DnaK chaperone-dependent disaggregation by caseinolytic peptidase B (ClpB) mutants reveals functional overlap in the N-terminal domain and nucleotide-binding domain-1 pore tyrosine.
about
Metazoan Hsp70-based protein disaggregases: emergence and mechanismsSpiral architecture of the Hsp104 disaggregase reveals the basis for polypeptide translocationCooperation of Hsp70 and Hsp100 chaperone machines in protein disaggregationSubstrate Discrimination by ClpB and Hsp104.ClpB chaperone passively threads soluble denatured proteins through its central pore.ClpB N-terminal domain plays a regulatory role in protein disaggregationHeat shock protein (Hsp) 70 is an activator of the Hsp104 motor.Mechanistic and Structural Insights into the Prion-Disaggregase Activity of Hsp104.Fusion protein analysis reveals the precise regulation between Hsp70 and Hsp100 during protein disaggregation.Structural determinants for protein unfolding and translocation by the Hsp104 protein disaggregase.Katanin spiral and ring structures shed light on power stroke for microtubule severing.Asymmetric processing of a substrate protein in sequential allosteric cycles of AAA+ nanomachines.Comparative roles of clpA and clpB in the survival of S. Typhimurium under stress and virulence in poultry.The amino-terminal domain of ClpB protein plays a crucial role in its substrate disaggregation activity
P2860
Q26779046-EE7E18A5-A3F6-417B-AE70-E069B4549CFDQ27723476-434A12B3-A588-449B-89AB-5C01E226F8E0Q28085237-FC1278D1-0AF5-43C0-AD0C-C8F7B9ADADE0Q33734726-01C5B490-CF00-4F84-BF62-4FAC602F095BQ34442141-452A519E-1361-4830-8850-D484F6ACE150Q36394450-7C0F5557-8633-419A-9940-3A4C9D51D305Q36884034-89548E24-AC3C-4203-BF33-56AA4D759B33Q38648239-0F43FC0B-6068-4CB2-AE3B-328DC21EAC7DQ41447461-C7C6FFE7-148B-42E6-82A0-01FC783A0CFBQ47106105-DE64E1BF-1BBC-437D-BDF8-83D8415F8CDEQ47983792-DF69758C-3F97-4754-935D-A4CF37A2E757Q53127332-F960791D-6F21-4DEB-85E1-79E58FF60129Q55246036-5EFCADE0-9C29-4096-8FCE-E8047AA8858DQ58554573-3AB93353-F44C-4F2E-868B-452709ADB5C9
P2860
DnaK chaperone-dependent disaggregation by caseinolytic peptidase B (ClpB) mutants reveals functional overlap in the N-terminal domain and nucleotide-binding domain-1 pore tyrosine.
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
2012年论文
@zh
2012年论文
@zh-cn
name
DnaK chaperone-dependent disag ...... inding domain-1 pore tyrosine.
@ast
DnaK chaperone-dependent disag ...... inding domain-1 pore tyrosine.
@en
type
label
DnaK chaperone-dependent disag ...... inding domain-1 pore tyrosine.
@ast
DnaK chaperone-dependent disag ...... inding domain-1 pore tyrosine.
@en
prefLabel
DnaK chaperone-dependent disag ...... inding domain-1 pore tyrosine.
@ast
DnaK chaperone-dependent disag ...... inding domain-1 pore tyrosine.
@en
P2093
P2860
P356
P1476
DnaK chaperone-dependent disag ...... inding domain-1 pore tyrosine.
@en
P2093
Joel R Hoskins
Shannon M Doyle
Sue Wickner
P2860
P304
28470-28479
P356
10.1074/JBC.M112.383091
P407
P577
2012-06-28T00:00:00Z