-
1
-
-
77951213476
-
Increased monomerization of mutant HSPB1 leads to protein hyperactivity in Charcot-Marie-Tooth neuropathy
-
COI: 1:CAS:528:DC%2BC3cXkvVGju74%3D, PID: 20178975
-
Almeida-Souza L et al (2010) Increased monomerization of mutant HSPB1 leads to protein hyperactivity in Charcot-Marie-Tooth neuropathy. J Biol Chem 285:12778–12786. doi:10.1074/jbc.M109.082644
-
(2010)
J Biol Chem
, vol.285
, pp. 12778-12786
-
-
Almeida-Souza, L.1
-
2
-
-
9644268864
-
Mechanism and function of deubiquitinating enzymes
-
COI: 1:CAS:528:DC%2BD2cXhtVantbzF, PID: 15571815
-
Amerik AY, Hochstrasser M (2004) Mechanism and function of deubiquitinating enzymes. Biochim Biophys Acta 1695:189–207. doi:10.1016/j.bbamcr.2004.10.003
-
(2004)
Biochim Biophys Acta
, vol.1695
, pp. 189-207
-
-
Amerik, A.Y.1
Hochstrasser, M.2
-
3
-
-
70149097520
-
Crystal structures of alpha-crystallin domain dimers of alphaB-crystallin and Hsp20
-
COI: 1:CAS:528:DC%2BD1MXhtFKnt77L, PID: 19646995
-
Bagneris C, Bateman OA, Naylor CE, Cronin N, Boelens WC, Keep NH, Slingsby C (2009) Crystal structures of alpha-crystallin domain dimers of alphaB-crystallin and Hsp20. J Mol Biol 392:1242–1252. doi:10.1016/j.jmb.2009.07.069
-
(2009)
J Mol Biol
, vol.392
, pp. 1242-1252
-
-
Bagneris, C.1
Bateman, O.A.2
Naylor, C.E.3
Cronin, N.4
Boelens, W.C.5
Keep, N.H.6
Slingsby, C.7
-
4
-
-
79960698253
-
Three-dimensional structure of alpha-crystallin domain dimers of human small heat shock proteins HSPB1 and HSPB6
-
COI: 1:CAS:528:DC%2BC3MXpt1Oqurk%3D, PID: 21641913
-
Baranova EV, Weeks SD, Beelen S, Bukach OV, Gusev NB, Strelkov SV (2011) Three-dimensional structure of alpha-crystallin domain dimers of human small heat shock proteins HSPB1 and HSPB6. J Mol Biol 411:110–122. doi:10.1016/j.jmb.2011.05.024
-
(2011)
J Mol Biol
, vol.411
, pp. 110-122
-
-
Baranova, E.V.1
Weeks, S.D.2
Beelen, S.3
Bukach, O.V.4
Gusev, N.B.5
Strelkov, S.V.6
-
5
-
-
84858003372
-
Small heat shock proteins and alpha-crystallins: dynamic proteins with flexible functions
-
COI: 1:CAS:528:DC%2BC38XjsFOnsrY%3D, PID: 22177323
-
Basha E, O’Neill H, Vierling E (2012) Small heat shock proteins and alpha-crystallins: dynamic proteins with flexible functions. Trends Biochem Sci 37:106–117. doi:10.1016/j.tibs.2011.11.005
-
(2012)
Trends Biochem Sci
, vol.37
, pp. 106-117
-
-
Basha, E.1
O’Neill, H.2
Vierling, E.3
-
6
-
-
0024500879
-
Interaction of Drosophila 27,000 Mr heat-shock protein with the nucleus of heat-shocked and ecdysone-stimulated culture cells
-
PID: 2777913
-
Beaulieu JF, Arrigo AP, Tanguay RM (1989) Interaction of Drosophila 27,000 Mr heat-shock protein with the nucleus of heat-shocked and ecdysone-stimulated culture cells. J Cell Sci 92(Pt 1):29–36
-
(1989)
J Cell Sci
, vol.92
, pp. 29-36
-
-
Beaulieu, J.F.1
Arrigo, A.P.2
Tanguay, R.M.3
-
7
-
-
84921856085
-
Neuropathy- and myopathy-associated mutations in human small heat shock proteins: characteristics and evolutionary history of the mutation sites
-
PID: 24607769
-
Benndorf R, Martin JL, Kosakovsky Pond SL, Wertheim JO (2014) Neuropathy- and myopathy-associated mutations in human small heat shock proteins: characteristics and evolutionary history of the mutation sites. Mutat Res Rev Mutat Res. doi:10.1016/j.mrrev.2014.02.004
-
(2014)
Mutat Res Rev Mutat Res
-
-
Benndorf, R.1
Martin, J.L.2
Kosakovsky Pond, S.L.3
Wertheim, J.O.4
-
8
-
-
0037039153
-
The alphaA-crystallin R116C mutant has a higher affinity for forming heteroaggregates with alphaB-crystallin
-
COI: 1:CAS:528:DC%2BD3MXovFSltb8%3D, PID: 11772029
-
Bera S, Abraham EC (2002) The alphaA-crystallin R116C mutant has a higher affinity for forming heteroaggregates with alphaB-crystallin. Biochemistry 41:297–305
-
(2002)
Biochemistry
, vol.41
, pp. 297-305
-
-
Bera, S.1
Abraham, E.C.2
-
9
-
-
0037108280
-
A positive charge preservation at position 116 of alpha A-crystallin is critical for its structural and functional integrity
-
COI: 1:CAS:528:DC%2BD38Xns1Sntb8%3D, PID: 12369832
-
Bera S, Thampi P, Cho WJ, Abraham EC (2002) A positive charge preservation at position 116 of alpha A-crystallin is critical for its structural and functional integrity. Biochemistry 41:12421–12426
-
(2002)
Biochemistry
, vol.41
, pp. 12421-12426
-
-
Bera, S.1
Thampi, P.2
Cho, W.J.3
Abraham, E.C.4
-
10
-
-
84904815625
-
SWISS-MODEL: modelling protein tertiary and quaternary structure using evolutionary information
-
COI: 1:CAS:528:DC%2BC2cXhtFCqs73I, PID: 24782522
-
Biasini M et al (2014) SWISS-MODEL: modelling protein tertiary and quaternary structure using evolutionary information. Nucleic Acids Res 42:W252–W258. doi:10.1093/nar/gku340
-
(2014)
Nucleic Acids Res
, vol.42
, pp. W252-W258
-
-
Biasini, M.1
-
11
-
-
84864486839
-
The family of mammalian small heat shock proteins (HSPBs): implications in protein deposit diseases and motor neuropathies
-
COI: 1:CAS:528:DC%2BC38XlsFGiurs%3D, PID: 22484489
-
Boncoraglio A, Minoia M, Carra S (2012) The family of mammalian small heat shock proteins (HSPBs): implications in protein deposit diseases and motor neuropathies. Int J Biochem Cell Biol 44:1657–1669. doi:10.1016/j.biocel.2012.03.011
-
(2012)
Int J Biochem Cell Biol
, vol.44
, pp. 1657-1669
-
-
Boncoraglio, A.1
Minoia, M.2
Carra, S.3
-
12
-
-
0030613769
-
Subunit exchange of alphaA-crystallin
-
COI: 1:CAS:528:DyaK2sXnsFWgur0%3D, PID: 9368012
-
Bova MP, Ding LL, Horwitz J, Fung BK (1997) Subunit exchange of alphaA-crystallin. J Biol Chem 272:29511–29517
-
(1997)
J Biol Chem
, vol.272
, pp. 29511-29517
-
-
Bova, M.P.1
Ding, L.L.2
Horwitz, J.3
Fung, B.K.4
-
13
-
-
0032586878
-
Mutation R120G in alphaB-crystallin, which is linked to a desmin-related myopathy, results in an irregular structure and defective chaperone-like function
-
COI: 1:CAS:528:DyaK1MXksFKks78%3D, PID: 10339554
-
Bova MP, Yaron O, Huang Q, Ding L, Haley DA, Stewart PL, Horwitz J (1999) Mutation R120G in alphaB-crystallin, which is linked to a desmin-related myopathy, results in an irregular structure and defective chaperone-like function. Proc Natl Acad Sci U S A 96:6137–6142
-
(1999)
Proc Natl Acad Sci U S A
, vol.96
, pp. 6137-6142
-
-
Bova, M.P.1
Yaron, O.2
Huang, Q.3
Ding, L.4
Haley, D.A.5
Stewart, P.L.6
Horwitz, J.7
-
14
-
-
0037064015
-
Subunit exchange, conformational stability, and chaperone-like function of the small heat shock protein 16.5 from Methanococcus jannaschii
-
COI: 1:CAS:528:DC%2BD38Xns1Cnsb0%3D, PID: 12176992
-
Bova MP, Huang Q, Ding L, Horwitz J (2002) Subunit exchange, conformational stability, and chaperone-like function of the small heat shock protein 16.5 from Methanococcus jannaschii. J Biol Chem 277:38468–38475. doi:10.1074/jbc.M205594200
-
(2002)
J Biol Chem
, vol.277
, pp. 38468-38475
-
-
Bova, M.P.1
Huang, Q.2
Ding, L.3
Horwitz, J.4
-
15
-
-
0028903455
-
The expanding small heat-shock protein family, and structure predictions of the conserved “alpha-crystallin domain
-
COI: 1:CAS:528:DyaK2MXksl2gs7o%3D, PID: 7723051
-
Caspers GJ, Leunissen JA, de Jong WW (1995) The expanding small heat-shock protein family, and structure predictions of the conserved “alpha-crystallin domain”. J Mol Evol 40:238–248
-
(1995)
J Mol Evol
, vol.40
, pp. 238-248
-
-
Caspers, G.J.1
Leunissen, J.A.2
de Jong, W.W.3
-
16
-
-
79953253901
-
Crystal structure of R120G disease mutant of human alphaB-crystallin domain dimer shows closure of a groove
-
COI: 1:CAS:528:DC%2BC3MXktFyhtrc%3D, PID: 21329698
-
Clark AR, Naylor CE, Bagneris C, Keep NH, Slingsby C (2011) Crystal structure of R120G disease mutant of human alphaB-crystallin domain dimer shows closure of a groove. J Mol Biol 408:118–134. doi:10.1016/j.jmb.2011.02.020
-
(2011)
J Mol Biol
, vol.408
, pp. 118-134
-
-
Clark, A.R.1
Naylor, C.E.2
Bagneris, C.3
Keep, N.H.4
Slingsby, C.5
-
17
-
-
0034719154
-
Structural and functional changes in the alpha A-crystallin R116C mutant in hereditary cataracts
-
COI: 1:CAS:528:DC%2BD3cXot1KhtLk%3D, PID: 11123904
-
Cobb BA, Petrash JM (2000) Structural and functional changes in the alpha A-crystallin R116C mutant in hereditary cataracts. Biochemistry 39:15791–15798
-
(2000)
Biochemistry
, vol.39
, pp. 15791-15798
-
-
Cobb, B.A.1
Petrash, J.M.2
-
18
-
-
0032077156
-
Genealogy of the alpha-crystallin—small heat-shock protein superfamily
-
PID: 9650070
-
de Jong WW, Caspers GJ, Leunissen JA (1998) Genealogy of the alpha-crystallin—small heat-shock protein superfamily. Int J Biol Macromol 22:151–162
-
(1998)
Int J Biol Macromol
, vol.22
, pp. 151-162
-
-
de Jong, W.W.1
Caspers, G.J.2
Leunissen, J.A.3
-
19
-
-
84878935108
-
Mutations of small heat shock proteins and human congenital diseases
-
COI: 1:CAS:528:DC%2BC3sXjtVektA%3D%3D
-
Datskevich PN, Nefedova VV, Sudnitsyna MV, Gusev NB (2012) Mutations of small heat shock proteins and human congenital diseases. Biochemistry (Mosc) 77:1500–1514. doi:10.1134/S0006297912130081
-
(2012)
Biochemistry (Mosc)
, vol.77
, pp. 1500-1514
-
-
Datskevich, P.N.1
Nefedova, V.V.2
Sudnitsyna, M.V.3
Gusev, N.B.4
-
20
-
-
84876065814
-
One size does not fit all: the oligomeric states of alphaB crystallin
-
COI: 1:CAS:528:DC%2BC3sXhvFWktbw%3D, PID: 23340341
-
Delbecq SP, Klevit RE (2013) One size does not fit all: the oligomeric states of alphaB crystallin. FEBS Lett 587:1073–1080. doi:10.1016/j.febslet.2013.01.021
-
(2013)
FEBS Lett
, vol.587
, pp. 1073-1080
-
-
Delbecq, S.P.1
Klevit, R.E.2
-
21
-
-
2642563501
-
Mutant small heat-shock protein 27 causes axonal Charcot-Marie-Tooth disease and distal hereditary motor neuropathy
-
COI: 1:CAS:528:DC%2BD2cXksVajtrk%3D, PID: 15122254
-
Evgrafov OV et al (2004) Mutant small heat-shock protein 27 causes axonal Charcot-Marie-Tooth disease and distal hereditary motor neuropathy. Nat Genet 36:602–606. doi:10.1038/ng1354
-
(2004)
Nat Genet
, vol.36
, pp. 602-606
-
-
Evgrafov, O.V.1
-
22
-
-
33644922974
-
Phylogenetic and biochemical studies reveal a potential evolutionary origin of small heat shock proteins of animals from bacterial class
-
COI: 1:CAS:528:DC%2BD28XitlKgs7g%3D, PID: 16474980
-
Fu X, Jiao W, Chang Z (2006) Phylogenetic and biochemical studies reveal a potential evolutionary origin of small heat shock proteins of animals from bacterial class. A J Mol Evol 62:257–266. doi:10.1007/s00239-005-0076-5
-
(2006)
A J Mol Evol
, vol.62
, pp. 257-266
-
-
Fu, X.1
Jiao, W.2
Chang, Z.3
-
23
-
-
84862529764
-
Molecular basis of axonal dysfunction and traffic impairments in CMT
-
COI: 1:CAS:528:DC%2BC38XnslSju70%3D, PID: 22595495
-
Gentil BJ, Cooper L (2012) Molecular basis of axonal dysfunction and traffic impairments in CMT. Brain Res Bull 88:444–453. doi:10.1016/j.brainresbull.2012.05.003
-
(2012)
Brain Res Bull
, vol.88
, pp. 444-453
-
-
Gentil, B.J.1
Cooper, L.2
-
24
-
-
84924126477
-
A first line of stress defense: small heat shock proteins and their function in protein homeostasis
-
COI: 1:CAS:528:DC%2BC2MXisl2rsLs%3D, PID: 25681016
-
Haslbeck M, Vierling E (2015) A first line of stress defense: small heat shock proteins and their function in protein homeostasis. J Mol Biol 427:1537–1548. doi:10.1016/j.jmb.2015.02.002
-
(2015)
J Mol Biol
, vol.427
, pp. 1537-1548
-
-
Haslbeck, M.1
Vierling, E.2
-
25
-
-
84925510894
-
Dissecting the functional role of the N-terminal domain of the human small heat shock protein HSPB6
-
PID: 25157403
-
Heirbaut M, Beelen S, Strelkov SV, Weeks SD (2014) Dissecting the functional role of the N-terminal domain of the human small heat shock protein HSPB6. PLoS One 9:e105892. doi:10.1371/journal.pone.0105892
-
(2014)
PLoS One
, vol.9
-
-
Heirbaut, M.1
Beelen, S.2
Strelkov, S.V.3
Weeks, S.D.4
-
26
-
-
84899118154
-
The structured core domain of alphaB-crystallin can prevent amyloid fibrillation and associated toxicity
-
COI: 1:CAS:528:DC%2BC2cXmtlSrtLw%3D, PID: 24711386
-
Hochberg GK et al (2014) The structured core domain of alphaB-crystallin can prevent amyloid fibrillation and associated toxicity. Proc Natl Acad Sci U S A 111:E1562–E1570. doi:10.1073/pnas.1322673111
-
(2014)
Proc Natl Acad Sci U S A
, vol.111
, pp. E1562-E1570
-
-
Hochberg, G.K.1
-
27
-
-
0018723651
-
Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide
-
COI: 1:CAS:528:DyaE1MXlsFentbY%3D, PID: 385588
-
Holmgren A (1979) Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide. J Biol Chem 254:9627–9632
-
(1979)
J Biol Chem
, vol.254
, pp. 9627-9632
-
-
Holmgren, A.1
-
28
-
-
33344474711
-
Alpha B-crystallin mutation in dilated cardiomyopathy
-
COI: 1:CAS:528:DC%2BD28XhvVeiu7k%3D, PID: 16483541
-
Inagaki N et al (2006) Alpha B-crystallin mutation in dilated cardiomyopathy. Biochem Biophys Res Commun 342:379–386. doi:10.1016/j.bbrc.2006.01.154
-
(2006)
Biochem Biophys Res Commun
, vol.342
, pp. 379-386
-
-
Inagaki, N.1
-
29
-
-
2642539919
-
Hot-spot residue in small heat-shock protein 22 causes distal motor neuropathy
-
COI: 1:CAS:528:DC%2BD2cXksVajtrg%3D, PID: 15122253
-
Irobi J et al (2004) Hot-spot residue in small heat-shock protein 22 causes distal motor neuropathy. Nat Genet 36:597–601. doi:10.1038/ng1328
-
(2004)
Nat Genet
, vol.36
, pp. 597-601
-
-
Irobi, J.1
-
30
-
-
77957841871
-
Independent evolution of the core domain and its flanking sequences in small heat shock proteins
-
COI: 1:CAS:528:DC%2BC3cXht12isLbM, PID: 20501794
-
Kriehuber T, Rattei T, Weinmaier T, Bepperling A, Haslbeck M, Buchner J (2010) Independent evolution of the core domain and its flanking sequences in small heat shock proteins. FASEB J 24:3633–3642
-
(2010)
FASEB J
, vol.24
, pp. 3633-3642
-
-
Kriehuber, T.1
Rattei, T.2
Weinmaier, T.3
Bepperling, A.4
Haslbeck, M.5
Buchner, J.6
-
31
-
-
0033588379
-
Structural and functional consequences of the mutation of a conserved arginine residue in alphaA and alphaB crystallins
-
COI: 1:CAS:528:DyaK1MXlsVOntb0%3D, PID: 10446186
-
Kumar LV, Ramakrishna T, Rao CM (1999) Structural and functional consequences of the mutation of a conserved arginine residue in alphaA and alphaB crystallins. J Biol Chem 274:24137–24141
-
(1999)
J Biol Chem
, vol.274
, pp. 24137-24141
-
-
Kumar, L.V.1
Ramakrishna, T.2
Rao, C.M.3
-
32
-
-
77957296137
-
Crystal structures of truncated alphaA and alphaB crystallins reveal structural mechanisms of polydispersity important for eye lens function
-
COI: 1:CAS:528:DC%2BC3cXlsFSgtrw%3D, PID: 20440841
-
Laganowsky A et al (2010) Crystal structures of truncated alphaA and alphaB crystallins reveal structural mechanisms of polydispersity important for eye lens function. Protein Sci 19:1031–1043. doi:10.1002/pro.380
-
(2010)
Protein Sci
, vol.19
, pp. 1031-1043
-
-
Laganowsky, A.1
-
33
-
-
0000243829
-
PROCHECK: a program to check the stereochemical quality of protein structures
-
COI: 1:CAS:528:DyaK3sXit12lurY%3D
-
Laskowski RA, MacArthur MW, Moss DS, Thornton JM (1993) PROCHECK: a program to check the stereochemical quality of protein structures. J Appl Crystallogr 26:283–291. doi:10.1107/S0021889892009944
-
(1993)
J Appl Crystallogr
, vol.26
, pp. 283-291
-
-
Laskowski, R.A.1
MacArthur, M.W.2
Moss, D.S.3
Thornton, J.M.4
-
34
-
-
0031934121
-
Autosomal dominant congenital cataract associated with a missense mutation in the human alpha crystallin gene CRYAA
-
COI: 1:CAS:528:DyaK1cXitFWmtLo%3D, PID: 9467006
-
Litt M, Kramer P, LaMorticella DM, Murphey W, Lovrien EW, Weleber RG (1998) Autosomal dominant congenital cataract associated with a missense mutation in the human alpha crystallin gene CRYAA. Hum Mol Genet 7:471–474
-
(1998)
Hum Mol Genet
, vol.7
, pp. 471-474
-
-
Litt, M.1
Kramer, P.2
LaMorticella, D.M.3
Murphey, W.4
Lovrien, E.W.5
Weleber, R.G.6
-
35
-
-
84893007959
-
Analysis and phylogeny of small heat shock proteins from marine viruses and their cyanobacteria host
-
Maaroufi H, Tanguay RM (2013) Analysis and phylogeny of small heat shock proteins from marine viruses and their cyanobacteria host. PLoS One 8:e81207. doi:10.1371/journal.pone.0081207
-
(2013)
PLoS One
, vol.e81207
, pp. 8
-
-
Maaroufi, H.1
Tanguay, R.M.2
-
36
-
-
84962667327
-
Multiple oligomeric structures of a bacterial small heat shock protein
-
COI: 1:CAS:528:DC%2BC28XlvF2qtb4%3D, PID: 27053150
-
Mani N, Bhandari S, Moreno R, Hu L, Prasad BV, Suguna K (2016) Multiple oligomeric structures of a bacterial small heat shock protein. Sci Rep 6:24019. doi:10.1038/srep24019
-
(2016)
Sci Rep
, vol.6
, pp. 24019
-
-
Mani, N.1
Bhandari, S.2
Moreno, R.3
Hu, L.4
Prasad, B.V.5
Suguna, K.6
-
37
-
-
0036371814
-
Drosophila small heat shock proteins: cell and organelle-specific chaperones?
-
COI: 1:CAS:528:DC%2BD38XivVGrurk%3D, PID: 11908067
-
Michaud S, Morrow G, Marchand J, Tanguay RM (2002) Drosophila small heat shock proteins: cell and organelle-specific chaperones? Prog Mol Subcell Biol 28:79–101
-
(2002)
Prog Mol Subcell Biol
, vol.28
, pp. 79-101
-
-
Michaud, S.1
Morrow, G.2
Marchand, J.3
Tanguay, R.M.4
-
38
-
-
43549114993
-
The nuclear localization of Drosophila Hsp27 is dependent on a monopartite arginine-rich NLS and is uncoupled from its association to nuclear speckles
-
COI: 1:CAS:528:DC%2BD1cXmtVahtL4%3D, PID: 18339325
-
Michaud S, Lavoie S, Guimond MO, Tanguay RM (2008) The nuclear localization of Drosophila Hsp27 is dependent on a monopartite arginine-rich NLS and is uncoupled from its association to nuclear speckles. Biochim Biophys Acta 1783:1200–1210. doi:10.1016/j.bbamcr.2008.01.031
-
(2008)
Biochim Biophys Acta
, vol.1783
, pp. 1200-1210
-
-
Michaud, S.1
Lavoie, S.2
Guimond, M.O.3
Tanguay, R.M.4
-
39
-
-
59849129128
-
Abnormal assemblies and subunit exchange of alphaB-crystallin R120 mutants could be associated with destabilization of the dimeric substructure
-
COI: 1:CAS:528:DC%2BD1cXhsFelsL7N, PID: 19140694
-
Michiel M, Skouri-Panet F, Duprat E, Simon S, Ferard C, Tardieu A, Finet S (2009) Abnormal assemblies and subunit exchange of alphaB-crystallin R120 mutants could be associated with destabilization of the dimeric substructure. Biochemistry 48:442–453. doi:10.1021/bi8014967
-
(2009)
Biochemistry
, vol.48
, pp. 442-453
-
-
Michiel, M.1
Skouri-Panet, F.2
Duprat, E.3
Simon, S.4
Ferard, C.5
Tardieu, A.6
Finet, S.7
-
40
-
-
0042733148
-
Refolding of substrates bound to small Hsps relies on a disaggregation reaction mediated most efficiently by ClpB/DnaK
-
COI: 1:CAS:528:DC%2BD3sXmtFeqtLo%3D, PID: 12788951
-
Mogk A, Schlieker C, Friedrich KL, Schonfeld HJ, Vierling E, Bukau B (2003) Refolding of substrates bound to small Hsps relies on a disaggregation reaction mediated most efficiently by ClpB/DnaK. J Biol Chem 278:31033–31042. doi:10.1074/jbc.M303587200
-
(2003)
J Biol Chem
, vol.278
, pp. 31033-31042
-
-
Mogk, A.1
Schlieker, C.2
Friedrich, K.L.3
Schonfeld, H.J.4
Vierling, E.5
Bukau, B.6
-
41
-
-
84953404286
-
Drosophila small heat shock proteins: an update on their features and functions
-
Heat shock proteins, Springer International Publishing
-
Morrow G, Tanguay RM (2015) Drosophila small heat shock proteins: an update on their features and functions. In: Tanguay RM, Hightower LE (eds) The big book on small heat shock proteins, vol 8. Heat shock proteins. Springer International Publishing, pp 579–606
-
(2015)
The big book on small heat shock proteins
, vol.8
, pp. 579-606
-
-
Morrow, G.1
Tanguay, R.M.2
Tanguay, R.M.3
Hightower, L.E.4
-
42
-
-
33644842178
-
Differences in the chaperone-like activities of the four main small heat shock proteins of Drosophila melanogaster
-
COI: 1:CAS:528:DC%2BD28XjslWisr8%3D, PID: 16572729
-
Morrow G, Heikkila JJ, Tanguay RM (2006) Differences in the chaperone-like activities of the four main small heat shock proteins of Drosophila melanogaster. Cell Stress Chaperones 11:51–60
-
(2006)
Cell Stress Chaperones
, vol.11
, pp. 51-60
-
-
Morrow, G.1
Heikkila, J.J.2
Tanguay, R.M.3
-
43
-
-
84862848512
-
Heterooligomeric complexes of human small heat shock proteins
-
COI: 1:CAS:528:DC%2BC38XitFGgsLw%3D, PID: 22002549
-
Mymrikov EV, Seit-Nebi AS, Gusev NB (2012) Heterooligomeric complexes of human small heat shock proteins. Cell Stress Chaperones 17:157–169. doi:10.1007/s12192-011-0296-0
-
(2012)
Cell Stress Chaperones
, vol.17
, pp. 157-169
-
-
Mymrikov, E.V.1
Seit-Nebi, A.S.2
Gusev, N.B.3
-
44
-
-
84879689977
-
Physico-chemical properties of R140G and K141Q mutants of human small heat shock protein HspB1 associated with hereditary peripheral neuropathies
-
COI: 1:CAS:528:DC%2BC3sXot1Klu78%3D, PID: 23643870
-
Nefedova VV, Datskevich PN, Sudnitsyna MV, Strelkov SV, Gusev NB (2013) Physico-chemical properties of R140G and K141Q mutants of human small heat shock protein HspB1 associated with hereditary peripheral neuropathies. Biochimie 95:1582–1592. doi:10.1016/j.biochi.2013.04.014
-
(2013)
Biochimie
, vol.95
, pp. 1582-1592
-
-
Nefedova, V.V.1
Datskevich, P.N.2
Sudnitsyna, M.V.3
Strelkov, S.V.4
Gusev, N.B.5
-
45
-
-
84864436301
-
KoBaMIN: a knowledge-based minimization web server for protein structure refinement
-
COI: 1:CAS:528:DC%2BC3sXjtVCru7Y%3D, PID: 22564897
-
Rodrigues JP, Levitt M, Chopra G (2012) KoBaMIN: a knowledge-based minimization web server for protein structure refinement. Nucleic Acids Res 40:W323–W328. doi:10.1093/nar/gks376
-
(2012)
Nucleic Acids Res
, vol.40
, pp. W323-W328
-
-
Rodrigues, J.P.1
Levitt, M.2
Chopra, G.3
-
46
-
-
34548067977
-
Residue R120 is essential for the quaternary structure and functional integrity of human alphaB-crystallin
-
COI: 1:CAS:528:DC%2BD2sXotF2gtrw%3D, PID: 17655279
-
Simon S, Michiel M, Skouri-Panet F, Lechaire JP, Vicart P, Tardieu A (2007) Residue R120 is essential for the quaternary structure and functional integrity of human alphaB-crystallin. Biochemistry 46:9605–9614. doi:10.1021/bi7003125
-
(2007)
Biochemistry
, vol.46
, pp. 9605-9614
-
-
Simon, S.1
Michiel, M.2
Skouri-Panet, F.3
Lechaire, J.P.4
Vicart, P.5
Tardieu, A.6
-
47
-
-
84857450272
-
Structural and functional specificity of small heat shock protein HspB1 and HspB4, two cellular partners of HspB5: role of the in vitro hetero-complex formation in chaperone activity
-
COI: 1:CAS:528:DC%2BC38XjtFSntrk%3D, PID: 22210387
-
Skouri-Panet F, Michiel M, Ferard C, Duprat E, Finet S (2012) Structural and functional specificity of small heat shock protein HspB1 and HspB4, two cellular partners of HspB5: role of the in vitro hetero-complex formation in chaperone activity. Biochimie 94:975–984. doi:10.1016/j.biochi.2011.12.018
-
(2012)
Biochimie
, vol.94
, pp. 975-984
-
-
Skouri-Panet, F.1
Michiel, M.2
Ferard, C.3
Duprat, E.4
Finet, S.5
-
48
-
-
76649084269
-
Quaternary dynamics and plasticity underlie small heat shock protein chaperone function
-
COI: 1:CAS:528:DC%2BC3cXhvFSnsbs%3D, PID: 20133845
-
Stengel F et al (2010) Quaternary dynamics and plasticity underlie small heat shock protein chaperone function. Proc Natl Acad Sci U S A 107:2007–2012. doi:10.1073/pnas.0910126107
-
(2010)
Proc Natl Acad Sci U S A
, vol.107
, pp. 2007-2012
-
-
Stengel, F.1
-
49
-
-
13444260973
-
R120G alphaB-crystallin promotes the unfolding of reduced alpha-lactalbumin and is inherently unstable
-
COI: 1:CAS:528:DC%2BD2MXht12hurw%3D, PID: 15670152
-
Treweek TM et al (2005) R120G alphaB-crystallin promotes the unfolding of reduced alpha-lactalbumin and is inherently unstable. FEBS J 272:711–724. doi:10.1111/j.1742-4658.2004.04507.x
-
(2005)
FEBS J
, vol.272
, pp. 711-724
-
-
Treweek, T.M.1
-
50
-
-
0035718677
-
Structure and function of the small heat shock protein/alpha-crystallin family of molecular chaperones
-
COI: 1:STN:280:DC%2BD387jtleitQ%3D%3D, PID: 11868270
-
Van Montfort R, Slingsby C, Vierling E (2001) Structure and function of the small heat shock protein/alpha-crystallin family of molecular chaperones. Adv Protein Chem 59:105–156
-
(2001)
Adv Protein Chem
, vol.59
, pp. 105-156
-
-
Van Montfort, R.1
Slingsby, C.2
Vierling, E.3
-
51
-
-
17344361902
-
A missense mutation in the alphaB-crystallin chaperone gene causes a desmin-related myopathy
-
COI: 1:CAS:528:DyaK1cXmtVOmurk%3D, PID: 9731540
-
Vicart P et al (1998) A missense mutation in the alphaB-crystallin chaperone gene causes a desmin-related myopathy. Nat Genet 20:92–95. doi:10.1038/1765
-
(1998)
Nat Genet
, vol.20
, pp. 92-95
-
-
Vicart, P.1
-
52
-
-
33847163530
-
Ligation independent cloning vectors for expression of SUMO fusions
-
COI: 1:CAS:528:DC%2BD2sXit1Gls70%3D, PID: 17251035
-
Weeks SD, Drinker M, Loll PJ (2007) Ligation independent cloning vectors for expression of SUMO fusions. Protein Expr Purif 53:40–50. doi:10.1016/j.pep.2006.12.006
-
(2007)
Protein Expr Purif
, vol.53
, pp. 40-50
-
-
Weeks, S.D.1
Drinker, M.2
Loll, P.J.3
-
53
-
-
0032077161
-
The effect of the intersubunit disulfide bond on the structural and functional properties of the small heat shock protein Hsp25
-
COI: 1:CAS:528:DyaK1cXis1Cltbo%3D, PID: 9650071
-
Zavialov A, Benndorf R, Ehrnsperger M, Zav’yalov V, Dudich I, Buchner J, Gaestel M (1998) The effect of the intersubunit disulfide bond on the structural and functional properties of the small heat shock protein Hsp25. Int J Biol Macromol 22:163–173
-
(1998)
Int J Biol Macromol
, vol.22
, pp. 163-173
-
-
Zavialov, A.1
Benndorf, R.2
Ehrnsperger, M.3
Zav’yalov, V.4
Dudich, I.5
Buchner, J.6
Gaestel, M.7
|