Ser-59 is the major phosphorylation site in alphaB-crystallin accumulated in the brains of patients with Alexander's disease.
about
Binding determinants of the small heat shock protein, αB-crystallin: recognition of the 'IxI' motifSolid-state NMR and SAXS studies provide a structural basis for the activation of αB-crystallin oligomersN-terminal domain of B-crystallin provides a conformational switch for multimerization and structural heterogeneityBehavioral defects in chaperone-deficient Alzheimer's disease model mice.Identification of the molecular chaperone alpha B-crystallin in demineralized bone powder and osteoblast-like cells.A novel molecular dynamics approach to evaluate the effect of phosphorylation on multimeric protein interface: the αB-Crystallin case study.Novel roles for α-crystallins in retinal function and disease.Crystallins and neuroinflammation: The glial side of the story.One size does not fit all: the oligomeric states of αB crystallin.Regulation of αA- and αB-crystallins via phosphorylation in cellular homeostasis.Phosphorylation of αB-crystallin supports reactive astrogliosis in demyelination.Mimicking phosphorylation of alphaB-crystallin affects its chaperone activityInteractive sequences in the stress protein and molecular chaperone human alphaB crystallin recognize and modulate the assembly of filamentsPhosphorylation of Ser45 and Ser59 of αB-crystallin and p38/extracellular regulated kinase activity determine αB-crystallin-mediated protection of rat brain astrocytes from C2-ceramide- and staurosporine-induced cell death.Age-related increase of insoluble, phosphorylated small heat shock proteins in human skeletal muscle.
P2860
Q24305073-0FAFD96C-E0B8-49E8-857D-0979708F6A39Q27664218-AFAA8EBB-2066-4471-964C-C37750B38348Q27667422-A80B774B-F950-4678-BF6C-56771FDAA8A7Q30476539-887569E5-E146-4365-B83E-7D64C28B81FDQ30873360-C27609A4-D275-4761-9915-1CD23F25B66FQ35951744-6371704F-5269-47D5-8C3F-816794F1E403Q36319594-BB1DDECA-A6AE-426B-B474-CD967DEE3802Q36345592-43F9D898-0C0B-4322-B57F-37FE056AFE71Q37398573-FD86EC70-D408-4540-BCC5-4ACD82005EC1Q38554083-3CA93EFE-C61E-4504-86A7-1DC3FD74D893Q40333374-FD4A96F2-F101-425F-B9E7-D3D2D6E339BDQ41084011-ACF6C09A-8836-465B-994F-20828FE1A740Q42058804-548666B0-AE35-49BD-B629-4900705EAE5AQ54369374-64E359B9-280C-40A1-8025-B257F1CD4AADQ54690177-FB8AE85B-ECCE-44A8-A743-07D36E1EADEE
P2860
Ser-59 is the major phosphorylation site in alphaB-crystallin accumulated in the brains of patients with Alexander's disease.
description
2001 nî lūn-bûn
@nan
2001 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Ser-59 is the major phosphoryl ...... ents with Alexander's disease.
@ast
Ser-59 is the major phosphoryl ...... ents with Alexander's disease.
@en
type
label
Ser-59 is the major phosphoryl ...... ents with Alexander's disease.
@ast
Ser-59 is the major phosphoryl ...... ents with Alexander's disease.
@en
prefLabel
Ser-59 is the major phosphoryl ...... ents with Alexander's disease.
@ast
Ser-59 is the major phosphoryl ...... ents with Alexander's disease.
@en
P2093
P2860
P1476
Ser-59 is the major phosphoryl ...... ents with Alexander's disease.
@en
P2093
Kishikawa M
P2860
P304
P356
10.1046/J.1471-4159.2001.00038.X
P407
P577
2001-02-01T00:00:00Z