Serine 59 phosphorylation of {alpha}B-crystallin down-regulates its anti-apoptotic function by binding and sequestering Bcl-2 in breast cancer cells.
about
Multiple molecular architectures of the eye lens chaperone B-crystallin elucidated by a triple hybrid approachHeat shock proteins and heat shock factor 1 in carcinogenesis and tumor development: an updateStrain-independent increases of crystallin proteins in the retina of type 1 diabetic rats.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.Effect of proline rich 15-deficiency on trophoblast viability and survival.Phosphoproteomic differences in major depressive disorder postmortem brains indicate effects on synaptic function.Chaperone peptides of α-crystallin inhibit epithelial cell apoptosis, protein insolubilization, and opacification in experimental cataractsRegulated structural transitions unleash the chaperone activity of αB-crystallinαB-crystallin: Portrait of a malignant chaperone as a cancer therapeutic targetPathology-dependent effects linked to small heat shock proteins expression: an updateContribution of small heat shock proteins to muscle development and function.Small heat-shock proteins: important players in regulating cellular proteostasis.Therapeutic potential of α-crystallin.Regulation of αA- and αB-crystallins via phosphorylation in cellular homeostasis.HspB1, HspB5 and HspB4 in Human Cancers: Potent Oncogenic Role of Some of Their Client Proteins.Differential phosphorylation-based regulation of αB-crystallin chaperone activity for multipass transmembrane proteins.Increased expression of small heat shock protein αB-crystallin after intracerebral hemorrhage in adult rats.
P2860
Q27675996-3A4E48CE-64DD-478C-B797-B16C98F2FFCFQ28272905-E1F13103-A230-445B-B48C-A6A4F95D1E1FQ35070341-EE0B8C42-A155-4E5B-A2C5-22E8A206EF76Q35951744-3E3C0FEA-83A3-4A05-9D50-94A6E5296828Q36319594-237FC4F4-51DF-4FA8-B819-37DDFDA1C4D0Q36336018-2D1AA1DA-37F8-42E9-B9A7-730AC341C5ADQ36377477-E87DBF8D-289C-44C1-8567-CA31CDF4D886Q36812475-8613A853-739E-47A6-B697-993B23C8A280Q37218406-E6AC9444-ACE4-4751-AC5F-B99AAE85DB65Q37241367-DADC1B4A-E63C-4234-9299-5F1C9E416DDBQ37288545-52A75AF4-6B01-46EF-8E76-3C644435C48EQ38179729-B6D532FA-96A3-42F6-A0D3-71C2F2DD18D2Q38263437-C33C1CC9-9786-4CF6-977D-13C52091F8E0Q38404383-4D96810F-2310-4D44-BA94-5C978128D533Q38554083-AEF97F5D-FCD2-4BBB-8A54-562A5F1A39F9Q38671885-C7F2AF89-DE32-4088-A5A5-E6C0799A7AE5Q38745474-37DFFB90-2844-4879-AA53-85912F3B7F13Q48174378-7934FFC0-2D9E-4EFB-A554-D367AFCE5617
P2860
Serine 59 phosphorylation of {alpha}B-crystallin down-regulates its anti-apoptotic function by binding and sequestering Bcl-2 in breast cancer cells.
description
2010 nî lūn-bûn
@nan
2010 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Serine 59 phosphorylation of { ...... Bcl-2 in breast cancer cells.
@ast
Serine 59 phosphorylation of { ...... Bcl-2 in breast cancer cells.
@en
Serine 59 phosphorylation of { ...... Bcl-2 in breast cancer cells.
@nl
type
label
Serine 59 phosphorylation of { ...... Bcl-2 in breast cancer cells.
@ast
Serine 59 phosphorylation of { ...... Bcl-2 in breast cancer cells.
@en
Serine 59 phosphorylation of { ...... Bcl-2 in breast cancer cells.
@nl
prefLabel
Serine 59 phosphorylation of { ...... Bcl-2 in breast cancer cells.
@ast
Serine 59 phosphorylation of { ...... Bcl-2 in breast cancer cells.
@en
Serine 59 phosphorylation of { ...... Bcl-2 in breast cancer cells.
@nl
P2093
P2860
P356
P1476
Serine 59 phosphorylation of { ...... g Bcl-2 in breast cancer cells
@en
P2093
Alain Lilienbaum
Nathalie Launay
Patrick Vicart
P2860
P304
37324-37332
P356
10.1074/JBC.M110.124388
P407
P50
P577
2010-09-14T00:00:00Z