Adenosine Diphosphate

heat shock protein 90 beta family member 1 ; Homo sapiens







9 Article(s)
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Title
Pub. Year
#Total Relationships
1 30787103 The endoplasmic reticulum (ER) chaperones BiP and Grp94 selectively associate when BiP is in the ADP conformation. 2019 Apr 19 4
2 31202885 Conformational Cycling within the Closed State of Grp94, an Hsp90-Family Chaperone. 2019 Aug 9 2
3 29805488 Potential mechanism and drug candidates for sepsis-induced acute lung injury. 2018 Jun 1
4 17936703 Structures of GRP94-nucleotide complexes reveal mechanistic differences between the hsp90 chaperones. 2007 Oct 12 1
5 15951571 Structure of unliganded GRP94, the endoplasmic reticulum Hsp90. Basis for nucleotide-induced conformational change. 2005 Aug 26 1
6 15236592 Adenosine nucleotides and the regulation of GRP94-client protein interactions. 2004 Jul 13 3
7 15292259 Ligand-induced conformational shift in the N-terminal domain of GRP94, an Hsp90 chaperone. 2004 Oct 29 1
8 10816561 Ligand interactions in the adenosine nucleotide-binding domain of the Hsp90 chaperone, GRP94. I. Evidence for allosteric regulation of ligand binding. 2000 Jul 28 2
9 10478836 Interaction of radicicol with members of the heat shock protein 90 family of molecular chaperones. 1999 Sep 1