about
Heterozygous yeast deletion collection screens reveal essential targets of Hsp90Mutation of the ATP-binding pocket of SSA1 indicates that a functional interaction between Ssa1p and Ydj1p is required for post-translational translocation into the yeast endoplasmic reticulum.Identification of the TRiC/CCT substrate binding sites uncovers the function of subunit diversity in eukaryotic chaperoninsThe amino-terminal transforming region of simian virus 40 large T and small t antigens functions as a J domain.Specific molecular chaperone interactions and an ATP-dependent conformational change are required during posttranslational protein translocation into the yeast ER.Protein quality control: chaperones culling corrupt conformations.Molecular chaperones and the art of recognizing a lost causeMitochondrial Hsp70 cannot replace BiP in driving protein translocation into the yeast endoplasmic reticulumFolding and quality control of the VHL tumor suppressor proceed through distinct chaperone pathwaysEvidence for interaction between Hsp90 and the ER membrane complexCellular functions and molecular mechanisms of non-lysine ubiquitination
P50
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P50
description
researcher ORCID ID = 0000-0002-8033-6748
@en
wetenschapper
@nl
name
Amie J McClellan
@ast
Amie J McClellan
@en
Amie J McClellan
@nl
type
label
Amie J McClellan
@ast
Amie J McClellan
@en
Amie J McClellan
@nl
prefLabel
Amie J McClellan
@ast
Amie J McClellan
@en
Amie J McClellan
@nl
P106
P31
P496
0000-0002-8033-6748