about
Structural plasticity and noncovalent substrate binding in the GroEL apical domain. A study using electrospay ionization mass spectrometry and fluorescence binding studiesStructure and function of RbcX, an assembly chaperone for hexadecameric RubiscoCoupled chaperone action in folding and assembly of hexadecameric RubiscoCrystal structure of a chaperone-bound assembly intermediate of form I RubiscoStructure and function of the AAA+ protein CbbX, a red-type Rubisco activaseStructure of green-type Rubisco activase from tobaccoGroEL/ES Chaperonin Modulates the Mechanism and Accelerates the Rate of TIM-Barrel Domain FoldingStructure and mechanism of the Rubisco-assembly chaperone Raf1Structure of human heat-shock transcription factor 1 in complex with DNADegradation of potent Rubisco inhibitor by selective sugar phosphataseCrystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaKPolyQ proteins interfere with nuclear degradation of cytosolic proteins by sequestering the Sis1p chaperone.Molecular chaperones in the cytosol: from nascent chain to folded proteinShift reagents for 39K NmrRole of small subunit in mediating assembly of red-type form I Rubisco.Coexistence of group I and group II chaperonins in the archaeon Methanosarcina mazei.Chaperonin-catalyzed rescue of kinetically trapped states in protein folding.Protein folding in the cytoplasm and the heat shock response.Molecular chaperone functions in protein folding and proteostasis.Molecular chaperones as modulators of polyglutamine protein aggregation and toxicityOpposing effects of folding and assembly chaperones on evolvability of Rubisco.Structural basis for subunit assembly in UDP-glucose pyrophosphorylase from Saccharomyces cerevisiae.Converging concepts of protein folding in vitro and in vivo.Structural Analysis of the Rubisco-Assembly Chaperone RbcX-II from Chlamydomonas reinhardtii.A mobile loop order-disorder transition modulates the speed of chaperonin cycling.The GroEL-GroES Chaperonin Machine: A Nano-Cage for Protein Folding.Essential role of the chaperonin folding compartment in vivo.Soluble Oligomers of PolyQ-Expanded Huntingtin Target a Multiplicity of Key Cellular Factors.Role of auxiliary proteins in Rubisco biogenesis and function.In vivo aspects of protein folding and quality control.Biogenesis and Metabolic Maintenance of Rubisco.Rubisco Activases: AAA+ Chaperones Adapted to Enzyme RepairAmyloid-like aggregates sequester numerous metastable proteins with essential cellular functions.The protein import motor of mitochondria: a targeted molecular ratchet driving unfolding and translocation.Cellular toxicity of polyglutamine expansion proteins: mechanism of transcription factor deactivation.Mechanism of Enzyme Repair by the AAA+ Chaperone Rubisco Activase.Chaperonin cofactors, Cpn10 and Cpn20, of green algae and plants function as hetero-oligomeric ring complexes.Differential substrate specificity of group I and group II chaperonins in the archaeon Methanosarcina mazei.The first chaperonin.Functional characterization of an archaeal GroEL/GroES chaperonin system: significance of substrate encapsulation.
P50
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P50
description
hulumtuese
@sq
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Manajit Hayer-Hartl
@ast
Manajit Hayer-Hartl
@en
Manajit Hayer-Hartl
@es
Manajit Hayer-Hartl
@nl
Manajit Hayer-Hartl
@sl
type
label
Manajit Hayer-Hartl
@ast
Manajit Hayer-Hartl
@en
Manajit Hayer-Hartl
@es
Manajit Hayer-Hartl
@nl
Manajit Hayer-Hartl
@sl
prefLabel
Manajit Hayer-Hartl
@ast
Manajit Hayer-Hartl
@en
Manajit Hayer-Hartl
@es
Manajit Hayer-Hartl
@nl
Manajit Hayer-Hartl
@sl
P1053
V-8078-2017
P106
P21
P31
P496
0000-0001-8213-6742