相关参考文献
注意：仅列出部分参考文献，下载原文获取全部文献信息。ATP-Independent Chaperones
Rishav Mitra et al.
ANNUAL REVIEW OF BIOPHYSICS (2022)
Folding or holding?-Hsp70 and Hsp90 chaperoning of misfolded proteins in neurodegenerative disease
Benjamin S. Rutledge et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2022)
The multiple roles and therapeutic potential of HSP60 in cancer
Yaoxiang Tang et al.
BIOCHEMICAL PHARMACOLOGY (2022)
Hsp70 Inhibits Aggregation of IAPP by Binding to the Heterogeneous Prenucleation Oligomers
Neeraja Chilukoti et al.
BIOPHYSICAL JOURNAL (2021)
ATP Impedes the Inhibitory Effect of Hsp90 on Aβ40 Fibrillation
Hongzhi Wang et al.
JOURNAL OF MOLECULAR BIOLOGY (2021)
Hsp90-interacting Co-chaperones and their Family Proteins in Tau Regulation: Introducing a Novel Role for Cdc37L1
Stephanie L. Peak et al.
NEUROSCIENCE (2021)
Structural basis for the structural dynamics of human mitochondrial chaperonin mHsp60 (vol 11, 14809, 2021)
Joseph Che-Yen Wang et al.
SCIENTIFIC REPORTS (2021)
Hsp70 chaperone blocks α-synuclein oligomer formation via a novel engagement mechanism
Jiahui Tao et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2021)
Human Molecular Chaperone Hsp60 and Its Apical Domain Suppress Amyloid Fibril Formation of α-Synuclein
Hanae Yamamoto et al.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES (2020)
Curcumin Affects HSP60 Folding Activity and Levels in Neuroblastoma Cells
Celeste Caruso Bavisotto et al.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES (2020)
Structural basis for active single and double ring complexes in human mitochondrial Hsp60-Hsp10 chaperonin
Yacob Gomez-Llorente et al.
NATURE COMMUNICATIONS (2020)
The mechanism of Hsp90-induced oligomerizaton of Tau
S. Weickert et al.
SCIENCE ADVANCES (2020)
Molecular Chaperones: A Double-Edged Sword in Neurodegenerative Diseases
Jessica Tittelmeier et al.
FRONTIERS IN AGING NEUROSCIENCE (2020)
Differential scanning fluorimetry (DSF) screen to identify inhibitors of Hsp60 protein-protein interactions
Hao Shao et al.
ORGANIC & BIOMOLECULAR CHEMISTRY (2020)
Heat shock protein 104 (HSP104) chaperones soluble Tau via a mechanism distinct from its disaggregase activity
Xiang Zhang et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2019)
Hsp60 Protects against Amyloid β Oligomer Synaptic Toxicity via Modification of Toxic Oligomer Conformation
Claudia Marino et al.
ACS CHEMICAL NEUROSCIENCE (2019)
Stochasticity of Biological Soft Matter: Emerging Concepts in Intrinsically Disordered Proteins and Biological Phase Separation
Konstantin K. Turoverov et al.
TRENDS IN BIOCHEMICAL SCIENCES (2019)
Inhibition of Aβ1-42 Fibrillation by Chaperonins: Human Hsp60 Is a Stronger Inhibitor than Its Bacterial Homologue GroEL
Silvia Vilasi et al.
ACS CHEMICAL NEUROSCIENCE (2019)
Protein moonlighting: what is it, and why is it important?
Constance J. Jeffery
PHILOSOPHICAL TRANSACTIONS OF THE ROYAL SOCIETY B-BIOLOGICAL SCIENCES (2018)
Physicochemical Properties of the Mammalian Molecular Chaperone HSP60
Ryuichi Ishida et al.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES (2018)
Heat Shock Proteins in Alzheimer's Disease: Role and Targeting
Claudia Campanella et al.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES (2018)
Chaperonin of Group I: Oligomeric Spectrum and Biochemical and Biological Implications
Silvia Vilasi et al.
FRONTIERS IN MOLECULAR BIOSCIENCES (2018)
Chaperone-client interactions: Non-specificity engenders multifunctionality
Philipp Koldewey et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2017)
The dissociation of the Hsp60/pro-Caspase-3 complex by bis(pyridyl)oxadiazole copper complex (CubipyOXA) leads to cell death in NCI-H292 cancer cells
Celeste Caruso Bavisotto et al.
JOURNAL OF INORGANIC BIOCHEMISTRY (2017)
Doxorubicin anti-tumor mechanisms include Hsp60 post-translational modifications leading to the Hsp60/p53 complex dissociation and instauration of replicative senescence
Antonella Marino Gammazza et al.
CANCER LETTERS (2017)
Hsp60, amateur chaperone in amyloid-beta fibrillogenesis
Maria Rosalia Mangione et al.
BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS (2016)
In vivo aspects of protein folding and quality control
David Balchin et al.
SCIENCE (2016)
The GroEL-GroES Chaperonin Machine: A Nano-Cage for Protein Folding
Manajit Hayer-Hartl et al.
TRENDS IN BIOCHEMICAL SCIENCES (2016)
Kinetic analysis reveals the diversity of microscopic mechanisms through which molecular chaperones suppress amyloid formation
Paolo Arosio et al.
NATURE COMMUNICATIONS (2016)
Intrinsically Disordered Energy Landscapes
Yassmine Chebaro et al.
SCIENTIFIC REPORTS (2015)
Small heat-shock proteins: important players in regulating cellular proteostasis
Teresa M. Treweek et al.
CELLULAR AND MOLECULAR LIFE SCIENCES (2015)
Cytosolic Hsp60 Can Modulate Proteasome Activity in Yeast
Bella Kalderon et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2015)
Classification of Intrinsically Disordered Regions and Proteins
Robin van der Lee et al.
CHEMICAL REVIEWS (2014)
Human Hsp60 with Its Mitochondrial Import Signal Occurs in Solution as Heptamers and Tetradecamers Remarkably Stable over a Wide Range of Concentrations
Silvia Vilasi et al.
PLOS ONE (2014)
Chaperonin 60: a paradoxical, evolutionarily conserved protein family with multiple moonlighting functions
Brian Henderson et al.
BIOLOGICAL REVIEWS (2013)
Chaperone machines for protein folding, unfolding and disaggregation
Helen Saibil
NATURE REVIEWS MOLECULAR CELL BIOLOGY (2013)
Conditional disorder in chaperone action
James C. A. Bardwell et al.
TRENDS IN BIOCHEMICAL SCIENCES (2012)
Understanding protein non-folding
Vladimir N. Uversky et al.
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS (2010)
The MitCHAP-60 Disease Is Due to Entropic Destabilization of the Human Mitochondrial Hsp60 Oligomer
Avital Parnas et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2009)
Hsp60 expression, new locations, functions and perspectives for cancer diagnosis and therapy
Francesco Cappello et al.
CANCER BIOLOGY & THERAPY (2008)
How do proteins interact?
David D. Boehr et al.
SCIENCE (2008)
Cytosolic accumulation of HSP60 during apoptosis with or without apparent mitochondrial release - Evidence that its pro-apoptotic or pro-survival functions involve differential interactions with caspase
Dhyan Chandra et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2007)
Role of solvation barriers in protein kinetic stability
David Rodriguez-Larrea et al.
JOURNAL OF MOLECULAR BIOLOGY (2006)
GroEL stability and function -: Contribution of the ionic interactions at the inter-ring contact sites
B Sot et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2003)
Intrinsic disorder and protein function
AK Dunker et al.
BIOCHEMISTRY (2002)
The effect of nucleotides and mitochondrial chaperonin 10 on the structure and chaperone activity of mitochondrial chaperonin 60
G Levy-Rimler et al.
EUROPEAN JOURNAL OF BIOCHEMISTRY (2001)
An improved method of preparing the amyloid β-protein for fibrillogenesis and neurotoxicity experiments
Y Fezoui et al.
AMYLOID-JOURNAL OF PROTEIN FOLDING DISORDERS (2000)
分享论文
