Crystal Structure of R120G Disease Mutant of Human αB-Crystallin Domain Dimer Shows Closure of a Groove - Wikidata - wikimedia - TriplyDB

Crystal Structure of R120G Disease Mutant of Human αB-Crystallin Domain Dimer Shows Closure of a Groove

Crystal Structure of R120G Disease Mutant of Human αB-Crystallin Domain Dimer Shows Closure of a Groove

http://www.wikidata.org/entity/Q27666994

about

Binding determinants of the small heat shock protein, αB-crystallin: recognition of the 'IxI' motif Multiple molecular architectures of the eye lens chaperone B-crystallin elucidated by a triple hybrid approach Changes in the quaternary structure and function of MjHSP16.5 attributable to deletion of the IXI motif and introduction of the substitution, R107G, in the -crystallin domain The structured core domain of B-crystallin can prevent amyloid fibrillation and associated toxicity Identification of subunit-subunit interaction sites in αA-WT crystallin and mutant αA-G98R crystallin using isotope-labeled cross-linker and mass spectrometry Functions of crystallins in and out of lens: roles in elongated and post-mitotic cells The specificity of the interaction between αB-crystallin and desmin filaments and its impact on filament aggregation and cell viability.Getting folded: chaperone proteins in muscle development, maintenance and disease.Structural features of isomerizable aspartyl residues in human α-crystallins.A Mechanism of Subunit Recruitment in Human Small Heat Shock Protein Oligomers The novel αB-crystallin (CRYAB) mutation p.D109G causes restrictive cardiomyopathy.Selective acquisition of host-derived ICAM-1 by HIV-1 is a matrix-dependent process.A first line of stress defense: small heat shock proteins and their function in protein homeostasis.Tobacco class I cytosolic small heat shock proteins are under transcriptional and translational regulations in expression and heterocomplex prevails under the high-temperature stress condition in vitro.Desmin-related cardiomyopathy: an unfolding story A conserved histidine modulates HSPB5 structure to trigger chaperone activity in response to stress-related acidosis Small heat shock proteins and α-crystallins: dynamic proteins with flexible functions.Chaperone activity of small heat shock proteins underlies therapeutic efficacy in experimental autoimmune encephalomyelitis.Cryoelectron microscopy analysis of small heat shock protein 16.5 (Hsp16.5) complexes with T4 lysozyme reveals the structural basis of multimode binding Evolution of crystallins for a role in the vertebrate eye lens.Multiple oligomeric structures of a bacterial small heat shock protein An unusual dimeric small heat shock protein provides insight into the mechanism of this class of chaperones.Differential role of arginine mutations on the structure and functions of α-crystallin.The Human 343delT HSPB5 Chaperone Associated with Early-onset Skeletal Myopathy Causes Defects in Protein Solubility Five small heat shock protein genes from Chilo suppressalis: characteristics of gene, genomic organization, structural analysis, and transcription profiles.One size does not fit all: the oligomeric states of αB crystallin.Large potentials of small heat shock proteins.Contribution of small heat shock proteins to muscle development and function.Medical implications of understanding the functions of human small heat shock proteins.Regulation of αA- and αB-crystallins via phosphorylation in cellular homeostasis.C-terminal interactions mediate the quaternary dynamics of αB-crystallin.Structural and mechanistic implications of metal binding in the small heat-shock protein αB-crystallin Structure of the α-crystallin domain from the redox-sensitive chaperone, HSPB1.A S52P mutation in the 'α-crystallin domain' of Mycobacterium leprae HSP18 reduces its oligomeric size and chaperone function.Hsp27 gene in Drosophila ananassae subgroup was split by a recently acquired intron.Characterization of human small heat shock protein HSPB1 α-crystallin domain localized mutants associated with hereditary motor neuron diseases.The chaperone αB-crystallin uses different interfaces to capture an amorphous and an amyloid client.Oligomeric structure and chaperone-like activity of Drosophila melanogaster mitochondrial small heat shock protein Hsp22 and arginine mutants in the alpha-crystallin domain.The Potential Functions of Small Heat Shock Proteins in the Uterine Musculature during Pregnancy.Chaperone activity of human small heat shock protein-GST fusion proteins.

P2860

Q24305073-84B1C9D2-6298-493D-A022-FF7B9DEC06B6 Q27675996-9B17D846-F928-4094-BD26-0E804F6D32EB Q27677069-57A666DF-F398-4E64-AE0A-08665B5C3E37 Q27683083-CCBD3F56-9C28-4A4B-95AF-8B3987A5D501 Q28533655-7E2DEA3A-5AFE-4016-B71C-52FAA484F485 Q28655525-80894D9B-ADEA-449A-952B-727CDD4323F1 Q30539278-B8BC98D5-AFAE-4C3B-A322-2847F34F6AA1 Q34055646-3914A6E7-1206-494A-A07A-E96A9EA1B181 Q34344539-AA5125D5-FC2E-4FFF-8915-679D16D5CEC8 Q34481801-7E225EC1-2CC7-49B6-A90E-33C0014075DC Q34556520-EED95CA6-9896-4A1D-B8F7-F2C09FDAFBAC Q34992721-CAC5BED8-83B0-4310-84E9-56D28AB7CDC9 Q35178845-9E184AA5-2F81-4CB7-AF7B-D598D5D5FF17 Q35232294-5A319947-311F-4D78-80D6-CDF681C8334F Q35395372-95D28C9D-7E00-4A9C-ACFD-263AD4BD59E3 Q35686039-302F82C2-32FE-42F7-8780-DE02509C7F5F Q36287203-4263A7F8-80A8-465A-BF5C-640A24061750 Q36332934-5CD2760C-A014-45D1-82F5-1B3313776457 Q36620780-35D211A6-AF29-4056-A50C-3C1D74671631 Q36722216-BDCD8282-65BE-414D-9147-7473B3D9D678 Q36774315-FF4FEE91-FC17-4BEF-8792-F883635C43D6 Q36823804-94B91B7A-8832-4F22-9A3C-97D7778411E0 Q37021424-FC58450C-06F8-4B42-8D16-D900FF644732 Q37098883-43062ED5-C410-420B-99DD-3B7EF2B22E4E Q37378873-98AF71AC-33E0-42C5-81A4-AD4EF9514D26 Q37398573-08C7FD92-F62D-4F82-87D3-7354CDAAFDF3 Q37947562-506B50F5-F9A9-4D49-A0CD-52D7D545B6C8 Q38179729-EB2F45FB-97D2-4D31-B596-777A7688B1C0 Q38443894-F44E31A7-E20A-4C05-A000-191D2946E1C8 Q38554083-2ECC1AC3-32EB-48D3-98D5-8326F7DC5980 Q40183520-906E228D-6B5A-4F95-9416-D988F24C9913 Q40354579-68C3F2C8-1589-4293-A876-5849A98C92B0 Q41555741-AA6C91FB-923D-40C9-91EA-E0E128B3DDC4 Q43746026-C8B771F3-6185-4139-B250-F91D8A297913 Q46526383-6BCC7E56-D502-4E57-B473-1D0755FDC500 Q47734624-F6AA1B99-579F-47C4-B6B8-89B9FCB729FD Q48121254-6972E4A1-CFBC-4E00-8189-94A4751CF774 Q51066662-0EC746FD-2A22-40D7-A46F-EC3B20A16A46 Q51066680-1913665D-BDEC-4115-96C3-8256CB61ED15 Q51165051-DADBC586-97EB-4854-A416-8E6D66440D4E

P2860

Crystal Structure of R120G Disease Mutant of Human αB-Crystallin Domain Dimer Shows Closure of a Groove

http://www.wikidata.org/entity/Q27666994

description

2011 nî lūn-bûn

@nan

2011 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի ապրիլին հրատարակված գիտական հոդված

@hy

2011年の論文

@ja

2011年論文

@yue

2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

@zh-tw

2011年论文

@wuu

name

Crystal Structure of R120G Dis ...... imer Shows Closure of a Groove

@ast

Crystal Structure of R120G Dis ...... imer Shows Closure of a Groove

@en

Crystal Structure of R120G Dis ...... imer Shows Closure of a Groove

@nl

type

label

Crystal Structure of R120G Dis ...... imer Shows Closure of a Groove

@ast

Crystal Structure of R120G Dis ...... imer Shows Closure of a Groove

@en

Crystal Structure of R120G Dis ...... imer Shows Closure of a Groove

@nl

prefLabel

Crystal Structure of R120G Dis ...... imer Shows Closure of a Groove

@ast

Crystal Structure of R120G Dis ...... imer Shows Closure of a Groove

@en

Crystal Structure of R120G Dis ...... imer Shows Closure of a Groove

@nl

P1433

Q27666994-6362D536-E085-474C-8367-43548E8BC55D

P1476

Q27666994-607F77A9-A4D9-4A24-9144-DEDA09E71046

P2093

Q27666994-4D5FE6CB-1B2C-4A54-BE9F-276037D3937B

Q27666994-5ED5F40A-5CF8-44E0-95D1-C9C5B2B9FA4C

Q27666994-6ADFAC5B-ECD1-4718-96E3-BBC1FA638F29

Q27666994-B56FCBCF-9A1F-4B0F-AD5C-A1339B63DD30

Q27666994-DD23C61C-BEF5-4D8F-AAE2-8A84E4FE3DD7

P2860

Q27666994-0DE3DE23-18A1-4FAD-B6CA-7BFCF293D6F1

Q27666994-119B3A09-BF61-43ED-A26D-F963A32E6AE6

Q27666994-12643DF4-AA02-4FD4-AB7A-4E52FEED03E5

Q27666994-129C85C9-4C6C-45F3-A590-14FBC9B0AB5B

Q27666994-14AE37D1-0AC7-4A5F-A5D8-FB9B723F6D5E

Q27666994-17C18BE9-4310-474A-B0BE-66A606FD1798

Q27666994-1A405964-2071-4C50-AF22-3046223D059D

Q27666994-2A7E9A59-1D5F-4540-BF7A-7710AA90EB80

Q27666994-3B7ABCBB-A109-4197-8C30-4B805498176F

Q27666994-3B9DB611-AB40-4206-A4C5-64A94B95ED48

P304

Q27666994-6830B9CA-DB1B-4140-B31E-43305A11C06F

P31

Q27666994-4CCF410E-282F-459B-91C8-AB4DEEDA594D

P3181

Q27666994-7C156C33-A284-43A1-B790-C81636117215

P356

Q27666994-A900B04D-E895-4327-8AA5-C2F672248F96

P407

Q27666994-527F7B2B-3404-49D6-B0A1-FB90B16EA37B

P433

Q27666994-3E8E87D6-D96D-48C1-855D-2472C947F2D9

P478

Q27666994-43695CBF-5D72-40C5-9A41-441EAB0C1A60

P577

Q27666994-BA31779C-1586-4E4E-87C1-13D814F7310C

P5875

Q27666994-1D3738B8-C4E4-46A8-AEDE-CC56BD476648

P698

Q27666994-B7079E07-20B8-4E6C-8C98-7A69D115D85A

P921

Q27666994-F3683956-6BD9-47CE-B26B-204F0BDCE34F

P932

Q27666994-EB46C321-5804-475F-A2B2-57A288360129

P3181

P356

J.JMB.2011.02.020

P1433

Journal of Molecular Biology

P1476

Crystal Structure of R120G Dis ...... imer Shows Closure of a Groove

@en

P2093

A R Clark

http://www.w3.org/2001/XMLSchema#string

C Bagnéris

http://www.w3.org/2001/XMLSchema#string

C E Naylor

http://www.w3.org/2001/XMLSchema#string

C Slingsby

http://www.w3.org/2001/XMLSchema#string

N H Keep

http://www.w3.org/2001/XMLSchema#string

P2860

Autosomal dominant congenital cataract associated with a missense mutation in the human alpha crystallin gene CRYAA

A missense mutation in the alphaB-crystallin chaperone gene causes a desmin-related myopathy

Protein quality control during aging involves recruitment of the macroautophagy pathway by BAG3

Crystal structures of alpha-crystallin domain dimers of alphaB-crystallin and Hsp20

The human genome encodes 10 alpha-crystallin-related small heat shock proteins: HspB1-10

MolProbity: all-atom contacts and structure validation for proteins and nucleic acids

Crystal structure and assembly of a eukaryotic small heat shock protein

Crystal structures of truncated alphaA and alphaB crystallins reveal structural mechanisms of polydispersity important for eye lens function

Non-3D domain swapped crystal structure of truncated zebrafish alphaA crystallin

Solid-state NMR and SAXS studies provide a structural basis for the activation of αB-crystallin oligomers

P304

118-34

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P3181

2438455

http://www.w3.org/2001/XMLSchema#string

P356

10.1016/J.JMB.2011.02.020

http://www.w3.org/2001/XMLSchema#string

P407

P433

1

http://www.w3.org/2001/XMLSchema#string

P478

408

http://www.w3.org/2001/XMLSchema#string

P577

2011-04-22T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

49844101

http://www.w3.org/2001/XMLSchema#string

P698

21329698

http://www.w3.org/2001/XMLSchema#string

P921

crystal structure

P932

3158665

http://www.w3.org/2001/XMLSchema#string