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Volumn 28, Issue 6, 2011, Pages 1203-1210

The C-terminus of ICln is natively disordered but displays local structural preformation

Author keywords

ICln; Intrinsic disorder; NMR; Structure

Indexed keywords

CELL PROTEIN; PROTEIN ICLN; UNCLASSIFIED DRUG;

EID: 83755206931     PISSN: 10158987     EISSN: 14219778     Source Type: Journal    
DOI: 10.1159/000335852     Document Type: Article
Times cited : (8)

References (49)
  • 3
    • 0032080214 scopus 로고    scopus 로고
    • PICln binds to a mammalian homolog of a yeast protein involved in regulation of cell morphology
    • DOI 10.1074/jbc.273.18.10811
    • Krapivinsky G, Pu W, Wickman K, Krapivinsky L, Clapham DE: pICln binds to a mammalian homolog of a yeast protein involved in regulation of cell morphology. J Biol Chem 1998;273:10811-10814. (Pubitemid 28204911)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.18 , pp. 10811-10814
    • Krapivinsky, G.1    Pu, W.2    Wickman, K.3    Krapivinsky, L.4    Clapham, D.E.5
  • 6
    • 58549105917 scopus 로고    scopus 로고
    • Compartmentalization regulates the interaction between the platelet integrin alpha IIb beta 3 and ICln
    • Larkin D, Treumann A, Murphy D, DeChaumont C, Kiernan A, Moran N: Compartmentalization regulates the interaction between the platelet integrin alpha IIb beta 3 and ICln. Br J Haematol 2009;144:580-590.
    • (2009) Br J Haematol , vol.144 , pp. 580-590
    • Larkin, D.1    Treumann, A.2    Murphy, D.3    Dechaumont, C.4    Kiernan, A.5    Moran, N.6
  • 8
    • 0035846546 scopus 로고    scopus 로고
    • Methylation of Sm proteins by a complex containing PRMT5 and the putative U snRNP assembly factor pICln
    • DOI 10.1016/S0960-9822(01)00592-9
    • Meister G, Eggert C, Buhler D, Brahms H, Kambach C, Fischer U: Methylation of Sm proteins by a complex containing PRMT5 and the putative U snRNP assembly factor pICln. Curr Biol 2001;11:1990-1994. (Pubitemid 33146428)
    • (2001) Current Biology , vol.11 , Issue.24 , pp. 1990-1994
    • Meister, G.1    Eggert, C.2    Buhler, D.3    Brahms, H.4    Kambach, C.5    Fischer, U.6
  • 10
    • 0034724675 scopus 로고    scopus 로고
    • ICln is essential for cellular and early embryonic viability
    • DOI 10.1074/jbc.275.17.12363
    • Pu WT, Wickman K, Clapham DE: ICln is essential for cellular and early embryonic viability. J Biol Chem 2000;275:12363-12366. (Pubitemid 30241374)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.17 , pp. 12363-12366
    • Pu, W.T.1    Wickman, K.2    Clapham, D.E.3
  • 12
    • 0028144541 scopus 로고
    • Molecular characterization of a swellinginduced chloride conductance regulatory protein, pICln
    • Krapivinsky GB, Ackerman MJ, Gordon EA, Krapivinsky LD, Clapham DE: Molecular characterization of a swellinginduced chloride conductance regulatory protein, pICln. Cell 1994;76:439-448.
    • (1994) Cell , vol.76 , pp. 439-448
    • Krapivinsky, G.B.1    Ackerman, M.J.2    Gordon, E.A.3    Krapivinsky, L.D.4    Clapham, D.E.5
  • 13
    • 0030725583 scopus 로고    scopus 로고
    • Molecular cloning and expression of a chloride channel-associated protein pICln in human young red blood cells: Association with actin
    • Schwartz RS, Rybicki AC, Nagel RL: Molecular cloning and expression of a chloride channel-associated protein pICln in human young red blood cells: Association with actin. Biochem J 1997;327:609-616.
    • (1997) Biochem J , vol.327 , pp. 609-616
    • Schwartz, R.S.1    Rybicki, A.C.2    Nagel, R.L.3
  • 16
    • 0032529271 scopus 로고    scopus 로고
    • The 30-kD domain of protein 4.1 mediates its binding to the carboxyl terminus of pICln, a protein involved in cellular volume regulation
    • Tang CJ, Tang TK: The 30-kD domain of protein 4.1 mediates its binding to the carboxyl terminus of pICln, a protein involved in cellular volume regulation. Blood 1998;92:1442-1447. (Pubitemid 28369059)
    • (1998) Blood , vol.92 , Issue.4 , pp. 1442-1447
    • Tang, C.-J.C.1    Tang, T.K.2
  • 18
    • 0032537951 scopus 로고    scopus 로고
    • Characterization of pI(Cln) binding proteins: Identification of p17 and assessment of the role of acidic domains in mediating protein-protein interactions
    • DOI 10.1016/S0167-4889(98)00073-1, PII S0167488998000731
    • Emma F, Sanchez-Olea R, Strange K: Characterization of pI(Cln) binding proteins: Identification of p17 and assessment of the role of acidic domains in mediating protein-protein interactions. Biochim Biophys Acta 1998;1404:321-328. (Pubitemid 28470534)
    • (1998) Biochimica et Biophysica Acta - Molecular Cell Research , vol.1404 , Issue.3 , pp. 321-328
    • Emma, F.1    Sanchez-Olea, R.2    Strange, K.3
  • 29
    • 0028267319 scopus 로고
    • Expression vectors for affinity purification and radiolabeling of proteins using Escherichia coli as host
    • DOI 10.1016/0378-1119(94)90525-8
    • Chen BP, Hai T: Expression vectors for affinity purification and radiolabeling of proteins using Escherichia coli as host. Gene 1994;139:73-75. (Pubitemid 24086741)
    • (1994) Gene , vol.139 , Issue.1 , pp. 73-75
    • Chen, B.P.C.1    Hai, T.2
  • 32
    • 34249765651 scopus 로고
    • NMR View: A computer program for the visualization and analysis of NMR data
    • Johnson BA, Blevins RA: NMR View: A computer program for the visualization and analysis of NMR data. J Biomol NMR 1994;4:603-614.
    • (1994) J Biomol NMR , vol.4 , pp. 603-614
    • Johnson, B.A.1    Blevins, R.A.2
  • 33
    • 70449534683 scopus 로고    scopus 로고
    • The protein meta-structure: A novel concept for chemical and molecular biology
    • Konrat R: The protein meta-structure: A novel concept for chemical and molecular biology. Cell Mol Life Sci 2009;66:3625-3639.
    • (2009) Cell Mol Life Sci , vol.66 , pp. 3625-3639
    • Konrat, R.1
  • 36
    • 0021678506 scopus 로고
    • Anomalous behavior of bovine alpha(s1)- and -caseins on gel electrophoresis in sodium dodecyl sulfate buffers
    • DOI 10.1016/0003-9861(84)90295-9
    • Creamer LK, Richardson T: Anomalous behavior of bovine alpha s1-and betacaseins on gel electrophoresis in sodium dodecyl sulfate buffers. Arch Biochem Biophys 1984;234:476-486. (Pubitemid 15189102)
    • (1984) Archives of Biochemistry and Biophysics , vol.234 , Issue.2 , pp. 476-486
    • Creamer, L.K.1    Richardson, T.2
  • 38
    • 34548750953 scopus 로고    scopus 로고
    • Natively unstructured regions in proteins identified from contact predictions
    • DOI 10.1093/bioinformatics/btm349
    • Schlessinger A, Punta M, Rost B: Natively unstructured regions in proteins identified from contact predictions. Bioinformatics 2007;23:2376-2384. (Pubitemid 47423834)
    • (2007) Bioinformatics , vol.23 , Issue.18 , pp. 2376-2384
    • Schlessinger, A.1    Punta, M.2    Rost, B.3
  • 40
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • DOI 10.1038/nrm1589
    • Dyson HJ, Wright PE: Intrinsically unstructured proteins and their functions. Nat Rev Mol Cell Biol 2005;6:197-208. (Pubitemid 40314921)
    • (2005) Nature Reviews Molecular Cell Biology , vol.6 , Issue.3 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 41
    • 69949105161 scopus 로고    scopus 로고
    • The rules of disorder or why disorder rules
    • Gsponer J, Madan Babu M: The rules of disorder or why disorder rules. Prog Biophys Mol Biol 2009;99:94-103.
    • (2009) Prog Biophys Mol Biol , vol.99 , pp. 94-103
    • Gsponer, J.1    Madan Babu, M.2
  • 44
    • 24044538903 scopus 로고    scopus 로고
    • IUPred: Web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content
    • DOI 10.1093/bioinformatics/bti541
    • Dosztanyi Z, Csizmok V, Tompa P, Simon I: IUPred: Web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content. Bioinformatics 2005;21:3433-3434. (Pubitemid 41222453)
    • (2005) Bioinformatics , vol.21 , Issue.16 , pp. 3433-3434
    • Dosztanyi, Z.1    Csizmok, V.2    Tompa, P.3    Simon, I.4
  • 45
    • 0036468397 scopus 로고    scopus 로고
    • Coupling of folding and binding for unstructured proteins
    • DOI 10.1016/S0959-440X(02)00289-0
    • Dyson HJ, Wright PE: Coupling of folding and binding for unstructured proteins. Curr Opin Struct Biol 2002;12:54-60. (Pubitemid 34142721)
    • (2002) Current Opinion in Structural Biology , vol.12 , Issue.1 , pp. 54-60
    • Dyson, H.J.1    Wright, P.E.2
  • 46
    • 0035805117 scopus 로고    scopus 로고
    • The structure of the -catenin/E-cadherin complex and the molecular basis of diverse ligand recognition by -catenin
    • DOI 10.1016/S0092-8674(01)00330-0
    • Huber AH, Weis WI: The structure of the beta-catenin/E-cadherin complex and the molecular basis of diverse ligand recognition by beta-catenin. Cell 2001;105:391-402. (Pubitemid 32455345)
    • (2001) Cell , vol.105 , Issue.3 , pp. 391-402
    • Huber, A.H.1    Weis, W.I.2
  • 47
    • 21444431780 scopus 로고    scopus 로고
    • Phosphorylation regulates the activity of the SMN complex during assembly of spliceosomal U snRNPs
    • DOI 10.1038/sj.embor.7400301
    • Grimmler M, Bauer L, Nousiainen M, Korner R, Meister G, Fischer U: Phosphorylation regulates the activity of the SMN complex during assembly of spliceosomal U snRNPs. EMBO Rep 2005;6:70-76. (Pubitemid 41710077)
    • (2005) EMBO Reports , vol.6 , Issue.1 , pp. 70-76
    • Grimmler, M.1    Bauer, L.2    Nousiainen, M.3    Korner, R.4    Meister, G.5    Fischer, U.6
  • 48
    • 0032485963 scopus 로고    scopus 로고
    • Characterization of pI(Cln) phosphorylation state and a pI(Cln)-associated protein kinase
    • DOI 10.1016/S0304-4165(98)00009-9, PII S0304416598000099
    • Sanchez-Olea R, Emma F, Coghlan M, Strange K: Characterization of pICln phosphorylation state and a pIClnassociated protein kinase. Biochim Biophys Acta 1998;1381:49-60. (Pubitemid 28248115)
    • (1998) Biochimica et Biophysica Acta - General Subjects , vol.1381 , Issue.1 , pp. 49-60
    • Sanchez-Olea, R.1    Emma, F.2    Coghlan, M.3    Strange, K.4
  • 49
    • 44949272730 scopus 로고
    • A time-efficient, linear-space local similarity algorithm
    • Huang X, Miller W: A time-efficient, linear-space local similarity algorithm. Adv Appl Math 1991;12:337-357.
    • (1991) Adv Appl Math , vol.12 , pp. 337-357
    • Huang, X.1    Miller, W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.