Split Renilla luciferase protein fragment-assisted complementation (SRL-PFAC) to characterize Hsp90-Cdc37 complex and identify critical residues in protein/protein interactions.
about
Allosteric regulation of the Hsp90 dynamics and stability by client recruiter cochaperones: protein structure network modelingFirefly luciferase and RLuc8 exhibit differential sensitivity to oxidative stress in apoptotic cells.Probing molecular mechanisms of the Hsp90 chaperone: biophysical modeling identifies key regulators of functional dynamics.Diversity in genetic in vivo methods for protein-protein interaction studies: from the yeast two-hybrid system to the mammalian split-luciferase system.A Novel Allosteric Mechanism of NF-κB Dimerization and DNA Binding Targeted by an Anti-Inflammatory Drug.Sulforaphane inhibits pancreatic cancer through disrupting Hsp90-p50(Cdc37) complex and direct interactions with amino acids residues of Hsp90.Soluble epoxide hydrolase dimerization is required for hydrolase activity.The molecular chaperone Hsp70 activates protein phosphatase 5 (PP5) by binding the tetratricopeptide repeat (TPR) domain.Split-luciferase complementary assay: applications, recent developments, and future perspectives.Restricting direct interaction of CDC37 with HSP90 does not compromise chaperoning of client proteinsAtomistic simulations and network-based modeling of the Hsp90-Cdc37 chaperone binding with Cdk4 client protein: A mechanism of chaperoning kinase clients by exploiting weak spots of intrinsically dynamic kinase domains.Bovine Hemoglobin Derived Peptide Asn-Phe-Gly-Lys Inhibits Pancreatic Cancer Cells Metastasis by Targeting Secreted Hsp90α.Amino acids essential for the interaction between cellular heat shock protein 90 and a Kaposi's sarcoma-associated herpesvirus-encoded protein kinase ORF36.
P2860
Q30358343-B52B1085-1341-4092-8D99-07E850671DCFQ33908603-BB3FE0FF-6E50-481D-8BF1-DD50BB867E4FQ34280087-A99CFCB8-5027-4DA5-A8B7-7B85FF31ABD7Q34280594-4B2A44F2-8FE9-45F4-B574-EC314FD93EF4Q34511687-9DC4A632-F843-4DD9-AFEA-23F26BB1494AQ36066968-8DEE6703-7929-4034-85FA-42B0A6628FAAQ36685182-11825F14-B6CB-4065-910B-AD6C491B9798Q37536572-7DFBFD63-5D4A-4720-BF78-8829EB686C5CQ38227133-705E725B-4CFE-4D7E-B6E3-B5AFDB0EF2A2Q38725015-AE3BC917-9198-4599-ABA8-6242CE2BE25DQ47265199-AB694651-6377-4840-9A68-5153DE0FD308Q47588577-80FAA81A-DB04-4517-A60B-49CA570A1637Q47992374-B56C7C46-34D9-46EB-B332-D643E1FE01DF
P2860
Split Renilla luciferase protein fragment-assisted complementation (SRL-PFAC) to characterize Hsp90-Cdc37 complex and identify critical residues in protein/protein interactions.
description
2010 nî lūn-bûn
@nan
2010 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի ապրիլին 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
Split Renilla luciferase prote ...... protein/protein interactions.
@ast
Split Renilla luciferase prote ...... protein/protein interactions.
@en
type
label
Split Renilla luciferase prote ...... protein/protein interactions.
@ast
Split Renilla luciferase prote ...... protein/protein interactions.
@en
prefLabel
Split Renilla luciferase prote ...... protein/protein interactions.
@ast
Split Renilla luciferase prote ...... protein/protein interactions.
@en
P2093
P2860
P50
P356
P1476
Split Renilla luciferase prote ...... n protein/protein interactions
@en
P2093
Yiqun Jiang
P2860
P304
21023-21036
P356
10.1074/JBC.M110.103390
P407
P577
2010-04-22T00:00:00Z