchard, L.I.4    Shiell, B.5    Michalski, W.P.6    Eaton, B.T.7
  • 5
    • 31344481506 scopus 로고    scopus 로고
    • Hendra and Nipah viruses: different and dangerous
    • COI: 1:CAS:528:DC%2BD2MXhtlSqu7jE, PID: 16357858
    • Eaton BT, Broder CC, Middleton D, Wang LF (2006) Hendra and Nipah viruses: different and dangerous. Nat Rev Microbiol 4:23–35
    • (2006) Nat Rev Microbiol , vol.4 , pp. 23-35
    • Eaton, B.T.1    Broder, C.C.2    Middleton, D.3    Wang, L.F.4
  • 7
    • 0036441105 scopus 로고    scopus 로고
    • Substitution of two residues in the measles virus nucleoprotein results in an impaired self-association
    • COI: 1:CAS:528:DC%2BD38XosFWnsL8%3D, PID: 12441086
    • Karlin D, Longhi S, Canard B (2002) Substitution of two residues in the measles virus nucleoprotein results in an impaired self-association. Virology 302:420–432
    • (2002) Virology , vol.302 , pp. 420-432
    • Karlin, D.1    Longhi, S.2    Canard, B.3
  • 8
    • 0037705413 scopus 로고    scopus 로고
    • The C-terminal domain of the measles virus nucleoprotein is intrinsically disordered and folds upon binding to the C-terminal moiety of the phosphoprotein
    • COI: 1:CAS:528:DC%2BD3sXjs1KhtLs%3D, PID: 12621042
    • Longhi S, Receveur-Brechot V, Karlin D, Johansson K, Darbon H, Bhella D, Yeo R, Finet S, Canard B (2003) The C-terminal domain of the measles virus nucleoprotein is intrinsically disordered and folds upon binding to the C-terminal moiety of the phosphoprotein. J Biol Chem 278:18638–18648
    • (2003) J Biol Chem , vol.278 , pp. 18638-18648
    • Longhi, S.1    Receveur-Brechot, V.2    Karlin, D.3    Johansson, K.4    Darbon, H.5    Bhella, D.6    Yeo, R.7    Finet, S.8    Canard, B.9
  • 9
    • 2342521282 scopus 로고    scopus 로고
    • The 12 A structure of trypsin-treated measles virus N-RNA
    • COI: 1:CAS:528:DC%2BD2cXjsl2nsrc%3D, PID: 15136034
    • Schoehn G, Mavrakis M, Albertini A, Wade R, Hoenger A, Ruigrok RW (2004) The 12 A structure of trypsin-treated measles virus N-RNA. J Mol Biol 339:301–312
    • (2004) J Mol Biol , vol.339 , pp. 301-312
    • Schoehn, G.1    Mavrakis, M.2    Albertini, A.3    Wade, R.4    Hoenger, A.5    Ruigrok, R.W.6
  • 10
    • 77955359459 scopus 로고    scopus 로고
    • Measles virus nucleocapsid structure, conformational flexibility and the rule of six
    • Longhi S, (ed), Nova Publishers Inc., Hauppage
    • Bhella D (2007) Measles virus nucleocapsid structure, conformational flexibility and the rule of six. In: Longhi S (ed) Measles virus nucleoprotein. Nova Publishers Inc., Hauppage
    • (2007) Measles virus nucleoprotein
    • Bhella, D.1
  • 11
    • 78651394593 scopus 로고    scopus 로고
    • Nucleoprotein–RNA orientation in the measles virus nucleocapsid by three-dimensional electron microscopy
    • COI: 1:CAS:528:DC%2BC3MXisVOksbs%3D, PID: 21106738
    • Desfosses A, Goret G, Farias Estrozi L, Ruigrok RW, Gutsche I (2011) Nucleoprotein–RNA orientation in the measles virus nucleocapsid by three-dimensional electron microscopy. J Virol 85:1391–1395
    • (2011) J Virol , vol.85 , pp. 1391-1395
    • Desfosses, A.1    Goret, G.2    Farias Estrozi, L.3    Ruigrok, R.W.4    Gutsche, I.5
  • 12
  • 13
    • 1642305606 scopus 로고    scopus 로고
    • Nipah virus conforms to the rule of six in a minigenome replication assay
    • COI: 1:CAS:528:DC%2BD2cXisFGrsbk%3D, PID: 14993656
    • Halpin K, Bankamp B, Harcourt BH, Bellini WJ, Rota PA (2004) Nipah virus conforms to the rule of six in a minigenome replication assay. J Gen Virol 85:701–707
    • (2004) J Gen Virol , vol.85 , pp. 701-707
    • Halpin, K.1    Bankamp, B.2    Harcourt, B.H.3    Bellini, W.J.4    Rota, P.A.5
  • 14
    • 0031883549 scopus 로고    scopus 로고
    • Paramyxovirus RNA synthesis and the requirement for hexamer genome length: the rule of six revisited
    • COI: 1:CAS:528:DyaK1cXlt1CmsA%3D%3D, PID: 9444980
    • Kolakofsky D, Pelet T, Garcin D, Hausmann S, Curran J, Roux L (1998) Paramyxovirus RNA synthesis and the requirement for hexamer genome length: the rule of six revisited. J Virol 72:891–899
    • (1998) J Virol , vol.72 , pp. 891-899
    • Kolakofsky, D.1    Pelet, T.2    Garcin, D.3    Hausmann, S.4    Curran, J.5    Roux, L.6
  • 15
    • 17244373335 scopus 로고    scopus 로고
    • Dans le génome des Paramyxovirinae, les promoteurs et leurs activités sont façonnés par la « règle de six
    • Roux L (2005) Dans le génome des Paramyxovirinae, les promoteurs et leurs activités sont façonnés par la « règle de six. Virologie 9:19–34
    • (2005) Virologie , vol.9 , pp. 19-34
    • Roux, L.1
  • 16
    • 80051781196 scopus 로고    scopus 로고
    • Nucleoproteins and nucleocapsids of negative-strand RNA viruses
    • COI: 1:CAS:528:DC%2BC3MXhtVGlsLvN, PID: 21824806
    • Ruigrok RW, Crepin T, Kolakofsky D (2011) Nucleoproteins and nucleocapsids of negative-strand RNA viruses. Curr Opin Microbiol 14:504–510
    • (2011) Curr Opin Microbiol , vol.14 , pp. 504-510
    • Ruigrok, R.W.1    Crepin, T.2    Kolakofsky, D.3
  • 17
    • 0034846320 scopus 로고    scopus 로고
    • Complete nucleotide sequences of Nipah virus isolates from Malaysia
    • COI: 1:CAS:528:DC%2BD3MXmslSktLY%3D, PID: 11514724
    • Chan YP, Chua KB, Koh CL, Lim ME, Lam SK (2001) Complete nucleotide sequences of Nipah virus isolates from Malaysia. J Gen Virol 82:2151–2155
    • (2001) J Gen Virol , vol.82 , pp. 2151-2155
    • Chan, Y.P.1    Chua, K.B.2    Koh, C.L.3    Lim, M.E.4    Lam, S.K.5
  • 19
    • 0035983614 scopus 로고    scopus 로고
    • Significant differences in nucleocapsid morphology within the Paramyxoviridae
    • COI: 1:CAS:528:DC%2BD38XlvVCrsr0%3D, PID: 12124447
    • Bhella D, Ralph A, Murphy LB, Yeo RP (2002) Significant differences in nucleocapsid morphology within the Paramyxoviridae. J Gen Virol 83:1831–1839
    • (2002) J Gen Virol , vol.83 , pp. 1831-1839
    • Bhella, D.1    Ralph, A.2    Murphy, L.B.3    Yeo, R.P.4
  • 20
    • 1842612571 scopus 로고    scopus 로고
    • Solubility, immunogenicity and physical properties of the nucleocapsid protein of Nipah virus produced in Escherichia coli
    • COI: 1:CAS:528:DC%2BD2cXjslertrc%3D, PID: 15042656
    • Tan WS, Ong ST, Eshaghi M, Foo SS, Yusoff K (2004) Solubility, immunogenicity and physical properties of the nucleocapsid protein of Nipah virus produced in Escherichia coli. J Med Virol 73:105–112
    • (2004) J Med Virol , vol.73 , pp. 105-112
    • Tan, W.S.1    Ong, S.T.2    Eshaghi, M.3    Foo, S.S.4    Yusoff, K.5
  • 22
    • 0030832332 scopus 로고    scopus 로고
    • The assembly of the measles virus nucleoprotein into nucleocapsid-like particles is modulated by the phosphoprotein
    • COI: 1:CAS:528:DyaK2sXjvFamtbc%3D, PID: 9191839
    • Spehner D, Drillien R, Howley PM (1997) The assembly of the measles virus nucleoprotein into nucleocapsid-like particles is modulated by the phosphoprotein. Virology 232:260–268
    • (1997) Virology , vol.232 , pp. 260-268
    • Spehner, D.1    Drillien, R.2    Howley, P.M.3
  • 23
    • 18344382350 scopus 로고    scopus 로고
    • Structures impliquées dans la réplication et la transcription des virus à ARN non segmentés de sens négatif
    • Albertini AAV, Schoehn G, Ruigrok RW (2005) Structures impliquées dans la réplication et la transcription des virus à ARN non segmentés de sens négatif. Virologie 9:83–92
    • (2005) Virologie , vol.9 , pp. 83-92
    • Albertini, A.A.V.1    Schoehn, G.2    Ruigrok, R.W.3
  • 24
    • 0032795316 scopus 로고    scopus 로고
    • Mécanismes de transcription et de réplication des Paramyxoviridae
    • Longhi S, Canard B (1999) Mécanismes de transcription et de réplication des Paramyxoviridae. Virologie 3:227–240
    • (1999) Virologie , vol.3 , pp. 227-240
    • Longhi, S.1    Canard, B.2
  • 25
    • 84857998251 scopus 로고    scopus 로고
    • Mechanism of RNA synthesis initiation by the vesicular stomatitis virus polymerase
    • COI: 1:CAS:528:DC%2BC38XlsFylsA%3D%3D, PID: 22246179
    • Morin B, Rahmeh AA, Whelan SP (2012) Mechanism of RNA synthesis initiation by the vesicular stomatitis virus polymerase. EMBO J 31:1320–1329
    • (2012) EMBO J , vol.31 , pp. 1320-1329
    • Morin, B.1    Rahmeh, A.A.2    Whelan, S.P.3
  • 26
    • 85008219763 scopus 로고    scopus 로고
    • An in vitro RNA synthesis assay for rabies virus defines critical ribonucleoprotein interactions for polymerase activity
    • PID: 27795419
    • Morin B, Liang B, Gardner E, Ross RA, Whelan SP (2016) An in vitro RNA synthesis assay for rabies virus defines critical ribonucleoprotein interactions for polymerase activity. J Virol 91(1):e01508-16
    • (2016) J Virol , vol.91 , Issue.1
    • Morin, B.1    Liang, B.2    Gardner, E.3    Ross, R.A.4    Whelan, S.P.5
  • 27
    • 84982822062 scopus 로고    scopus 로고
    • HSP90 Chaperoning in addition to phosphoprotein required for folding but not for supporting enzymatic activities of measles and Nipah virus L polymerases
    • COI: 1:CAS:528:DC%2BC28Xhslyrs7jP, PID: 27170753
    • Bloyet LM, Welsch J, Enchery F, Mathieu C, de Breyne S, Horvat B, Grigorov B, Gerlier D (2016) HSP90 Chaperoning in addition to phosphoprotein required for folding but not for supporting enzymatic activities of measles and Nipah virus L polymerases. J Virol 90:6642–6656
    • (2016) J Virol , vol.90 , pp. 6642-6656
    • Bloyet, L.M.1    Welsch, J.2    Enchery, F.3    Mathieu, C.4    de Breyne, S.5    Horvat, B.6    Grigorov, B.7    Gerlier, D.8
  • 28
    • 85014091503 scopus 로고    scopus 로고
    • Heat shock protein 90 ensures efficient mumps virus replication by assisting with viral polymerase complex formation
    • Katoh H, Kubota T, Nakatsu Y, Tahara M, Kidokoro M, Takeda M (2017) Heat shock protein 90 ensures efficient mumps virus replication by assisting with viral polymerase complex formation. J Virol. doi:10.1128/JVI.02220-16
    • (2017) J Virol
    • Katoh, H.1    Kubota, T.2    Nakatsu, Y.3    Tahara, M.4    Kidokoro, M.5    Takeda, M.6
  • 29
    • 58149131364 scopus 로고    scopus 로고
    • Phosphoprotein, P of human parainfluenza virus type 3 prevents self-association of RNA-dependent RNA polymerase, L
    • COI: 1:CAS:528:DC%2BD1MXktlKgsQ%3D%3D, PID: 19012944
    • Chattopadhyay S, Banerjee AK (2009) Phosphoprotein, P of human parainfluenza virus type 3 prevents self-association of RNA-dependent RNA polymerase, L. Virology 383:226–236
    • (2009) Virology , vol.383 , pp. 226-236
    • Chattopadhyay, S.1    Banerjee, A.K.2
  • 30
    • 44349115502 scopus 로고    scopus 로고
    • Recombinant L and P protein complex of Rinderpest virus catalyses mRNA synthesis in vitro
    • COI: 1:CAS:528:DC%2BD1cXmsFKntrc%3D, PID: 18430484
    • Gopinath M, Shaila MS (2008) Recombinant L and P protein complex of Rinderpest virus catalyses mRNA synthesis in vitro. Virus Res 135:150–154
    • (2008) Virus Res , vol.135 , pp. 150-154
    • Gopinath, M.1    Shaila, M.S.2
  • 31
    • 14244266290 scopus 로고    scopus 로고
    • Sendai virus RNA-dependent RNA polymerase L protein catalyzes cap methylation of virus-specific mRNA
    • COI: 1:CAS:528:DC%2BD2MXhtVyms74%3D, PID: 15574411
    • Ogino T, Kobayashi M, Iwama M, Mizumoto K (2005) Sendai virus RNA-dependent RNA polymerase L protein catalyzes cap methylation of virus-specific mRNA. J Biol Chem 280:4429–4435
    • (2005) J Biol Chem , vol.280 , pp. 4429-4435
    • Ogino, T.1    Kobayashi, M.2    Iwama, M.3    Mizumoto, K.4
  • 32
    • 0036558021 scopus 로고    scopus 로고
    • Viral RNA-polymerases—a predicted 2′-O-ribose methyltransferase domain shared by all Mononegavirales
    • COI: 1:CAS:528:DC%2BD38XktlSms7s%3D, PID: 12076527
    • Ferron F, Longhi S, Henrissat B, Canard B (2002) Viral RNA-polymerases—a predicted 2′-O-ribose methyltransferase domain shared by all Mononegavirales. Trends Biochem Sci 27:222–224
    • (2002) Trends Biochem Sci , vol.27 , pp. 222-224
    • Ferron, F.1    Longhi, S.2    Henrissat, B.3    Canard, B.4
  • 33
    • 84868120541 scopus 로고    scopus 로고
    • The respiratory syncytial virus polymerase has multiple RNA synthesis activities at the promoter
    • COI: 1:CAS:528:DC%2BC38Xhs1ant7jM, PID: 23093940
    • Noton SL, Deflube LR, Tremaglio CZ, Fearns R (2012) The respiratory syncytial virus polymerase has multiple RNA synthesis activities at the promoter. PLoS Pathog 8:e1002980
    • (2012) PLoS Pathog , vol.8
    • Noton, S.L.1    Deflube, L.R.2    Tremaglio, C.Z.3    Fearns, R.4
  • 35
    • 63149159388 scopus 로고    scopus 로고
    • Measles virus nucleoprotein: structural organization and functional role of the intrinsically disordered C-terminal domain
    • Longhi S, (ed), Nova Publishers Inc., Hauppage
    • Bourhis JM, Longhi S (2007) Measles virus nucleoprotein: structural organization and functional role of the intrinsically disordered C-terminal domain. In: Longhi S (ed) Measles virus nucleoprotein. Nova Publishers Inc., Hauppage, pp 1–35
    • (2007) Measles virus nucleoprotein , pp. 1-35
    • Bourhis, J.M.1    Longhi, S.2
  • 37
    • 58349120410 scopus 로고    scopus 로고
    • Nucleocapsid structure and function
    • COI: 1:CAS:528:DC%2BD1MXhs1Sqtb8%3D, PID: 19198564
    • Longhi S (2009) Nucleocapsid structure and function. Curr Top Microbiol Immunol 329:103–128
    • (2009) Curr Top Microbiol Immunol , vol.329 , pp. 103-128
    • Longhi, S.1
  • 38
    • 77956596750 scopus 로고    scopus 로고
    • Structural disorder within the measles virus nucleoprotein and phosphoprotein
    • COI: 1:CAS:528:DC%2BC3cXpsFeitrs%3D, PID: 20450481
    • Longhi S, Oglesbee M (2010) Structural disorder within the measles virus nucleoprotein and phosphoprotein. Protein Pept Lett 17:961–978
    • (2010) Protein Pept Lett , vol.17 , pp. 961-978
    • Longhi, S.1    Oglesbee, M.2
  • 39
    • 84973102890 scopus 로고    scopus 로고
    • Structural disorder within the measles virus nucleoprotein and phosphoprotein: functional implications for transcription and replication
    • Luo M, (ed), World Scientific Publishing, Singapore
    • Longhi S (2011) Structural disorder within the measles virus nucleoprotein and phosphoprotein: functional implications for transcription and replication. In: Luo M (ed) Negative strand RNA virus. World Scientific Publishing, Singapore, pp 95–125
    • (2011) Negative strand RNA virus , pp. 95-125
    • Longhi, S.1
  • 40
    • 82655179925 scopus 로고    scopus 로고
    • Structural disorder within paramyxovirus nucleoproteins and phosphoproteins
    • COI: 1:CAS:528:DC%2BC3MXhsFKgs7jI, PID: 21805002
    • Habchi J, Longhi S (2012) Structural disorder within paramyxovirus nucleoproteins and phosphoproteins. Mol BioSyst 8:69–81
    • (2012) Mol BioSyst , vol.8 , pp. 69-81
    • Habchi, J.1    Longhi, S.2
  • 41
    • 82655165124 scopus 로고    scopus 로고
    • Structural disorder within the nucleoprotein and phosphoprotein from measles, Nipah and Hendra viruses
    • Uversky VN, Longhi S, (eds), Wiley, Hoboken
    • Habchi J, Mamelli L, Longhi S (2012) Structural disorder within the nucleoprotein and phosphoprotein from measles, Nipah and Hendra viruses. In: Uversky VN, Longhi S (eds) Flexible viruses: structural disorder in viral proteins. Wiley, Hoboken, pp 47–94
    • (2012) Flexible viruses: structural disorder in viral proteins , pp. 47-94
    • Habchi, J.1    Mamelli, L.2    Longhi, S.3
  • 42
    • 84896518166 scopus 로고    scopus 로고
    • Intrinsically disordered proteins implicated in paramyxoviral replication machinery
    • COI: 1:CAS:528:DC%2BC2cXosVWht70%3D, PID: 24631901
    • Communie G, Ruigrok RW, Jensen MR, Blackledge M (2014) Intrinsically disordered proteins implicated in paramyxoviral replication machinery. Curr Opin Virol 5:72–81
    • (2014) Curr Opin Virol , vol.5 , pp. 72-81
    • Communie, G.1    Ruigrok, R.W.2    Jensen, M.R.3    Blackledge, M.4
  • 43
    • 84942293554 scopus 로고    scopus 로고
    • Structural disorder within paramyxoviral nucleoproteins
    • COI: 1:CAS:528:DC%2BC2MXhtVeitLbI, PID: 26071376
    • Longhi S (2015) Structural disorder within paramyxoviral nucleoproteins. FEBS Lett 589:2649–2659
    • (2015) FEBS Lett , vol.589 , pp. 2649-2659
    • Longhi, S.1
  • 44
    • 84939561035 scopus 로고    scopus 로고
    • Structural disorder within paramyxoviral nucleoproteins and phosphoproteins in their free and bound forms: from predictions to experimental assessment
    • COI: 1:CAS:528:DC%2BC2MXhsl2qs7bI, PID: 26184170
    • Habchi J, Longhi S (2015) Structural disorder within paramyxoviral nucleoproteins and phosphoproteins in their free and bound forms: from predictions to experimental assessment. Int J Mol Sci 16:15688–15726
    • (2015) Int J Mol Sci , vol.16 , pp. 15688-15726
    • Habchi, J.1    Longhi, S.2
  • 45
    • 0036299393 scopus 로고    scopus 로고
    • The N-terminal domain of the phosphoprotein of Morbilliviruses belongs to the natively unfolded class of proteins
    • COI: 1:CAS:528:DC%2BD38XksFOgtLg%3D, PID: 12069524
    • Karlin D, Longhi S, Receveur V, Canard B (2002) The N-terminal domain of the phosphoprotein of Morbilliviruses belongs to the natively unfolded class of proteins. Virology 296:251–262
    • (2002) Virology , vol.296 , pp. 251-262
    • Karlin, D.1    Longhi, S.2    Receveur, V.3    Canard, B.4
  • 47
    • 37749053887 scopus 로고    scopus 로고
    • Fuzzy complexes: polymorphism and structural disorder in protein–protein interactions
    • COI: 1:CAS:528:DC%2BD1cXlvV2jsw%3D%3D, PID: 18054235
    • Tompa P, Fuxreiter M (2008) Fuzzy complexes: polymorphism and structural disorder in protein–protein interactions. Trends Biochem Sci 33:2–8
    • (2008) Trends Biochem Sci , vol.33 , pp. 2-8
    • Tompa, P.1    Fuxreiter, M.2
  • 48
    • 85016050879 scopus 로고    scopus 로고
    • FuzDB: database of fuzzy complexes, a tool to develop stochastic structure-function relationships for protein complexes and higher-order assemblies
    • PID: 27794553
    • Miskei M, Antal C, Fuxreiter M (2016) FuzDB: database of fuzzy complexes, a tool to develop stochastic structure-function relationships for protein complexes and higher-order assemblies. Nucleic Acids Res 45:D228–S235
    • (2016) Nucleic Acids Res , vol.45 , pp. D228-S235
    • Miskei, M.1    Antal, C.2    Fuxreiter, M.3
  • 49
    • 84903957091 scopus 로고    scopus 로고
    • Introducing protein intrinsic disorder
    • COI: 1:CAS:528:DC%2BC2cXmtlygt7Y%3D, PID: 24739139
    • Habchi J, Tompa P, Longhi S, Uversky VN (2014) Introducing protein intrinsic disorder. Chem Rev 114:6561–6588
    • (2014) Chem Rev , vol.114 , pp. 6561-6588
    • Habchi, J.1    Tompa, P.2    Longhi, S.3    Uversky, V.N.4
  • 50
    • 77955399035 scopus 로고    scopus 로고
    • Structural disorder within Henipavirus nucleoprotein and phosphoprotein: from predictions to experimental assessment
    • PID: 20657787
    • Habchi J, Mamelli L, Darbon H, Longhi S (2010) Structural disorder within Henipavirus nucleoprotein and phosphoprotein: from predictions to experimental assessment. PLoS One 5:e11684
    • (2010) PLoS One , vol.5
    • Habchi, J.1    Mamelli, L.2    Darbon, H.3    Longhi, S.4
  • 51
    • 0346752214 scopus 로고    scopus 로고
    • Structural disorder and modular organization in Paramyxovirinae N and P
    • COI: 1:CAS:528:DC%2BD3sXpvFartLo%3D, PID: 14645906
    • Karlin D, Ferron F, Canard B, Longhi S (2003) Structural disorder and modular organization in Paramyxovirinae N and P. J Gen Virol 84:3239–3252
    • (2003) J Gen Virol , vol.84 , pp. 3239-3252
    • Karlin, D.1    Ferron, F.2    Canard, B.3    Longhi, S.4
  • 52
    • 52249108097 scopus 로고    scopus 로고
    • MeDor: a metaserver for predicting protein disorder
    • Lieutaud P, Canard B, Longhi S (2008) MeDor: a metaserver for predicting protein disorder. BMC Genom 9:S25
    • (2008) BMC Genom , vol.9 , pp. S25
    • Lieutaud, P.1    Canard, B.2    Longhi, S.3
  • 54
    • 24944546549 scopus 로고    scopus 로고
    • Coupled folding and binding with alpha-helix-forming molecular recognition elements
    • COI: 1:CAS:528:DC%2BD2MXoslCnur4%3D, PID: 16156658
    • Oldfield CJ, Cheng Y, Cortese MS, Romero P, Uversky VN, Dunker AK (2005) Coupled folding and binding with alpha-helix-forming molecular recognition elements. Biochemistry 44:12454–12470
    • (2005) Biochemistry , vol.44 , pp. 12454-12470
    • Oldfield, C.J.1    Cheng, Y.2    Cortese, M.S.3    Romero, P.4    Uversky, V.N.5    Dunker, A.K.6
  • 56
    • 34250815165 scopus 로고    scopus 로고
    • Characterization of molecular recognition features, MoRFs, and their binding partners
    • COI: 1:CAS:528:DC%2BD2sXltVajtL8%3D, PID: 17488107
    • Vacic V, Oldfield CJ, Mohan A, Radivojac P, Cortese MS, Uversky VN, Dunker AK (2007) Characterization of molecular recognition features, MoRFs, and their binding partners. J Proteome Res 6:2351–2366
    • (2007) J Proteome Res , vol.6 , pp. 2351-2366
    • Vacic, V.1    Oldfield, C.J.2    Mohan, A.3    Radivojac, P.4    Cortese, M.S.5    Uversky, V.N.6    Dunker, A.K.7
  • 58
    • 84961158406 scopus 로고    scopus 로고
    • Crystal structure of the measles virus nucleoprotein core in complex with an N-terminal region of phosphoprotein
    • COI: 1:CAS:528:DC%2BC28XhtVChsrnF
    • Guryanov SG, Liljeroos L, Kasaragod P, Kajander T, Butcher SJ (2016) Crystal structure of the measles virus nucleoprotein core in complex with an N-terminal region of phosphoprotein. J Virol 90:2849–2857
    • (2016) J Virol , vol.90 , pp. 2849-2857
    • Guryanov, S.G.1    Liljeroos, L.2    Kasaragod, P.3    Kajander, T.4    Butcher, S.J.5
  • 59
    • 84857734722 scopus 로고    scopus 로고
    • Detecting remote sequence homology in disordered proteins: discovery of conserved motifs in the N-termini of Mononegavirales phosphoproteins
    • COI: 1:CAS:528:DC%2BC38XjvFajtLs%3D, PID: 22403617
    • Karlin D, Belshaw R (2012) Detecting remote sequence homology in disordered proteins: discovery of conserved motifs in the N-termini of Mononegavirales phosphoproteins. PLoS One 7:e31719
    • (2012) PLoS One , vol.7
    • Karlin, D.1    Belshaw, R.2
  • 62
    • 79952149646 scopus 로고    scopus 로고
    • The N(0)-binding region of the vesicular stomatitis virus phosphoprotein is globally disordered but contains transient alpha-helices
    • COI: 1:CAS:528:DC%2BC3MXjvFWnu7o%3D, PID: 21207454
    • Leyrat C, Jensen MR, Ribeiro EA Jr, Gerard FC, Ruigrok RW, Blackledge M, Jamin M (2011) The N(0)-binding region of the vesicular stomatitis virus phosphoprotein is globally disordered but contains transient alpha-helices. Protein Sci 20:542–556
    • (2011) Protein Sci , vol.20 , pp. 542-556
    • Leyrat, C.1    Jensen, M.R.2    Ribeiro, E.A.3    Gerard, F.C.4    Ruigrok, R.W.5    Blackledge, M.6    Jamin, M.7
  • 65
    • 85012065390 scopus 로고    scopus 로고
    • New insights into structural disorder in human respiratory syncytial virus phosphoprotein and implications for binding of protein partners
    • COI: 1:CAS:528:DC%2BC2sXisVGisLk%3D, PID: 28031463
    • Pereira N, Cardone C, Lassoued S, Galloux M, Fix J, Assrir N, Lescop E, Bontems F, Eleouet JF, Sizun C (2017) New insights into structural disorder in human respiratory syncytial virus phosphoprotein and implications for binding of protein partners. J Biol Chem 292:2120–2131
    • (2017) J Biol Chem , vol.292 , pp. 2120-2131
    • Pereira, N.1    Cardone, C.2    Lassoued, S.3    Galloux, M.4    Fix, J.5    Assrir, N.6    Lescop, E.7    Bontems, F.8    Eleouet, J.F.9    Sizun, C.10
  • 66
    • 0035866606 scopus 로고    scopus 로고
    • Rinderpest virus C and V proteins interact with the major (L) component of the viral polymerase
    • COI: 1:CAS:528:DC%2BD3MXit1antLk%3D, PID: 11277692
    • Sweetman DA, Miskin J, Baron MD (2001) Rinderpest virus C and V proteins interact with the major (L) component of the viral polymerase. Virology 281:193–204
    • (2001) Virology , vol.281 , pp. 193-204
    • Sweetman, D.A.1    Miskin, J.2    Baron, M.D.3
  • 67
    • 84901034931 scopus 로고    scopus 로고
    • Phosphoprotein of human parainfluenza virus type 3 blocks autophagosome–lysosome fusion to increase virus production
    • COI: 1:CAS:528:DC%2BC2cXotFyntLw%3D, PID: 24832451
    • Ding B, Zhang G, Yang X, Zhang S, Chen L, Yan Q, Xu M, Banerjee AK, Chen M (2014) Phosphoprotein of human parainfluenza virus type 3 blocks autophagosome–lysosome fusion to increase virus production. Cell Host Microbe 15:564–577
    • (2014) Cell Host Microbe , vol.15 , pp. 564-577
    • Ding, B.1    Zhang, G.2    Yang, X.3    Zhang, S.4    Chen, L.5    Yan, Q.6    Xu, M.7    Banerjee, A.K.8    Chen, M.9
  • 68
    • 70349728537 scopus 로고    scopus 로고
    • Peptides that mimic the amino-terminal end of the rabies virus phosphoprotein have antiviral activity
    • COI: 1:CAS:528:DC%2BD1MXhtlCltr%2FM, PID: 19706704
    • Castel G, Chteoui M, Caignard G, Prehaud C, Mehouas S, Real E, Jallet C, Jacob Y, Ruigrok RW, Tordo N (2009) Peptides that mimic the amino-terminal end of the rabies virus phosphoprotein have antiviral activity. J Virol 83:10808–10820
    • (2009) J Virol , vol.83 , pp. 10808-10820
    • Castel, G.1    Chteoui, M.2    Caignard, G.3    Prehaud, C.4    Mehouas, S.5    Real, E.6    Jallet, C.7    Jacob, Y.8    Ruigrok, R.W.9    Tordo, N.10
  • 69
    • 84865963708 scopus 로고    scopus 로고
    • Critical phosphoprotein elements that regulate polymerase architecture and function in vesicular stomatitis virus
    • COI: 1:CAS:528:DC%2BC38XhsVaqu7zE, PID: 22908284
    • Rahmeh AA, Morin B, Schenk AD, Liang B, Heinrich BS, Brusic V, Walz T, Whelan SP (2012) Critical phosphoprotein elements that regulate polymerase architecture and function in vesicular stomatitis virus. Proc Natl Acad Sci USA 109:14628–14633
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 14628-14633
    • Rahmeh, A.A.1    Morin, B.2    Schenk, A.D.3    Liang, B.4    Heinrich, B.S.5    Brusic, V.6    Walz, T.7    Whelan, S.P.8
  • 71
    • 85001114520 scopus 로고    scopus 로고
    • Nonsegmented negative-sense RNA viruses-structural data bring new insights into nucleocapsid assembly
    • COI: 1:STN:280:DC%2BC1c7islaltQ%3D%3D, PID: 28057258
    • Jamin M, Yabukarski F (2017) Nonsegmented negative-sense RNA viruses-structural data bring new insights into nucleocapsid assembly. Adv Virus Res 97:143–185
    • (2017) Adv Virus Res , vol.97 , pp. 143-185
    • Jamin, M.1    Yabukarski, F.2
  • 72
    • 33644774586 scopus 로고    scopus 로고
    • Crystal structure of the oligomerization domain of the phosphoprotein of vesicular stomatitis virus
    • COI: 1:CAS:528:DC%2BD28Xis1Cqsbo%3D, PID: 16501089
    • Ding H, Green TJ, Lu S, Luo M (2006) Crystal structure of the oligomerization domain of the phosphoprotein of vesicular stomatitis virus. J Virol 80:2808–2814
    • (2006) J Virol , vol.80 , pp. 2808-2814
    • Ding, H.1    Green, T.J.2    Lu, S.3    Luo, M.4
  • 73
    • 77949393859 scopus 로고    scopus 로고
    • Structure of the dimerization domain of the rabies virus phosphoprotein
    • COI: 1:CAS:528:DC%2BC3cXktFOgur8%3D, PID: 20089657
    • Ivanov I, Crepin T, Jamin M, Ruigrok RW (2010) Structure of the dimerization domain of the rabies virus phosphoprotein. J Virol 84:3707–3710
    • (2010) J Virol , vol.84 , pp. 3707-3710
    • Ivanov, I.1    Crepin, T.2    Jamin, M.3    Ruigrok, R.W.4
  • 74
    • 0036128797 scopus 로고    scopus 로고
    • Natively unfolded proteins: a point where biology waits for physics
    • COI: 1:CAS:528:DC%2BD38Xis1Wmu74%3D, PID: 11910019
    • Uversky VN (2002) Natively unfolded proteins: a point where biology waits for physics. Protein Sci 11:739–756
    • (2002) Protein Sci , vol.11 , pp. 739-756
    • Uversky, V.N.1
  • 76
    • 75849127571 scopus 로고    scopus 로고
    • Phosphorylation of paramyxovirus phosphoprotein and its role in viral gene expression
    • COI: 1:CAS:528:DC%2BD1MXhsFyhsL3N, PID: 20020826
    • Fuentes SM, Sun D, Schmitt AP, He B (2010) Phosphorylation of paramyxovirus phosphoprotein and its role in viral gene expression. Future Microbiol 5:9–13
    • (2010) Future Microbiol , vol.5 , pp. 9-13
    • Fuentes, S.M.1    Sun, D.2    Schmitt, A.P.3    He, B.4
  • 80
    • 1642512502 scopus 로고    scopus 로고
    • The C-terminal domain of measles virus nucleoprotein belongs to the class of intrinsically disordered proteins that fold upon binding to their physiological partner
    • COI: 1:CAS:528:DC%2BD2cXntV2gsQ%3D%3D, PID: 14749181
    • Bourhis J, Johansson K, Receveur-Bréchot V, Oldfield CJ, Dunker AK, Canard B, Longhi S (2004) The C-terminal domain of measles virus nucleoprotein belongs to the class of intrinsically disordered proteins that fold upon binding to their physiological partner. Virus Res 99:157–167
    • (2004) Virus Res , vol.99 , pp. 157-167
    • Bourhis, J.1    Johansson, K.2    Receveur-Bréchot, V.3    Oldfield, C.J.4    Dunker, A.K.5    Canard, B.6    Longhi, S.7
  • 81
    • 34250849555 scopus 로고    scopus 로고
    • Interaction of the C-terminal domains of Sendai virus N and P proteins: comparison of polymerase-nucleocapsid interactions within the paramyxovirus family
    • COI: 1:CAS:528:DC%2BD2sXntVOis78%3D, PID: 17459940
    • Houben K, Marion D, Tarbouriech N, Ruigrok RW, Blanchard L (2007) Interaction of the C-terminal domains of Sendai virus N and P proteins: comparison of polymerase-nucleocapsid interactions within the paramyxovirus family. J Virol 81:6807–6816
    • (2007) J Virol , vol.81 , pp. 6807-6816
    • Houben, K.1    Marion, D.2    Tarbouriech, N.3    Ruigrok, R.W.4    Blanchard, L.5
  • 82
    • 0242582329 scopus 로고    scopus 로고
    • Crystal structure of the measles virus phosphoprotein domain responsible for the induced folding of the C-terminal domain of the nucleoprotein
    • COI: 1:CAS:528:DC%2BD3sXoslWlsr8%3D, PID: 12944395
    • Johansson K, Bourhis JM, Campanacci V, Cambillau C, Canard B, Longhi S (2003) Crystal structure of the measles virus phosphoprotein domain responsible for the induced folding of the C-terminal domain of the nucleoprotein. J Biol Chem 278:44567–44573
    • (2003) J Biol Chem , vol.278 , pp. 44567-44573
    • Johansson, K.1    Bourhis, J.M.2    Campanacci, V.3    Cambillau, C.4    Canard, B.5    Longhi, S.6
  • 83
    • 2942595913 scopus 로고    scopus 로고
    • Structural basis for the attachment of a paramyxoviral polymerase to its template
    • COI: 1:CAS:528:DC%2BD2cXkvFOms7Y%3D, PID: 15159535
    • Kingston RL, Hamel DJ, Gay LS, Dahlquist FW, Matthews BW (2004) Structural basis for the attachment of a paramyxoviral polymerase to its template. Proc Natl Acad Sci USA 101:8301–8306
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 8301-8306
    • Kingston, R.L.1    Hamel, D.J.2    Gay, L.S.3    Dahlquist, F.W.4    Matthews, B.W.5
  • 84
    • 3543139986 scopus 로고    scopus 로고
    • Characterization of nucleocapsid binding by the measles and the mumps virus phosphoprotein
    • COI: 1:CAS:528:DC%2BD2cXmslSmtLs%3D, PID: 15280472
    • Kingston RL, Walter AB, Gay LS (2004) Characterization of nucleocapsid binding by the measles and the mumps virus phosphoprotein. J Virol 78:8630–8640
    • (2004) J Virol , vol.78 , pp. 8630-8640
    • Kingston, R.L.1    Walter, A.B.2    Gay, L.S.3
  • 85
    • 28044458515 scopus 로고    scopus 로고
    • A structural model for unfolded proteins from residual dipolar couplings and small-angle X-ray scattering
    • COI: 1:CAS:528:DC%2BD2MXht1yksLjO, PID: 16284250
    • Bernado P, Blanchard L, Timmins P, Marion D, Ruigrok RW, Blackledge M (2005) A structural model for unfolded proteins from residual dipolar couplings and small-angle X-ray scattering. Proc Natl Acad Sci USA 102:17002–17007
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 17002-17007
    • Bernado, P.1    Blanchard, L.2    Timmins, P.3    Marion, D.4    Ruigrok, R.W.5    Blackledge, M.6
  • 86
    • 1342321890 scopus 로고    scopus 로고
    • Structure and dynamics of the nucleocapsid-binding domain of the Sendai virus phosphoprotein in solution
    • COI: 1:CAS:528:DC%2BD2cXhsFWks70%3D, PID: 14980481
    • Blanchard L, Tarbouriech N, Blackledge M, Timmins P, Burmeister WP, Ruigrok RW, Marion D (2004) Structure and dynamics of the nucleocapsid-binding domain of the Sendai virus phosphoprotein in solution. Virology 319:201–211
    • (2004) Virology , vol.319 , pp. 201-211
    • Blanchard, L.1    Tarbouriech, N.2    Blackledge, M.3    Timmins, P.4    Burmeister, W.P.5    Ruigrok, R.W.6    Marion, D.7
  • 87
    • 35349018413 scopus 로고    scopus 로고
    • Intrinsic dynamics of the partly unstructured PX domain from the Sendai virus RNA polymerase cofactor P
    • COI: 1:CAS:528:DC%2BD2sXhtFKmsbjF, PID: 17586564
    • Houben K, Blanchard L, Blackledge M, Marion D (2007) Intrinsic dynamics of the partly unstructured PX domain from the Sendai virus RNA polymerase cofactor P. Biophys J 93:2830–2844
    • (2007) Biophys J , vol.93 , pp. 2830-2844
    • Houben, K.1    Blanchard, L.2    Blackledge, M.3    Marion, D.4
  • 88
    • 84878585682 scopus 로고    scopus 로고
    • Structure of the tetramerization domain of measles virus phosphoprotein
    • COI: 1:CAS:528:DC%2BC3sXptlKrtrc%3D, PID: 23576502
    • Communie G, Crepin T, Maurin D, Jensen MR, Blackledge M, Ruigrok RW (2013) Structure of the tetramerization domain of measles virus phosphoprotein. J Virol 87:7166–7169
    • (2013) J Virol , vol.87 , pp. 7166-7169
    • Communie, G.1    Crepin, T.2    Maurin, D.3    Jensen, M.R.4    Blackledge, M.5    Ruigrok, R.W.6
  • 89
    • 0033813425 scopus 로고    scopus 로고
    • Tetrameric coiled coil domain of Sendai virus phosphoprotein
    • COI: 1:CAS:528:DC%2BD3cXmsFWksrw%3D, PID: 10966649
    • Tarbouriech N, Curran J, Ruigrok RW, Burmeister WP (2000) Tetrameric coiled coil domain of Sendai virus phosphoprotein. Nat Struct Biol 7:777–781
    • (2000) Nat Struct Biol , vol.7 , pp. 777-781
    • Tarbouriech, N.1    Curran, J.2    Ruigrok, R.W.3    Burmeister, W.P.4
  • 90
    • 77955378293 scopus 로고    scopus 로고
    • Solution structure of the C-terminal X domain of the measles virus phosphoprotein and interaction with the intrinsically disordered C-terminal domain of the nucleoprotein
    • COI: 1:CAS:528:DC%2BC3cXhtFSis7zO, PID: 20058326
    • Gely S, Lowry DF, Bernard C, Ringkjobing-Jensen M, Blackledge M, Costanzo S, Darbon H, Daughdrill GW, Longhi S (2010) Solution structure of the C-terminal X domain of the measles virus phosphoprotein and interaction with the intrinsically disordered C-terminal domain of the nucleoprotein. J Mol Recognit 23:435–447
    • (2010) J Mol Recognit , vol.23 , pp. 435-447
    • Gely, S.1    Lowry, D.F.2    Bernard, C.3    Ringkjobing-Jensen, M.4    Blackledge, M.5    Costanzo, S.6    Darbon, H.7    Daughdrill, G.W.8    Longhi, S.9
  • 93
    • 44149110311 scopus 로고    scopus 로고
    • Structure of the nucleocapsid-binding domain from the mumps virus polymerase; an example of protein folding induced by crystallization
    • COI: 1:CAS:528:DC%2BD1cXmsFKqs7s%3D, PID: 18468621
    • Kingston RL, Gay LS, Baase WS, Matthews BW (2008) Structure of the nucleocapsid-binding domain from the mumps virus polymerase; an example of protein folding induced by crystallization. J Mol Biol 379:719–731
    • (2008) J Mol Biol , vol.379 , pp. 719-731
    • Kingston, R.L.1    Gay, L.S.2    Baase, W.S.3    Matthews, B.W.4
  • 95
    • 84885648103 scopus 로고    scopus 로고
    • The measles virus nucleocapsid protein tail domain is dispensable for viral polymerase recruitment and activity
    • COI: 1:CAS:528:DC%2BC3sXhs1Siu7jK, PID: 24003217
    • Krumm SA, Takeda M, Plemper RK (2013) The measles virus nucleocapsid protein tail domain is dispensable for viral polymerase recruitment and activity. J Biol Chem 288:29943–29953
    • (2013) J Biol Chem , vol.288 , pp. 29943-29953
    • Krumm, S.A.1    Takeda, M.2    Plemper, R.K.3
  • 96
    • 30344469079 scopus 로고    scopus 로고
    • Structural analysis of the human respiratory syncitial virus phosphoprotein: characterization of an a-helical domain involved in oligomerization
    • COI: 1:CAS:528:DC%2BD28XktlGiuw%3D%3D, PID: 16361428
    • Llorente MT, Barreno-Garcia B, Calero M, Camafeita E, Lopez JA, Longhi S, Ferron F, Varela PF, Melero JA (2006) Structural analysis of the human respiratory syncitial virus phosphoprotein: characterization of an a-helical domain involved in oligomerization. J Gen Virol 87:159–169
    • (2006) J Gen Virol , vol.87 , pp. 159-169
    • Llorente, M.T.1    Barreno-Garcia, B.2    Calero, M.3    Camafeita, E.4    Lopez, J.A.5    Longhi, S.6    Ferron, F.7    Varela, P.F.8    Melero, J.A.9
  • 97
    • 33846167722 scopus 로고    scopus 로고
    • The nine C-terminal amino acids of the respiratory syncytial virus protein P are necessary and sufficient for binding to ribonucleoprotein complexes in which six ribonucleotides are contacted per N protein protomer
    • COI: 1:CAS:528:DC%2BD2sXmslemug%3D%3D, PID: 17170452
    • Tran TL, Castagne N, Bhella D, Varela PF, Bernard J, Chilmonczyk S, Berkenkamp S, Benhamo V, Grznarova K, Grosclaude J, Nespoulos C, Rey FA, Eleouet JF (2007) The nine C-terminal amino acids of the respiratory syncytial virus protein P are necessary and sufficient for binding to ribonucleoprotein complexes in which six ribonucleotides are contacted per N protein protomer. J Gen Virol 88:196–206
    • (2007) J Gen Virol , vol.88 , pp. 196-206
    • Tran, T.L.1    Castagne, N.2    Bhella, D.3    Varela, P.F.4    Bernard, J.5    Chilmonczyk, S.6    Berkenkamp, S.7    Benhamo, V.8    Grznarova, K.9    Grosclaude, J.10    Nespoulos, C.11    Rey, F.A.12    Eleouet, J.F.13
  • 98
    • 84892688932 scopus 로고    scopus 로고
    • Protein domain definition should allow for conditional disorder
    • COI: 1:CAS:528:DC%2BC3sXhs1eks7%2FN, PID: 23963781
    • Yegambaram K, Bulloch EM, Kingston RL (2013) Protein domain definition should allow for conditional disorder. Protein Sci 22:1502–1518
    • (2013) Protein Sci , vol.22 , pp. 1502-1518
    • Yegambaram, K.1    Bulloch, E.M.2    Kingston, R.L.3
  • 99
    • 84923285656 scopus 로고    scopus 로고
    • Molecular basis for structural heterogeneity of an intrinsically disordered protein bound to a partner by combined ESI-IM-MS and modeling
    • PID: 25510932
    • D’Urzo A, Konijnenberg A, Rossetti G, Habchi J, Li J, Carloni P, Sobott F, Longhi S, Grandori R (2015) Molecular basis for structural heterogeneity of an intrinsically disordered protein bound to a partner by combined ESI-IM-MS and modeling. J Am Soc Mass Spectrom 26:472–481
    • (2015) J Am Soc Mass Spectrom , vol.26 , pp. 472-481
    • D’Urzo, A.1    Konijnenberg, A.2    Rossetti, G.3    Habchi, J.4    Li, J.5    Carloni, P.6    Sobott, F.7    Longhi, S.8    Grandori, R.9
  • 100
    • 84969179536 scopus 로고    scopus 로고
    • Identification and structural characterization of an intermediate in the folding of the measles virus X domain
    • COI: 1:CAS:528:DC%2BC28XnvVamsLc%3D, PID: 27002146
    • Bonetti D, Camilloni C, Visconti L, Longhi S, Brunori M, Vendruscolo M, Gianni S (2016) Identification and structural characterization of an intermediate in the folding of the measles virus X domain. J Biol Chem 291:10886–10892
    • (2016) J Biol Chem , vol.291 , pp. 10886-10892
    • Bonetti, D.1    Camilloni, C.2    Visconti, L.3    Longhi, S.4    Brunori, M.5    Vendruscolo, M.6    Gianni, S.7
  • 101
    • 2542492285 scopus 로고    scopus 로고
    • Phosphoprotein of the rinderpest virus forms a tetramer through a coiled coil region important for biological function. A structural insight
    • COI: 1:CAS:528:DC%2BD2cXkt1Gitbc%3D, PID: 15037604
    • Rahaman A, Srinivasan N, Shamala N, Shaila MS (2004) Phosphoprotein of the rinderpest virus forms a tetramer through a coiled coil region important for biological function. A structural insight. J Biol Chem 279:23606–23614
    • (2004) J Biol Chem , vol.279 , pp. 23606-23614
    • Rahaman, A.1    Srinivasan, N.2    Shamala, N.3    Shaila, M.S.4
  • 102
    • 84902482480 scopus 로고    scopus 로고
    • Coiled-coil deformations in crystal structures: the measles virus phosphoprotein multimerization domain as an illustrative example
    • COI: 1:CAS:528:DC%2BC2cXpsVGgu78%3D, PID: 24914970
    • Blocquel D, Habchi J, Durand E, Sevajol M, Ferron F, Erales J, Papageorgiou N, Longhi S (2014) Coiled-coil deformations in crystal structures: the measles virus phosphoprotein multimerization domain as an illustrative example. Acta Crystallogr D 70:1589–1603
    • (2014) Acta Crystallogr D , vol.70 , pp. 1589-1603
    • Blocquel, D.1    Habchi, J.2    Durand, E.3    Sevajol, M.4    Ferron, F.5    Erales, J.6    Papageorgiou, N.7    Longhi, S.8
  • 103
    • 84880345675 scopus 로고    scopus 로고
    • Structural and functional characterization of the mumps virus phosphoprotein
    • COI: 1:CAS:528:DC%2BC3sXpvFCqtLo%3D, PID: 23637399
    • Cox R, Green TJ, Purushotham S, Deivanayagam C, Bedwell GJ, Prevelige PE, Luo M (2013) Structural and functional characterization of the mumps virus phosphoprotein. J Virol 87:7558–7568
    • (2013) J Virol , vol.87 , pp. 7558-7568
    • Cox, R.1    Green, T.J.2    Purushotham, S.3    Deivanayagam, C.4    Bedwell, G.J.5    Prevelige, P.E.6    Luo, M.7
  • 105
    • 84891886231 scopus 로고    scopus 로고
    • Solution and crystallographic structures of the central region of the phosphoprotein from human metapneumovirus
    • COI: 1:CAS:528:DC%2BC3sXhslGisb7E, PID: 24224051
    • Leyrat C, Renner M, Harlos K, Grimes JM (2013) Solution and crystallographic structures of the central region of the phosphoprotein from human metapneumovirus. PLoS One 8:e80371
    • (2013) PLoS One , vol.8
    • Leyrat, C.1    Renner, M.2    Harlos, K.3    Grimes, J.M.4
  • 106
    • 2942687589 scopus 로고    scopus 로고
    • Biochemical characterization of the respiratory syncytial virus P–P and P–N protein complexes and localization of the P protein oligomerization domain
    • COI: 1:CAS:528:DC%2BD2cXltlGht7s%3D, PID: 15166449
    • Castagne N, Barbier A, Bernard J, Rezaei H, Huet JC, Henry C, Da Costa B, Eleouet JF (2004) Biochemical characterization of the respiratory syncytial virus P–P and P–N protein complexes and localization of the P protein oligomerization domain. J Gen Virol 85:1643–1653
    • (2004) J Gen Virol , vol.85 , pp. 1643-1653
    • Castagne, N.1    Barbier, A.2    Bernard, J.3    Rezaei, H.4    Huet, J.C.5    Henry, C.6    Da Costa, B.7    Eleouet, J.F.8
  • 107
    • 1242283916 scopus 로고    scopus 로고
    • Viral DNA polymerase scanning and the gymnastics of Sendai virus RNA synthesis
    • COI: 1:CAS:528:DC%2BD2cXht1Khurs%3D, PID: 15015496
    • Kolakofsky D, Le Mercier P, Iseni F, Garcin D (2004) Viral DNA polymerase scanning and the gymnastics of Sendai virus RNA synthesis. Virology 318:463–473
    • (2004) Virology , vol.318 , pp. 463-473
    • Kolakofsky, D.1    Le Mercier, P.2    Iseni, F.3    Garcin, D.4
  • 108
    • 47349091097 scopus 로고    scopus 로고
    • Structural properties of the human respiratory syncytial virus P protein: evidence for an elongated homotetrameric molecule that is the smallest orthologue within the family of paramyxovirus polymerase cofactors
    • COI: 1:CAS:528:DC%2BD1cXos1Grur8%3D, PID: 18300250
    • Llorente MT, Taylor IA, Lopez-Vinas E, Gomez-Puertas P, Calder LJ, Garcia-Barreno B, Melero JA (2008) Structural properties of the human respiratory syncytial virus P protein: evidence for an elongated homotetrameric molecule that is the smallest orthologue within the family of paramyxovirus polymerase cofactors. Proteins 72:946–958
    • (2008) Proteins , vol.72 , pp. 946-958
    • Llorente, M.T.1    Taylor, I.A.2    Lopez-Vinas, E.3    Gomez-Puertas, P.4    Calder, L.J.5    Garcia-Barreno, B.6    Melero, J.A.7
  • 109
    • 84928556586 scopus 로고    scopus 로고
    • Ebola virus VP35 interaction with dynein LC8 regulates viral RNA synthesis
    • COI: 1:CAS:528:DC%2BC2MXntFOgu7k%3D, PID: 25741013
    • Luthra P, Jordan DS, Leung DW, Amarasinghe GK, Basler CF (2015) Ebola virus VP35 interaction with dynein LC8 regulates viral RNA synthesis. J Virol 89:5148–5153
    • (2015) J Virol , vol.89 , pp. 5148-5153
    • Luthra, P.1    Jordan, D.S.2    Leung, D.W.3    Amarasinghe, G.K.4    Basler, C.F.5
  • 110
    • 84921960964 scopus 로고    scopus 로고
    • Insights into the coiled-coil organization of the Hendra virus phosphoprotein from combined biochemical and SAXS studies
    • COI: 1:CAS:528:DC%2BC2MXmt12ksg%3D%3D, PID: 25637789
    • Beltrandi M, Blocquel D, Erales J, Barbier P, Cavalli A, Longhi S (2015) Insights into the coiled-coil organization of the Hendra virus phosphoprotein from combined biochemical and SAXS studies. Virology 477:42–55
    • (2015) Virology , vol.477 , pp. 42-55
    • Beltrandi, M.1    Blocquel, D.2    Erales, J.3    Barbier, P.4    Cavalli, A.5    Longhi, S.6
  • 111
    • 84884527950 scopus 로고    scopus 로고
    • Biochemical and structural studies of the oligomerization domain of the Nipah virus phosphoprotein: evidence for an elongated coiled-coil homotrimer
    • COI: 1:CAS:528:DC%2BC3sXhsFensrjP, PID: 24074578
    • Blocquel D, Beltrandi M, Erales J, Barbier P, Longhi S (2013) Biochemical and structural studies of the oligomerization domain of the Nipah virus phosphoprotein: evidence for an elongated coiled-coil homotrimer. Virology 446:162–172
    • (2013) Virology , vol.446 , pp. 162-172
    • Blocquel, D.1    Beltrandi, M.2    Erales, J.3    Barbier, P.4    Longhi, S.5
  • 112
    • 84883807467 scopus 로고    scopus 로고
    • Oligomerization state of the multimerization domain of Nipah virus phosphoprotein
    • COI: 1:CAS:528:DC%2BC3sXht1yhsrzF
    • Salvamani S, Goh Z, Ho K, Tey B, Tan W (2013) Oligomerization state of the multimerization domain of Nipah virus phosphoprotein. Process Biochem 48:1476–1480
    • (2013) Process Biochem , vol.48 , pp. 1476-1480
    • Salvamani, S.1    Goh, Z.2    Ho, K.3    Tey, B.4    Tan, W.5
  • 113
    • 0035182946 scopus 로고    scopus 로고
    • PH-induced folding of an apoptotic coiled coil
    • COI: 1:CAS:528:DC%2BD3MXovVyru7s%3D, PID: 11714921
    • Dutta K, Alexandrov A, Huang H, Pascal SM (2001) pH-induced folding of an apoptotic coiled coil. Protein Sci 10:2531–2540
    • (2001) Protein Sci , vol.10 , pp. 2531-2540
    • Dutta, K.1    Alexandrov, A.2    Huang, H.3    Pascal, S.M.4
  • 114
    • 17444424974 scopus 로고    scopus 로고
    • The structure of alpha-helical coiled coils
    • COI: 1:CAS:528:DC%2BD28Xot1Gkuro%3D, PID: 15837513
    • Lupas AN, Gruber M (2005) The structure of alpha-helical coiled coils. Adv Protein Chem 70:37–78
    • (2005) Adv Protein Chem , vol.70 , pp. 37-78
    • Lupas, A.N.1    Gruber, M.2
  • 115
    • 84870210079 scopus 로고    scopus 로고
    • The native GCN4 leucine-zipper domain does not uniquely specify a dimeric oligomerization state
    • COI: 1:CAS:528:DC%2BC38Xhs1Wjt73M, PID: 23116373
    • Oshaben KM, Salari R, McCaslin DR, Chong LT, Horne WS (2012) The native GCN4 leucine-zipper domain does not uniquely specify a dimeric oligomerization state. Biochemistry 51:9581–9591
    • (2012) Biochemistry , vol.51 , pp. 9581-9591
    • Oshaben, K.M.1    Salari, R.2    McCaslin, D.R.3    Chong, L.T.4    Horne, W.S.5
  • 116
    • 0031968675 scopus 로고    scopus 로고
    • A role for the Sendai virus P protein trimer in RNA synthesis
    • COI: 1:CAS:528:DyaK1cXis1Khs78%3D, PID: 9557717
    • Curran J (1998) A role for the Sendai virus P protein trimer in RNA synthesis. J Virol 72:4274–4280
    • (1998) J Virol , vol.72 , pp. 4274-4280
    • Curran, J.1
  • 117
    • 0028793340 scopus 로고
    • Paramyxovirus phosphoproteins form homotrimers as determined by an epitope dilution assay, via predicted coiled coils
    • COI: 1:CAS:528:DyaK2MXpslOmtL8%3D, PID: 8525609
    • Curran J, Boeck R, Lin-Marq N, Lupas A, Kolakofsky D (1995) Paramyxovirus phosphoproteins form homotrimers as determined by an epitope dilution assay, via predicted coiled coils. Virology 214:139–149
    • (1995) Virology , vol.214 , pp. 139-149
    • Curran, J.1    Boeck, R.2    Lin-Marq, N.3    Lupas, A.4    Kolakofsky, D.5
  • 119
    • 39149113782 scopus 로고    scopus 로고
    • Residues in human respiratory syncytial virus P protein that are essential for its activity on RNA viral synthesis
    • COI: 1:CAS:528:DC%2BD1cXitVOhsbo%3D, PID: 18179840
    • Asenjo A, Mendieta J, Gomez-Puertas P, Villanueva N (2008) Residues in human respiratory syncytial virus P protein that are essential for its activity on RNA viral synthesis. Virus Res 132:160–173
    • (2008) Virus Res , vol.132 , pp. 160-173
    • Asenjo, A.1    Mendieta, J.2    Gomez-Puertas, P.3    Villanueva, N.4
  • 120
    • 33748931498 scopus 로고    scopus 로고
    • Mapping and functional role of the self-association domain of vesicular stomatitis virus phosphoprotein
    • COI: 1:CAS:528:DC%2BD28XhtVWgtrbE, PID: 16973555
    • Chen M, Ogino T, Banerjee AK (2006) Mapping and functional role of the self-association domain of vesicular stomatitis virus phosphoprotein. J Virol 80:9511–9518
    • (2006) J Virol , vol.80 , pp. 9511-9518
    • Chen, M.1    Ogino, T.2    Banerjee, A.K.3
  • 121
    • 0036441132 scopus 로고    scopus 로고
    • Characterization of the oligomerization domain of the phosphoprotein of human parainfluenza virus type 3
    • COI: 1:CAS:528:DC%2BD38XosFWnsLY%3D, PID: 12441081
    • Choudhary SK, Malur AG, Huo Y, De BP, Banerjee AK (2002) Characterization of the oligomerization domain of the phosphoprotein of human parainfluenza virus type 3. Virology 302:373–382
    • (2002) Virology , vol.302 , pp. 373-382
    • Choudhary, S.K.1    Malur, A.G.2    Huo, Y.3    De, B.P.4    Banerjee, A.K.5
  • 122
    • 0034811975 scopus 로고    scopus 로고
    • Functional interaction map of lyssavirus phosphoprotein: identification of the minimal transcription domains
    • COI: 1:CAS:528:DC%2BD3MXnt1GhtLw%3D, PID: 11559793
    • Jacob Y, Real E, Tordo N (2001) Functional interaction map of lyssavirus phosphoprotein: identification of the minimal transcription domains. J Virol 75:9613–9622
    • (2001) J Virol , vol.75 , pp. 9613-9622
    • Jacob, Y.1    Real, E.2    Tordo, N.3
  • 123
    • 0029143791 scopus 로고
    • Expression of the measles virus nucleoprotein gene in Escherichia coli and assembly of nucleocapsid-like structures
    • COI: 1:CAS:528:DyaK2MXns1Cqtb8%3D, PID: 7642091
    • Warnes A, Fooks AR, Dowsett AB, Wilkinson GW, Stephenson JR (1995) Expression of the measles virus nucleoprotein gene in Escherichia coli and assembly of nucleocapsid-like structures. Gene 160:173–178
    • (1995) Gene , vol.160 , pp. 173-178
    • Warnes, A.1    Fooks, A.R.2    Dowsett, A.B.3    Wilkinson, G.W.4    Stephenson, J.R.5
  • 124
    • 2942520968 scopus 로고    scopus 로고
    • Conformational flexibility in recombinant measles virus nucleocapsids visualised by cryo-negative stain electron microscopy and real-space helical reconstruction
    • COI: 1:CAS:528:DC%2BD2cXkvVKmu7w%3D, PID: 15201055
    • Bhella D, Ralph A, Yeo RP (2004) Conformational flexibility in recombinant measles virus nucleocapsids visualised by cryo-negative stain electron microscopy and real-space helical reconstruction. J Mol Biol 340:319–331
    • (2004) J Mol Biol , vol.340 , pp. 319-331
    • Bhella, D.1    Ralph, A.2    Yeo, R.P.3
  • 125
    • 84973438952 scopus 로고    scopus 로고
    • Self-assembly of measles virus nucleocapsid-like particles: kinetics and RNA sequence dependence
    • COI: 1:CAS:528:DC%2BC28Xpt1GqsLo%3D, PID: 27270664
    • Milles S, Jensen MR, Communie G, Maurin D, Schoehn G, Ruigrok RW, Blackledge M (2016) Self-assembly of measles virus nucleocapsid-like particles: kinetics and RNA sequence dependence. Angew Chem Int Ed Engl 55:9356–9360
    • (2016) Angew Chem Int Ed Engl , vol.55 , pp. 9356-9360
    • Milles, S.1    Jensen, M.R.2    Communie, G.3    Maurin, D.4    Schoehn, G.5    Ruigrok, R.W.6    Blackledge, M.7
  • 126
    • 77958027714 scopus 로고    scopus 로고
    • Structural disorder within Sendai virus nucleoprotein and phosphoprotein: insight into the structural basis of molecular recognition
    • COI: 1:CAS:528:DC%2BC3cXpsFeitro%3D, PID: 20450486
    • Jensen MR, Bernado P, Houben K, Blanchard L, Marion D, Ruigrok RW, Blackledge M (2010) Structural disorder within Sendai virus nucleoprotein and phosphoprotein: insight into the structural basis of molecular recognition. Protein Pept Lett 17:952–960
    • (2010) Protein Pept Lett , vol.17 , pp. 952-960
    • Jensen, M.R.1    Bernado, P.2    Houben, K.3    Blanchard, L.4    Marion, D.5    Ruigrok, R.W.6    Blackledge, M.7
  • 128
    • 0018847901 scopus 로고
    • Conformation of the helical nucleocapsids of paramyxoviruses and vesicular stomatitis virus: reversible coiling and uncoiling induced by changes in salt concentration
    • COI: 1:CAS:528:DyaL3cXksVSjs7c%3D, PID: 6248857
    • Heggeness MH, Scheid A, Choppin PW (1980) Conformation of the helical nucleocapsids of paramyxoviruses and vesicular stomatitis virus: reversible coiling and uncoiling induced by changes in salt concentration. Proc Natl Acad Sci USA 77:2631–2635
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 2631-2635
    • Heggeness, M.H.1    Scheid, A.2    Choppin, P.W.3
  • 129
    • 0019501692 scopus 로고
    • The relationship of conformational changes in the Sendai virus nucleocapsid to proteolytic cleavage of the NP polypeptide
    • COI: 1:CAS:528:DyaL3MXmtFOntrY%3D, PID: 6270887
    • Heggeness MH, Scheid A, Choppin PW (1981) The relationship of conformational changes in the Sendai virus nucleocapsid to proteolytic cleavage of the NP polypeptide. Virology 114:555–562
    • (1981) Virology , vol.114 , pp. 555-562
    • Heggeness, M.H.1    Scheid, A.2    Choppin, P.W.3
  • 131
    • 0029926011 scopus 로고    scopus 로고
    • Domains of the measles virus N protein required for binding to P protein and self-assembly
    • COI: 1:CAS:528:DyaK28XpsVCiuw%3D%3D, PID: 8615002
    • Bankamp B, Horikami SM, Thompson PD, Huber M, Billeter M, Moyer SA (1996) Domains of the measles virus N protein required for binding to P protein and self-assembly. Virology 216:272–277
    • (1996) Virology , vol.216 , pp. 272-277
    • Bankamp, B.1    Horikami, S.M.2    Thompson, P.D.3    Huber, M.4    Billeter, M.5    Moyer, S.A.6
  • 132
    • 0031055574 scopus 로고    scopus 로고
    • Protein interaction domains of the measles virus nucleocapsid protein (NP)
    • COI: 1:CAS:528:DyaK2sXisVWmsrc%3D
    • Liston P, Batal R, DiFlumeri C, Briedis DJ (1997) Protein interaction domains of the measles virus nucleocapsid protein (NP). Adv Virol 142:305–321
    • (1997) Adv Virol , vol.142 , pp. 305-321
    • Liston, P.1    Batal, R.2    DiFlumeri, C.3    Briedis, D.J.4
  • 133
    • 84928923069 scopus 로고    scopus 로고
    • Structure of the paramyxovirus parainfluenza virus 5 nucleoprotein–RNA complex
    • COI: 1:CAS:528:DC%2BC2MXkvFaqur8%3D, PID: 25831513
    • Alayyoubi M, Leser GP, Kors CA, Lamb RA (2015) Structure of the paramyxovirus parainfluenza virus 5 nucleoprotein–RNA complex. Proc Natl Acad Sci USA 112:E1792–E1799
    • (2015) Proc Natl Acad Sci USA , vol.112 , pp. E1792-E1799
    • Alayyoubi, M.1    Leser, G.P.2    Kors, C.A.3    Lamb, R.A.4
  • 137
    • 84937712896 scopus 로고    scopus 로고
    • Initiation and regulation of paramyxovirus transcription and replication
    • PID: 25683441
    • Noton SL, Fearns R (2015) Initiation and regulation of paramyxovirus transcription and replication. Virology 479–480:545–554
    • (2015) Virology , vol.479-480 , pp. 545-554
    • Noton, S.L.1    Fearns, R.2
  • 138
    • 84908077925 scopus 로고    scopus 로고
    • Structural studies on the authentic mumps virus nucleocapsid showing uncoiling by the phosphoprotein
    • COI: 1:CAS:528:DC%2BC2cXhs1yhtLfF, PID: 25288750
    • Cox R, Pickar A, Qiu S, Tsao J, Rodenburg C, Dokland T, Elson A, He B, Luo M (2014) Structural studies on the authentic mumps virus nucleocapsid showing uncoiling by the phosphoprotein. Proc Natl Acad Sci USA 111:15208–15213
    • (2014) Proc Natl Acad Sci USA , vol.111 , pp. 15208-15213
    • Cox, R.1    Pickar, A.2    Qiu, S.3    Tsao, J.4    Rodenburg, C.5    Dokland, T.6    Elson, A.7    He, B.8    Luo, M.9
  • 139
    • 84885065793 scopus 로고    scopus 로고
    • Multiscaled exploration of coupled folding and binding of an intrinsically disordered molecular recognition element in measles virus nucleoprotein
    • COI: 1:CAS:528:DC%2BC3sXhs1SqurzM, PID: 24043820
    • Wang Y, Chu X, Longhi S, Roche P, Han W, Wang E, Wang J (2013) Multiscaled exploration of coupled folding and binding of an intrinsically disordered molecular recognition element in measles virus nucleoprotein. Proc Natl Acad Sci USA 110:E3743–E3752
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. E3743-E3752
    • Wang, Y.1    Chu, X.2    Longhi, S.3    Roche, P.4    Han, W.5    Wang, E.6    Wang, J.7
  • 140
    • 33751289801 scopus 로고    scopus 로고
    • Assessing induced folding of an intrinsically disordered protein by site-directed spin-labeling EPR spectroscopy
    • COI: 1:CAS:528:DC%2BD28Xpsleisb8%3D, PID: 17034249
    • Morin B, Bourhis JM, Belle V, Woudstra M, Carrière F, Guigliarelli B, Fournel A, Longhi S (2006) Assessing induced folding of an intrinsically disordered protein by site-directed spin-labeling EPR spectroscopy. J Phys Chem B 110:20596–20608
    • (2006) J Phys Chem B , vol.110 , pp. 20596-20608
    • Morin, B.1    Bourhis, J.M.2    Belle, V.3    Woudstra, M.4    Carrière, F.5    Guigliarelli, B.6    Fournel, A.7    Longhi, S.8
  • 141
    • 58149279796 scopus 로고    scopus 로고
    • Mapping alpha-helical induced folding within the intrinsically disordered C-terminal domain of the measles virus nucleoprotein by site-directed spin-labeling EPR spectroscopy
    • COI: 1:CAS:528:DC%2BD1cXhsVCls7nI
    • Belle V, Rouger S, Costanzo S, Liquiere E, Strancar J, Guigliarelli B, Fournel A, Longhi S (2008) Mapping alpha-helical induced folding within the intrinsically disordered C-terminal domain of the measles virus nucleoprotein by site-directed spin-labeling EPR spectroscopy. Proteins Struct Funct Bioinform 73:973–988
    • (2008) Proteins Struct Funct Bioinform , vol.73 , pp. 973-988
    • Belle, V.1    Rouger, S.2    Costanzo, S.3    Liquiere, E.4    Strancar, J.5    Guigliarelli, B.6    Fournel, A.7    Longhi, S.8
  • 142
    • 45749102885 scopus 로고    scopus 로고
    • Quantitative conformational analysis of partially folded proteins from residual dipolar couplings: application to the molecular recognition element of Sendai virus nucleoprotein
    • COI: 1:CAS:528:DC%2BD1cXmsVelsbg%3D, PID: 18507376
    • Jensen MR, Houben K, Lescop E, Blanchard L, Ruigrok RW, Blackledge M (2008) Quantitative conformational analysis of partially folded proteins from residual dipolar couplings: application to the molecular recognition element of Sendai virus nucleoprotein. J Am Chem Soc 130:8055–8061
    • (2008) J Am Chem Soc , vol.130 , pp. 8055-8061
    • Jensen, M.R.1    Houben, K.2    Lescop, E.3    Blanchard, L.4    Ruigrok, R.W.5    Blackledge, M.6
  • 143
    • 0024972479 scopus 로고
    • Capping and alpha-helix stability
    • COI: 1:CAS:528:DyaK3cXhvVaitw%3D%3D, PID: 2812029
    • Serrano L, Fersht AR (1989) Capping and alpha-helix stability. Nature 342:296–299
    • (1989) Nature , vol.342 , pp. 296-299
    • Serrano, L.1    Fersht, A.R.2
  • 144
    • 82655175457 scopus 로고    scopus 로고
    • Compaction and binding properties of the intrinsically disordered C-terminal domain of Henipavirus nucleoprotein as unveiled by deletion studies
    • COI: 1:CAS:528:DC%2BC3MXhsFKgs7zO, PID: 22108848
    • Blocquel D, Habchi J, Gruet A, Blangy S, Longhi S (2012) Compaction and binding properties of the intrinsically disordered C-terminal domain of Henipavirus nucleoprotein as unveiled by deletion studies. Mol BioSyst 8:392–410
    • (2012) Mol BioSyst , vol.8 , pp. 392-410
    • Blocquel, D.1    Habchi, J.2    Gruet, A.3    Blangy, S.4    Longhi, S.5
  • 145
    • 67650045816 scopus 로고    scopus 로고
    • Limitations of induced folding in molecular recognition by intrinsically disordered proteins
    • COI: 1:CAS:528:DC%2BD1MXptVGhuro%3D, PID: 19462392
    • Hazy E, Tompa P (2009) Limitations of induced folding in molecular recognition by intrinsically disordered proteins. ChemPhysChem 10:1415–1419
    • (2009) ChemPhysChem , vol.10 , pp. 1415-1419
    • Hazy, E.1    Tompa, P.2
  • 146
    • 84879206318 scopus 로고    scopus 로고
    • Assessing induced folding within the intrinsically disordered C-terminal domain of the Henipavirus nucleoproteins by site directed spin labeling EPR spectroscopy
    • COI: 1:CAS:528:DC%2BC3sXlslWmuro%3D, PID: 22881220
    • Martinho M, Habchi J, El Habre Z, Nesme L, Guigliarelli B, Belle V, Longhi S (2013) Assessing induced folding within the intrinsically disordered C-terminal domain of the Henipavirus nucleoproteins by site directed spin labeling EPR spectroscopy. J Biomol Struct Dyn 31:453–471
    • (2013) J Biomol Struct Dyn , vol.31 , pp. 453-471
    • Martinho, M.1    Habchi, J.2    El Habre, Z.3    Nesme, L.4    Guigliarelli, B.5    Belle, V.6    Longhi, S.7
  • 147
    • 84920758588 scopus 로고    scopus 로고
    • Dynamics of the intrinsically disordered C-terminal domain of the Nipah virus nucleoprotein and interaction with the X domain of the phosphoprotein as unveiled by NMR spectroscopy
    • COI: 1:CAS:528:DC%2BC2cXitVCks7vF, PID: 25492314
    • Baronti L, Erales J, Habchi J, Felli IC, Pierattelli R, Longhi S (2015) Dynamics of the intrinsically disordered C-terminal domain of the Nipah virus nucleoprotein and interaction with the X domain of the phosphoprotein as unveiled by NMR spectroscopy. ChemBioChem 16:268–276
    • (2015) ChemBioChem , vol.16 , pp. 268-276
    • Baronti, L.1    Erales, J.2    Habchi, J.3    Felli, I.C.4    Pierattelli, R.5    Longhi, S.6
  • 148
    • 84925346923 scopus 로고    scopus 로고
    • Demonstration of a folding after binding mechanism in the recognition between the measles virus NTAIL and X domains
    • COI: 1:CAS:528:DC%2BC2cXitFCrs7%2FP, PID: 25511246
    • Dosnon M, Bonetti D, Morrone A, Erales J, di Silvio E, Longhi S, Gianni S (2015) Demonstration of a folding after binding mechanism in the recognition between the measles virus NTAIL and X domains. ACS Chem Biol 10:795–802
    • (2015) ACS Chem Biol , vol.10 , pp. 795-802
    • Dosnon, M.1    Bonetti, D.2    Morrone, A.3    Erales, J.4    di Silvio, E.5    Longhi, S.6    Gianni, S.7
  • 149
    • 23644449725 scopus 로고    scopus 로고
    • The intrinsically disordered C-terminal domain of the measles virus nucleoprotein interacts with the C-terminal domain of the phosphoprotein via two distinct sites and remains predominantly unfolded
    • COI: 1:CAS:528:DC%2BD2MXntVejtr4%3D, PID: 16046624
    • Bourhis JM, Receveur-Bréchot V, Oglesbee M, Zhang X, Buccellato M, Darbon H, Canard B, Finet S, Longhi S (2005) The intrinsically disordered C-terminal domain of the measles virus nucleoprotein interacts with the C-terminal domain of the phosphoprotein via two distinct sites and remains predominantly unfolded. Protein Sci 14:1975–1992
    • (2005) Protein Sci , vol.14 , pp. 1975-1992
    • Bourhis, J.M.1    Receveur-Bréchot, V.2    Oglesbee, M.3    Zhang, X.4    Buccellato, M.5    Darbon, H.6    Canard, B.7    Finet, S.8    Longhi, S.9
  • 151
    • 84930216174 scopus 로고    scopus 로고
    • Insights into the Hendra virus NTAIL-XD complex: evidence for a parallel organization of the helical MoRE at the XD surface stabilized by a combination of hydrophobic and polar interactions
    • COI: 1:CAS:528:DC%2BC2MXot1Wltbg%3D
    • Erales J, Beltrandi M, Roche J, Maté M, Longhi S (2015) Insights into the Hendra virus NTAIL-XD complex: evidence for a parallel organization of the helical MoRE at the XD surface stabilized by a combination of hydrophobic and polar interactions. Biochim Biopys Acta 1854:1038–1053
    • (2015) Biochim Biopys Acta , vol.1854 , pp. 1038-1053
    • Erales, J.1    Beltrandi, M.2    Roche, J.3    Maté, M.4    Longhi, S.5
  • 152
    • 65249099497 scopus 로고    scopus 로고
    • Fundamental aspects of protein–protein association kinetics
    • COI: 1:CAS:528:DC%2BD1MXhsFWns7w%3D, PID: 19196002
    • Schreiber G, Haran G, Zhou HX (2009) Fundamental aspects of protein–protein association kinetics. Chem Rev 109:839–860
    • (2009) Chem Rev , vol.109 , pp. 839-860
    • Schreiber, G.1    Haran, G.2    Zhou, H.X.3
  • 153
    • 84908155664 scopus 로고    scopus 로고
    • Role of electrostatic interactions in binding of peptides and intrinsically disordered proteins to their folded targets. 1. NMR and MD characterization of the complex between the c-Crk N-SH3 domain and the peptide Sos
    • COI: 1:CAS:528:DC%2BC2cXhsFahtLrF, PID: 25207671
    • Xue Y, Yuwen T, Zhu F, Skrynnikov NR (2014) Role of electrostatic interactions in binding of peptides and intrinsically disordered proteins to their folded targets. 1. NMR and MD characterization of the complex between the c-Crk N-SH3 domain and the peptide Sos. Biochemistry 53:6473–6495
    • (2014) Biochemistry , vol.53 , pp. 6473-6495
    • Xue, Y.1    Yuwen, T.2    Zhu, F.3    Skrynnikov, N.R.4
  • 154
    • 34547943482 scopus 로고    scopus 로고
    • Molecular principles of the interactions of disordered proteins
    • COI: 1:CAS:528:DC%2BD2sXpsFagtLg%3D, PID: 17681540
    • Meszaros B, Tompa P, Simon I, Dosztanyi Z (2007) Molecular principles of the interactions of disordered proteins. J Mol Biol 372:549–561
    • (2007) J Mol Biol , vol.372 , pp. 549-561
    • Meszaros, B.1    Tompa, P.2    Simon, I.3    Dosztanyi, Z.4
  • 155
    • 0001450617 scopus 로고    scopus 로고
    • Protein folding: binding of conformationally fluctuating building blocks via population selection
    • COI: 1:CAS:528:DC%2BD3MXovVKgsbw%3D, PID: 11724155
    • Tsai CD, Ma B, Kumar S, Wolfson H, Nussinov R (2001) Protein folding: binding of conformationally fluctuating building blocks via population selection. Crit Rev Biochem Mol Biol 36:399–433
    • (2001) Crit Rev Biochem Mol Biol , vol.36 , pp. 399-433
    • Tsai, C.D.1    Ma, B.2    Kumar, S.3    Wolfson, H.4    Nussinov, R.5
  • 157
    • 0034255123 scopus 로고    scopus 로고
    • Speeding molecular recognition by using the folding funnel: the fly-casting mechanism
    • COI: 1:CAS:528:DC%2BD3cXls12ltLY%3D, PID: 10908673
    • Shoemaker BA, Portman JJ, Wolynes PG (2000) Speeding molecular recognition by using the folding funnel: the fly-casting mechanism. Proc Natl Acad Sci USA 97:8868–8873
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 8868-8873
    • Shoemaker, B.A.1    Portman, J.J.2    Wolynes, P.G.3
  • 158
    • 84898953700 scopus 로고    scopus 로고
    • Distinguishing induced fit from conformational selection
    • COI: 1:CAS:528:DC%2BC2cXmvVWltb0%3D, PID: 24747333
    • Gianni S, Dogan J, Jemth P (2014) Distinguishing induced fit from conformational selection. Biophys Chem 189:33–39
    • (2014) Biophys Chem , vol.189 , pp. 33-39
    • Gianni, S.1    Dogan, J.2    Jemth, P.3
  • 159
    • 84921835922 scopus 로고    scopus 로고
    • Visualizing the molecular recognition trajectory of an intrinsically disordered protein using multinuclear relaxation dispersion NMR
    • COI: 1:CAS:528:DC%2BC2MXhsFGqtg%3D%3D, PID: 25551399
    • Schneider R, Maurin D, Communie G, Kragelj J, Hansen DF, Ruigrok RW, Jensen MR, Blackledge M (2015) Visualizing the molecular recognition trajectory of an intrinsically disordered protein using multinuclear relaxation dispersion NMR. J Am Chem Soc 137:1220–1229
    • (2015) J Am Chem Soc , vol.137 , pp. 1220-1229
    • Schneider, R.1    Maurin, D.2    Communie, G.3    Kragelj, J.4    Hansen, D.F.5    Ruigrok, R.W.6    Jensen, M.R.7    Blackledge, M.8
  • 160
    • 58149215982 scopus 로고    scopus 로고
    • Fuzzy interactome: the limitations of models in molecular biology
    • COI: 1:CAS:528:DC%2BD1MXktl2gtg%3D%3D
    • Fuxreiter M, Tompa P (2009) Fuzzy interactome: the limitations of models in molecular biology. Trends Biochem Sci 34:3
    • (2009) Trends Biochem Sci , vol.34 , pp. 3
    • Fuxreiter, M.1    Tompa, P.2
  • 161
    • 82655180384 scopus 로고    scopus 로고
    • Fuzziness: linking regulation to protein dynamics
    • COI: 1:CAS:528:DC%2BC3MXhsFKgs73F, PID: 21927770
    • Fuxreiter M (2012) Fuzziness: linking regulation to protein dynamics. Mol BioSyst 8:168–177
    • (2012) Mol BioSyst , vol.8 , pp. 168-177
    • Fuxreiter, M.1
  • 162
    • 84859499620 scopus 로고    scopus 로고
    • The measles virus N(TAIL)-XD complex: an illustrative example of fuzziness
    • COI: 1:CAS:528:DC%2BC38XhtlynsbvL, PID: 22399322
    • Longhi S (2012) The measles virus N(TAIL)-XD complex: an illustrative example of fuzziness. Adv Exp Med Biol 725:126–141
    • (2012) Adv Exp Med Biol , vol.725 , pp. 126-141
    • Longhi, S.1
  • 166
    • 0036337962 scopus 로고    scopus 로고
    • Identification and characterization of a regulatory domain on the carboxyl terminus of the measles virus nucleocapsid protein
    • COI: 1:CAS:528:DC%2BD38Xmt1erurk%3D, PID: 12163594
    • Zhang X, Glendening C, Linke H, Parks CL, Brooks C, Udem SA, Oglesbee M (2002) Identification and characterization of a regulatory domain on the carboxyl terminus of the measles virus nucleocapsid protein. J Virol 76:8737–8746
    • (2002) J Virol , vol.76 , pp. 8737-8746
    • Zhang, X.1    Glendening, C.2    Linke, H.3    Parks, C.L.4    Brooks, C.5    Udem, S.A.6    Oglesbee, M.7
  • 167
    • 33644781718 scopus 로고    scopus 로고
    • A single codon in the nucleocapsid protein C terminus contributes to in vitro and in vivo fitness of Edmonston measles virus
    • COI: 1:CAS:528:DC%2BD28Xis1Cqtro%3D, PID: 16501099
    • Carsillo T, Zhang X, Vasconcelos D, Niewiesk S, Oglesbee M (2006) A single codon in the nucleocapsid protein C terminus contributes to in vitro and in vivo fitness of Edmonston measles virus. J Virol 80:2904–2912
    • (2006) J Virol , vol.80 , pp. 2904-2912
    • Carsillo, T.1    Zhang, X.2    Vasconcelos, D.3    Niewiesk, S.4    Oglesbee, M.5
  • 168
    • 66249143804 scopus 로고    scopus 로고
    • Nucleocapsid protein interactions with the major inducible heat shock protein
    • Longhi S, (ed), Nova Publishers Inc., Hauppage
    • Oglesbee M (2007) Nucleocapsid protein interactions with the major inducible heat shock protein. In: Longhi S (ed) Measles virus nucleoprotein. Nova Publishers Inc., Hauppage, pp 53–98
    • (2007) Measles virus nucleoprotein , pp. 53-98
    • Oglesbee, M.1
  • 169
    • 33750716581 scopus 로고    scopus 로고
    • Hsp72, a host determinant of measles virus neurovirulence
    • COI: 1:CAS:528:DC%2BD28Xht1KhurrP, PID: 16971451
    • Carsillo T, Traylor Z, Choi C, Niewiesk S, Oglesbee M (2006) hsp72, a host determinant of measles virus neurovirulence. J Virol 80:11031–11039
    • (2006) J Virol , vol.80 , pp. 11031-11039
    • Carsillo, T.1    Traylor, Z.2    Choi, C.3    Niewiesk, S.4    Oglesbee, M.5
  • 171
    • 84886895251 scopus 로고    scopus 로고
    • Phosphorylation of measles virus nucleoprotein affects viral growth by changing gene expression and genomic RNA stability
    • COI: 1:CAS:528:DC%2BC3sXhs1Kjt7nL, PID: 23966404
    • Sugai A, Sato H, Yoneda M, Kai C (2013) Phosphorylation of measles virus nucleoprotein affects viral growth by changing gene expression and genomic RNA stability. J Virol 87:11684–11692
    • (2013) J Virol , vol.87 , pp. 11684-11692
    • Sugai, A.1    Sato, H.2    Yoneda, M.3    Kai, C.4
  • 172
    • 80051740915 scopus 로고    scopus 로고
    • Determination of a phosphorylation site in Nipah virus nucleoprotein and its involvement in virus transcription
    • COI: 1:CAS:528:DC%2BC3MXhtF2htrrL, PID: 21613447
    • Huang M, Sato H, Hagiwara K, Watanabe A, Sugai A, Ikeda F, Kozuka-Hata H, Oyama M, Yoneda M, Kai C (2011) Determination of a phosphorylation site in Nipah virus nucleoprotein and its involvement in virus transcription. J Gen Virol 92:2133–2141
    • (2011) J Gen Virol , vol.92 , pp. 2133-2141
    • Huang, M.1    Sato, H.2    Hagiwara, K.3    Watanabe, A.4    Sugai, A.5    Ikeda, F.6    Kozuka-Hata, H.7    Oyama, M.8    Yoneda, M.9    Kai, C.10
  • 173
    • 84883289774 scopus 로고    scopus 로고
    • Dissecting partner recognition by an intrinsically disordered protein using descriptive random mutagenesis
    • COI: 1:CAS:528:DC%2BC3sXhtFOntr3L, PID: 23811056
    • Gruet A, Dosnon M, Vassena A, Lombard V, Gerlier D, Bignon C, Longhi S (2013) Dissecting partner recognition by an intrinsically disordered protein using descriptive random mutagenesis. J Mol Biol 425:3495–3509
    • (2013) J Mol Biol , vol.425 , pp. 3495-3509
    • Gruet, A.1    Dosnon, M.2    Vassena, A.3    Lombard, V.4    Gerlier, D.5    Bignon, C.6    Longhi, S.7
  • 175
    • 67650872991 scopus 로고    scopus 로고
    • Structure of the vesicular stomatitis virus nucleocapsid in complex with the nucleocapsid-binding domain of the small polymerase cofactor, P
    • COI: 1:CAS:528:DC%2BD1MXptVWhurs%3D, PID: 19571006
    • Green TJ, Luo M (2009) Structure of the vesicular stomatitis virus nucleocapsid in complex with the nucleocapsid-binding domain of the small polymerase cofactor, P. Proc Natl Acad Sci USA 106:11713–11718
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 11713-11718
    • Green, T.J.1    Luo, M.2
  • 176
    • 0025358461 scopus 로고
    • Interaction of canine distemper virus nucleocapsid variants with 70K heat-shock proteins
    • COI: 1:CAS:528:DyaK3cXkvFCnurY%3D, PID: 2374009
    • Oglesbee M, Ringler S, Krakowka S (1990) Interaction of canine distemper virus nucleocapsid variants with 70K heat-shock proteins. J Gen Virol 71:1585–1590
    • (1990) J Gen Virol , vol.71 , pp. 1585-1590
    • Oglesbee, M.1    Ringler, S.2    Krakowka, S.3
  • 177
    • 0024430009 scopus 로고
    • Isolation and characterization of canine distemper virus nucleocapsid variants
    • COI: 1:CAS:528:DyaL1MXlslSku7s%3D, PID: 2778437
    • Oglesbee M, Tatalick L, Rice J, Krakowka S (1989) Isolation and characterization of canine distemper virus nucleocapsid variants. J Gen Virol 70(Pt 9):2409–2419
    • (1989) J Gen Virol , vol.70 , pp. 2409-2419
    • Oglesbee, M.1    Tatalick, L.2    Rice, J.3    Krakowka, S.4
  • 178
    • 84859498913 scopus 로고    scopus 로고
    • Plasticity in structural and functional interactions between the phosphoprotein and nucleoprotein of measles virus
    • COI: 1:CAS:528:DC%2BC38XltVyksrs%3D, PID: 22318731
    • Shu Y, Habchi J, Costanzo S, Padilla A, Brunel J, Gerlier D, Oglesbee M, Longhi S (2012) Plasticity in structural and functional interactions between the phosphoprotein and nucleoprotein of measles virus. J Biol Chem 287:11951–11967
    • (2012) J Biol Chem , vol.287 , pp. 11951-11967
    • Shu, Y.1    Habchi, J.2    Costanzo, S.3    Padilla, A.4    Brunel, J.5    Gerlier, D.6    Oglesbee, M.7    Longhi, S.8
  • 180
    • 84868672577 scopus 로고    scopus 로고
    • Analysis of the relationships between evolvability, thermodynamics, and the functions of intrinsically disordered proteins/regions
    • COI: 1:CAS:528:DC%2BC38XhslOlt7zE, PID: 23153654
    • Huang H, Sarai A (2012) Analysis of the relationships between evolvability, thermodynamics, and the functions of intrinsically disordered proteins/regions. Comput Biol Chem 41:51–57
    • (2012) Comput Biol Chem , vol.41 , pp. 51-57
    • Huang, H.1    Sarai, A.2
  • 181
    • 84992738137 scopus 로고    scopus 로고
    • The Ebola virus VP30-NP interaction is a regulator of viral RNA synthesis
    • PID: 27755595
    • Kirchdoerfer RN, Moyer CL, Abelson DM, Saphire EO (2016) The Ebola virus VP30-NP interaction is a regulator of viral RNA synthesis. PLoS Pathog 12:e1005937
    • (2016) PLoS Pathog , vol.12
    • Kirchdoerfer, R.N.1    Moyer, C.L.2    Abelson, D.M.3    Saphire, E.O.4
  • 182
    • 33745325007 scopus 로고    scopus 로고
    • Mechanisms of drug inhibition of signalling molecules
    • COI: 1:CAS:528:DC%2BD28XkvVyrsrg%3D, PID: 16724058
    • Sebolt-Leopold JS, English JM (2006) Mechanisms of drug inhibition of signalling molecules. Nature 441:457–462
    • (2006) Nature , vol.441 , pp. 457-462
    • Sebolt-Leopold, J.S.1    English, J.M.2
  • 183
    • 42149181885 scopus 로고    scopus 로고
    • Structural diversity of G protein-coupled receptors and significance for drug discovery
    • PID: 18382464
    • Lagerstrom MC, Schioth HB (2008) Structural diversity of G protein-coupled receptors and significance for drug discovery. Nat Rev Drug Discov 7:339–357
    • (2008) Nat Rev Drug Discov , vol.7 , pp. 339-357
    • Lagerstrom, M.C.1    Schioth, H.B.2
  • 184
    • 37649000332 scopus 로고    scopus 로고
    • Protein protein interaction inhibition (2P2I) combining high throughput and virtual screening: application to the HIV-1 Nef protein
    • COI: 1:CAS:528:DC%2BD1cXisVKqsA%3D%3D, PID: 18042718
    • Betzi S, Restouin A, Opi S, Arold ST, Parrot I, Guerlesquin F, Morelli X, Collette Y (2007) Protein protein interaction inhibition (2P2I) combining high throughput and virtual screening: application to the HIV-1 Nef protein. Proc Natl Acad Sci USA 104:19256–19261
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 19256-19261
    • Betzi, S.1    Restouin, A.2    Opi, S.3    Arold, S.T.4    Parrot, I.5    Guerlesquin, F.6    Morelli, X.7    Collette, Y.8
  • 185
    • 84931267273 scopus 로고    scopus 로고
    • The paramyxovirus polymerase complex as a target for next-generation anti-paramyxovirus therapeutics
    • PID: 26029193
    • Cox R, Plemper RK (2015) The paramyxovirus polymerase complex as a target for next-generation anti-paramyxovirus therapeutics. Front Microbiol 6:459
    • (2015) Front Microbiol , vol.6 , pp. 459
    • Cox, R.1    Plemper, R.K.2
  • 187
    • 77954992237 scopus 로고    scopus 로고
    • Targeting intrinsically disordered proteins in neurodegenerative and protein dysfunction diseases: another illustration of the D(2) concept
    • COI: 1:CAS:528:DC%2BC3cXpsVahsrg%3D, PID: 20653509
    • Uversky VN (2010) Targeting intrinsically disordered proteins in neurodegenerative and protein dysfunction diseases: another illustration of the D(2) concept. Expert Rev Proteomics 7:543–564
    • (2010) Expert Rev Proteomics , vol.7 , pp. 543-564
    • Uversky, V.N.1
  • 188
    • 78149497463 scopus 로고    scopus 로고
    • Drugs for ‘protein clouds’: targeting intrinsically disordered transcription factors
    • COI: 1:CAS:528:DC%2BC3cXhsVals7vK, PID: 20889377
    • Dunker AK, Uversky VN (2010) Drugs for ‘protein clouds’: targeting intrinsically disordered transcription factors. Curr Opin Pharmacol 10:782–788
    • (2010) Curr Opin Pharmacol , vol.10 , pp. 782-788
    • Dunker, A.K.1    Uversky, V.N.2
  • 190
    • 84861512163 scopus 로고    scopus 로고
    • Intrinsically disordered proteins and novel strategies for drug discovery
    • COI: 1:CAS:528:DC%2BC38Xns1SrtL4%3D, PID: 22559227
    • Uversky VN (2012) Intrinsically disordered proteins and novel strategies for drug discovery. Expert Opin Drug Discov 7:475–488
    • (2012) Expert Opin Drug Discov , vol.7 , pp. 475-488
    • Uversky, V.N.1
  • 191
    • 84927645757 scopus 로고    scopus 로고
    • Identification of inhibitors of biological interactions involving intrinsically disordered proteins
    • COI: 1:CAS:528:DC%2BC2MXotFKjtrg%3D, PID: 25849651
    • Marasco D, Scognamiglio PL (2015) Identification of inhibitors of biological interactions involving intrinsically disordered proteins. Int J Mol Sci 16:7394–7412
    • (2015) Int J Mol Sci , vol.16 , pp. 7394-7412
    • Marasco, D.1    Scognamiglio, P.L.2
  • 192
    • 84942155226 scopus 로고    scopus 로고
    • Druggability of intrinsically disordered proteins
    • COI: 1:CAS:528:DC%2BC2sXmvVaru7k%3D, PID: 26387110
    • Joshi P, Vendruscolo M (2015) Druggability of intrinsically disordered proteins. Adv Exp Med Biol 870:383–400
    • (2015) Adv Exp Med Biol , vol.870 , pp. 383-400
    • Joshi, P.1    Vendruscolo, M.2
  • 193
    • 0003187567 scopus 로고    scopus 로고
    • The atomic structure of protein–protein recognition sites
    • COI: 1:STN:280:DyaK1M7is1Gntg%3D%3D, PID: 9925793
    • Lo Conte L, Chothia C, Janin J (1999) The atomic structure of protein–protein recognition sites. J Mol Biol 285:2177–2198
    • (1999) J Mol Biol , vol.285 , pp. 2177-2198
    • Lo Conte, L.1    Chothia, C.2    Janin, J.3
  • 194
    • 4143107222 scopus 로고    scopus 로고
    • Analysis of ordered and disordered protein complexes reveals structural features discriminating between stable and unstable monomers
    • COI: 1:CAS:528:DC%2BD2cXmsVCrtb8%3D, PID: 15321724
    • Gunasekaran K, Tsai CJ, Nussinov R (2004) Analysis of ordered and disordered protein complexes reveals structural features discriminating between stable and unstable monomers. J Mol Biol 341:1327–1341
    • (2004) J Mol Biol , vol.341 , pp. 1327-1341
    • Gunasekaran, K.1    Tsai, C.J.2    Nussinov, R.3
  • 195
    • 7944239221 scopus 로고    scopus 로고
    • Targeting the p53-MDM2 interaction to treat cancer
    • COI: 1:CAS:528:DC%2BD2cXotlCktbo%3D, PID: 15452548
    • Klein C, Vassilev LT (2004) Targeting the p53-MDM2 interaction to treat cancer. Br J Cancer 91:1415–1419
    • (2004) Br J Cancer , vol.91 , pp. 1415-1419
    • Klein, C.1    Vassilev, L.T.2
  • 196
    • 4344610526 scopus 로고    scopus 로고
    • Small-molecule antagonists of p53-MDM2 binding: research tools and potential therapeutics
    • COI: 1:CAS:528:DC%2BD2cXhtVSisrfI, PID: 15004525
    • Vassilev LT (2004) Small-molecule antagonists of p53-MDM2 binding: research tools and potential therapeutics. Cell Cycle 3:419–421
    • (2004) Cell Cycle , vol.3 , pp. 419-421
    • Vassilev, L.T.1
  • 199
    • 84983741973 scopus 로고    scopus 로고
    • A sting in the tail: the N-terminal domain of the androgen receptor as a drug target
    • COI: 1:CAS:528:DC%2BC28XhvFaksbjN, PID: 27212126
    • Monaghan AE, McEwan IJ (2016) A sting in the tail: the N-terminal domain of the androgen receptor as a drug target. Asian J Androl 18:687–694
    • (2016) Asian J Androl , vol.18 , pp. 687-694
    • Monaghan, A.E.1    McEwan, I.J.2
  • 200
    • 77950867698 scopus 로고    scopus 로고
    • The subunit interfaces of weakly associated homodimeric proteins
    • COI: 1:CAS:528:DC%2BC3cXktlCrt78%3D, PID: 20156457
    • Dey S, Pal A, Chakrabarti P, Janin J (2010) The subunit interfaces of weakly associated homodimeric proteins. J Mol Biol 398:146–160
    • (2010) J Mol Biol , vol.398 , pp. 146-160
    • Dey, S.1    Pal, A.2    Chakrabarti, P.3    Janin, J.4
  • 201
    • 77949743743 scopus 로고    scopus 로고
    • Atomic analysis of protein–protein interfaces with known inhibitors: the 2P2I database
    • PID: 20231898
    • Bourgeas R, Basse MJ, Morelli X, Roche P (2010) Atomic analysis of protein–protein interfaces with known inhibitors: the 2P2I database. PLoS One 5:e9598
    • (2010) PLoS One , vol.5
    • Bourgeas, R.1    Basse, M.J.2    Morelli, X.3    Roche, P.4
  • 203
    • 25144472591 scopus 로고    scopus 로고
    • Showing your ID: intrinsic disorder as an ID for recognition, regulation and cell signaling
    • COI: 1:CAS:528:DC%2BD2MXhtVCgt73F, PID: 16094605
    • Uversky VN, Oldfield CJ, Dunker AK (2005) Showing your ID: intrinsic disorder as an ID for recognition, regulation and cell signaling. J Mol Recognit 18:343–384
    • (2005) J Mol Recognit , vol.18 , pp. 343-384
    • Uversky, V.N.1    Oldfield, C.J.2    Dunker, A.K.3
  • 205
    • 33746561940 scopus 로고    scopus 로고
    • Morbillivirus nucleoprotein possesses a novel nuclear localization signal and a CRM1-independent nuclear export signal
    • COI: 1:CAS:528:DC%2BD28Xot1Wqs7Y%3D, PID: 16716375
    • Sato H, Masuda M, Miura R, Yoneda M, Kai C (2006) Morbillivirus nucleoprotein possesses a novel nuclear localization signal and a CRM1-independent nuclear export signal. Virology 352:121–130
    • (2006) Virology , vol.352 , pp. 121-130
    • Sato, H.1    Masuda, M.2    Miura, R.3    Yoneda, M.4    Kai, C.5
  • 206
    • 70349737884 scopus 로고    scopus 로고
    • The matrix protein of measles virus regulates viral RNA synthesis and assembly by interacting with the nucleocapsid protein
    • COI: 1:CAS:528:DC%2BD1MXhtlClsbnM, PID: 19656884
    • Iwasaki M, Takeda M, Shirogane Y, Nakatsu Y, Nakamura T, Yanagi Y (2009) The matrix protein of measles virus regulates viral RNA synthesis and assembly by interacting with the nucleocapsid protein. J Virol 83:10374–10383
    • (2009) J Virol , vol.83 , pp. 10374-10383
    • Iwasaki, M.1    Takeda, M.2    Shirogane, Y.3    Nakatsu, Y.4    Nakamura, T.5    Yanagi, Y.6
  • 207
    • 79551698035 scopus 로고    scopus 로고
    • Peroxiredoxin 1 is required for efficient transcription and replication of measles virus
    • COI: 1:CAS:528:DC%2BC3MXhtVWlt7fE, PID: 21159870
    • Watanabe A, Yoneda M, Ikeda F, Sugai A, Sato H, Kai C (2011) Peroxiredoxin 1 is required for efficient transcription and replication of measles virus. J Virol 85:2247–2253
    • (2011) J Virol , vol.85 , pp. 2247-2253
    • Watanabe, A.1    Yoneda, M.2    Ikeda, F.3    Sugai, A.4    Sato, H.5    Kai, C.6
  • 208
    • 0033569626 scopus 로고    scopus 로고
    • Involvement of actin microfilaments in the transcription/replication of human parainfluenza virus type 3: possible role of actin in other viruses
    • COI: 1:STN:280:DyaK1MvlsVOltQ%3D%3D, PID: 10523790
    • De BP, Banerjee AK (1999) Involvement of actin microfilaments in the transcription/replication of human parainfluenza virus type 3: possible role of actin in other viruses. Microsc Res Tech 47:114–123
    • (1999) Microsc Res Tech , vol.47 , pp. 114-123
    • De, B.P.1    Banerjee, A.K.2
  • 209
    • 0025356092 scopus 로고
    • Host cell proteins required for measles virus reproduction
    • COI: 1:CAS:528:DyaK3cXitFCmurc%3D, PID: 2324707
    • Moyer SA, Baker SC, Horikami SM (1990) Host cell proteins required for measles virus reproduction. J Gen Virol 71:775–783
    • (1990) J Gen Virol , vol.71 , pp. 775-783
    • Moyer, S.A.1    Baker, S.C.2    Horikami, S.M.3
  • 210
    • 0036199090 scopus 로고    scopus 로고
    • Recognition of the measles virus nucleocapsid as a mechanism of IRF-3 activation
    • COI: 1:CAS:528:DC%2BD38XisVynu7o%3D, PID: 11907205
    • tenOever BR, Servant MJ, Grandvaux N, Lin R, Hiscott J (2002) Recognition of the measles virus nucleocapsid as a mechanism of IRF-3 activation. J Virol 76:3659–3669
    • (2002) J Virol , vol.76 , pp. 3659-3669
    • tenOever, B.R.1    Servant, M.J.2    Grandvaux, N.3    Lin, R.4    Hiscott, J.5
  • 212
    • 20044387229 scopus 로고    scopus 로고
    • Measles virus nucleoprotein induces cell proliferation arrest and apoptosis through NTAIL/NR and NCORE/FcgRIIB1 interactions, respectively
    • COI: 1:CAS:528:DC%2BD2MXlsFensL4%3D, PID: 15914856
    • Laine D, Bourhis J, Longhi S, Flacher M, Cassard L, Canard B, Sautès-Fridman C, Rabourdin-Combe C, Valentin H (2005) Measles virus nucleoprotein induces cell proliferation arrest and apoptosis through NTAIL/NR and NCORE/FcgRIIB1 interactions, respectively. J Gen Virol 86:1771–1784
    • (2005) J Gen Virol , vol.86 , pp. 1771-1784
    • Laine, D.1    Bourhis, J.2    Longhi, S.3    Flacher, M.4    Cassard, L.5    Canard, B.6    Sautès-Fridman, C.7    Rabourdin-Combe, C.8    Valentin, H.9
  • 213
    • 10744224344 scopus 로고    scopus 로고
    • Measles virus nucleoprotein binds to a novel cell surface receptor distinct from FcgRII via its C-terminal domain: role in MV-induced immunosuppression
    • COI: 1:CAS:528:DC%2BD3sXosFSjtL0%3D, PID: 14557619
    • Laine D, Trescol-Biémont M, Longhi S, Libeau G, Marie J, Vidalain P, Azocar O, Diallo A, Canard B, Rabourdin-Combe C, Valentin H (2003) Measles virus nucleoprotein binds to a novel cell surface receptor distinct from FcgRII via its C-terminal domain: role in MV-induced immunosuppression. J Virol 77:11332–11346
    • (2003) J Virol , vol.77 , pp. 11332-11346
    • Laine, D.1    Trescol-Biémont, M.2    Longhi, S.3    Libeau, G.4    Marie, J.5    Vidalain, P.6    Azocar, O.7    Diallo, A.8    Canard, B.9    Rabourdin-Combe, C.10    Valentin, H.11
  • 214
    • 0345059128 scopus 로고    scopus 로고
    • Measles virus protein interactions in yeast: new findings and caveats
    • COI: 1:CAS:528:DC%2BD3sXptlOruro%3D, PID: 14659559
    • Chen M, Cortay JC, Gerlier D (2003) Measles virus protein interactions in yeast: new findings and caveats. Virus Res 98:123–129
    • (2003) Virus Res , vol.98 , pp. 123-129
    • Chen, M.1    Cortay, J.C.2    Gerlier, D.3
  • 215
    • 84882821864 scopus 로고    scopus 로고
    • The measles virus phosphoprotein interacts with the linker domain of STAT1
    • COI: 1:CAS:528:DC%2BC3sXhtFSmurvF, PID: 23856440
    • Devaux P, Priniski L, Cattaneo R (2013) The measles virus phosphoprotein interacts with the linker domain of STAT1. Virology 444:250–256
    • (2013) Virology , vol.444 , pp. 250-256
    • Devaux, P.1    Priniski, L.2    Cattaneo, R.3
  • 216
    • 0028895953 scopus 로고
    • An N-terminal domain of the Sendai paramyxovirus P protein acts as a chaperone for the NP protein during the nascent chain assembly step of genome replication
    • COI: 1:CAS:528:DyaK2MXjtlGqsLg%3D, PID: 7815552
    • Curran J, Marq JB, Kolakofsky D (1995) An N-terminal domain of the Sendai paramyxovirus P protein acts as a chaperone for the NP protein during the nascent chain assembly step of genome replication. J Virol 69:849–855
    • (1995) J Virol , vol.69 , pp. 849-855
    • Curran, J.1    Marq, J.B.2    Kolakofsky, D.3
  • 217
    • 0031922323 scopus 로고    scopus 로고
    • The activity of Sendai virus genomic and antigenomic promoters requires a second element past the leader template regions: a motif (GNNNNN)3 is essential for replication
    • COI: 1:CAS:528:DyaK1cXhvVOjtLY%3D, PID: 9525637
    • Tapparel C, Maurice D, Roux L (1998) The activity of Sendai virus genomic and antigenomic promoters requires a second element past the leader template regions: a motif (GNNNNN)3 is essential for replication. J Virol 72:3117–3128
    • (1998) J Virol , vol.72 , pp. 3117-3128
    • Tapparel, C.1    Maurice, D.2    Roux, L.3
  • 219
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm
    • COI: 1:CAS:528:DyaK1MXms12rtbw%3D, PID: 10550212
    • Wright PE, Dyson HJ (1999) Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm. J Mol Biol 293:321–331
    • (1999) J Mol Biol , vol.293 , pp. 321-331
    • Wright, P.E.1    Dyson, H.J.2
  • 220
    • 0034867975 scopus 로고    scopus 로고
    • The protein trinity–linking function and disorder
    • COI: 1:CAS:528:DC%2BD3MXmvVWrtLc%3D, PID: 11533628
    • Dunker AK, Obradovic Z (2001) The protein trinity–linking function and disorder. Nat Biotechnol 19:805–806
    • (2001) Nat Biotechnol , vol.19 , pp. 805-806
    • Dunker, A.K.1    Obradovic, Z.2
  • 221
    • 0036402827 scopus 로고    scopus 로고
    • Identification and functions of usefully disordered proteins
    • COI: 1:CAS:528:DC%2BD38XpsVeqsrc%3D, PID: 12418100
    • Dunker AK, Brown CJ, Obradovic Z (2002) Identification and functions of usefully disordered proteins. Adv Protein Chem 62:25–49
    • (2002) Adv Protein Chem , vol.62 , pp. 25-49
    • Dunker, A.K.1    Brown, C.J.2    Obradovic, Z.3
  • 222
    • 29244465452 scopus 로고    scopus 로고
    • Biophysical properties of the synucleins and their propensities to fibrillate: inhibition of alpha-synuclein assembly by beta- and gamma- synucleins
    • Uversky VN, Li J, Souillac P, Jakes R, Goedert M, Fink AL (2002) Biophysical properties of the synucleins and their propensities to fibrillate: inhibition of alpha-synuclein assembly by beta- and gamma- synucleins. J Biol Chem 25:25
    • (2002) J Biol Chem , vol.25 , pp. 25
    • Uversky, V.N.1    Li, J.2    Souillac, P.3    Jakes, R.4    Goedert, M.5    Fink, A.L.6
  • 223
    • 0037309985 scopus 로고    scopus 로고
    • Extended disordered proteins: targeting function with less scaffold
    • COI: 1:CAS:528:DC%2BD3sXptlyhuw%3D%3D, PID: 12575995
    • Gunasekaran K, Tsai CJ, Kumar S, Zanuy D, Nussinov R (2003) Extended disordered proteins: targeting function with less scaffold. Trends Biochem Sci 28:81–85
    • (2003) Trends Biochem Sci , vol.28 , pp. 81-85
    • Gunasekaran, K.1    Tsai, C.J.2    Kumar, S.3    Zanuy, D.4    Nussinov, R.5
  • 224
    • 13844255387 scopus 로고    scopus 로고
    • Natively unfolded proteins
    • COI: 1:CAS:528:DC%2BD2MXhsFSht7o%3D, PID: 15718131
    • Fink AL (2005) Natively unfolded proteins. Curr Opin Struct Biol 15:35–41
    • (2005) Curr Opin Struct Biol , vol.15 , pp. 35-41
    • Fink, A.L.1
  • 225
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • COI: 1:CAS:528:DC%2BD2MXhslSlsLo%3D, PID: 15738986
    • Dyson HJ, Wright PE (2005) Intrinsically unstructured proteins and their functions. Nat Rev Mol Cell Biol 6:197–208
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 226
    • 84861327457 scopus 로고    scopus 로고
    • Interactions via intrinsically disordered regions: what kind of motifs?
    • COI: 1:CAS:528:DC%2BC38XmtVKrt7s%3D, PID: 22535488
    • Pancsa R, Fuxreiter M (2012) Interactions via intrinsically disordered regions: what kind of motifs? IUBMB Life 64:513–520
    • (2012) IUBMB Life , vol.64 , pp. 513-520
    • Pancsa, R.1    Fuxreiter, M.2
  • 227
    • 0033972445 scopus 로고    scopus 로고
    • Molecular evolution of the Paramyxoviridae and Rhabdoviridae multiple-protein-encoding P gene
    • COI: 1:CAS:528:DC%2BD3cXot1Sjsg%3D%3D, PID: 10666708
    • Jordan IK, Sutter BA, McClure MA (2000) Molecular evolution of the Paramyxoviridae and Rhabdoviridae multiple-protein-encoding P gene. Mol Biol Evol 17:75–86
    • (2000) Mol Biol Evol , vol.17 , pp. 75-86
    • Jordan, I.K.1    Sutter, B.A.2    McClure, M.A.3
  • 228
    • 18144431290 scopus 로고    scopus 로고
    • Overlapping reading frames in closely related human papillomaviruses result in modular rates of selection within E2
    • COI: 1:CAS:528:DC%2BD2MXjvFSktro%3D, PID: 15831941
    • Narechania A, Terai M, Burk RD (2005) Overlapping reading frames in closely related human papillomaviruses result in modular rates of selection within E2. J Gen Virol 86:1307–1313
    • (2005) J Gen Virol , vol.86 , pp. 1307-1313
    • Narechania, A.1    Terai, M.2    Burk, R.D.3
  • 229
    • 70349737853 scopus 로고    scopus 로고
    • Overlapping genes produce proteins with unusual sequence properties and offer insight into de novo protein creation
    • COI: 1:CAS:528:DC%2BD1MXhtlCltr7O, PID: 19640978
    • Rancurel C, Khosravi M, Dunker KA, Romero PR, Karlin D (2009) Overlapping genes produce proteins with unusual sequence properties and offer insight into de novo protein creation. J Virol 83:10719–10736
    • (2009) J Virol , vol.83 , pp. 10719-10736
    • Rancurel, C.1    Khosravi, M.2    Dunker, K.A.3    Romero, P.R.4    Karlin, D.5
  • 230
    • 77950421789 scopus 로고    scopus 로고
    • Dual coding in alternative reading frames correlates with intrinsic protein disorder
    • COI: 1:CAS:528:DC%2BC3cXktFKhsrY%3D, PID: 20212158
    • Kovacs E, Tompa P, Liliom K, Kalmar L (2010) Dual coding in alternative reading frames correlates with intrinsic protein disorder. Proc Natl Acad Sci USA 107:5429–5434
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 5429-5434
    • Kovacs, E.1    Tompa, P.2    Liliom, K.3    Kalmar, L.4
  • 231
    • 29244470521 scopus 로고    scopus 로고
    • Structural disorder within the replicative complex of measles virus: functional implications
    • COI: 1:CAS:528:DC%2BD2MXhtlCqtbvN, PID: 16364741
    • Bourhis JM, Canard B, Longhi S (2006) Structural disorder within the replicative complex of measles virus: functional implications. Virology 344:94–110
    • (2006) Virology , vol.344 , pp. 94-110
    • Bourhis, J.M.1    Canard, B.2    Longhi, S.3
  • 234
    • 77958103698 scopus 로고    scopus 로고
    • Viral disorder or disordered viruses: do viral proteins possess unique features?
    • COI: 1:CAS:528:DC%2BC3cXpsFeitr0%3D, PID: 20450483
    • Xue B, Williams RW, Oldfield CJ, Goh GK, Dunker AK, Uversky VN (2010) Viral disorder or disordered viruses: do viral proteins possess unique features? Protein Pept Lett 17:932–951
    • (2010) Protein Pept Lett , vol.17 , pp. 932-951
    • Xue, B.1    Williams, R.W.2    Oldfield, C.J.3    Goh, G.K.4    Dunker, A.K.5    Uversky, V.N.6
  • 236
    • 40849122470 scopus 로고    scopus 로고
    • The PyMOL molecular graphics system
    • DeLano WL (2002) The PyMOL molecular graphics system. Proteins Struct Funct Bioinform 30:442–454
    • (2002) Proteins Struct Funct Bioinform , vol.30 , pp. 442-454
    • DeLano, W.L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.