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Title: On the nature of the optimal form of the holdase‐type chaperone stress response

Authors:
ORCiD logo [1]
  1. Laboratory of Biochemistry and Genetics NIDDK NIH Bethesda MD USA, Institute for Protein Research Osaka University Suita, Osaka Japan
Publication Date:
Sponsoring Org.:
USDOE
OSTI Identifier:
1564310
Grant/Contract Number:  
DE‐SC0014664
Resource Type:
Publisher's Accepted Manuscript
Journal Name:
FEBS Letters
Additional Journal Information:
Journal Name: FEBS Letters Journal Volume: 594 Journal Issue: 1; Journal ID: ISSN 0014-5793
Publisher:
Wiley Blackwell (John Wiley & Sons)
Country of Publication:
Netherlands
Language:
English

Citation Formats

Hall, Damien. On the nature of the optimal form of the holdase‐type chaperone stress response. Netherlands: N. p., 2019. Web. doi:10.1002/1873-3468.13580.
Hall, Damien. On the nature of the optimal form of the holdase‐type chaperone stress response. Netherlands. doi:10.1002/1873-3468.13580.
Hall, Damien. Thu . "On the nature of the optimal form of the holdase‐type chaperone stress response". Netherlands. doi:10.1002/1873-3468.13580.
@article{osti_1564310,
title = {On the nature of the optimal form of the holdase‐type chaperone stress response},
author = {Hall, Damien},
abstractNote = {},
doi = {10.1002/1873-3468.13580},
journal = {FEBS Letters},
number = 1,
volume = 594,
place = {Netherlands},
year = {2019},
month = {8}
}

Journal Article:
Free Publicly Available Full Text
Publisher's Version of Record
DOI: 10.1002/1873-3468.13580

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Cited by: 2 works
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Works referenced in this record:

Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavine T
journal, March 1989


Roles of the nucleotide exchange factor and chaperone Hsp110 in cellular proteostasis and diseases of protein misfolding
journal, September 2018

  • Yakubu, Unekwu M.; Morano, Kevin A.
  • Biological Chemistry, Vol. 399, Issue 10
  • DOI: 10.1515/hsz-2018-0209

A Quantitative Chaperone Interaction Network Reveals the Architecture of Cellular Protein Homeostasis Pathways
journal, July 2014


Pathways of cellular proteostasis in aging and disease
journal, November 2017

  • Klaips, Courtney L.; Jayaraj, Gopal Gunanathan; Hartl, F. Ulrich
  • The Journal of Cell Biology, Vol. 217, Issue 1
  • DOI: 10.1083/jcb.201709072

How do small single-domain proteins fold?
journal, August 1998


Molecular Chaperones in Cellular Protein Folding: The Birth of a Field
journal, April 2014


Some properties of human small heat shock protein Hsp20 (HspB6)
journal, January 2004


Alpha-crystallin can function as a molecular chaperone.
journal, November 1992


Allosteric Regulation of Hsp70 Chaperones Involves a Conserved Interdomain Linker
journal, October 2006

  • Vogel, Markus; Mayer, Matthias P.; Bukau, Bernd
  • Journal of Biological Chemistry, Vol. 281, Issue 50
  • DOI: 10.1074/jbc.M609020200

Cellular Functions and Mechanisms of Action of Small Heat Shock Proteins
journal, September 2019


Nucleosomes are assembled by an acidic protein which binds histones and transfers them to DNA
journal, October 1978

  • Laskey, R. A.; Honda, B. M.; Mills, A. D.
  • Nature, Vol. 275, Issue 5679
  • DOI: 10.1038/275416a0

Degradation by proteases Lon, Clp and HtrA, of Escherichia coli proteins aggregated in vivo by heat shock; HtrA protease action in vivo and in vitro
journal, November 1996


Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria
journal, February 1989

  • Cheng, Ming Y.; Hartl, F. -Ulrich; Martin, Jörg
  • Nature, Vol. 337, Issue 6208
  • DOI: 10.1038/337620a0

Stabilization of multimeric enzymes: Strategies to prevent subunit dissociation
journal, December 2009


A model of amyloid's role in disease based on fibril fracture
journal, November 2009


The eye lens chaperone  -crystallin forms defined globular assemblies
journal, July 2009

  • Peschek, J.; Braun, N.; Franzmann, T. M.
  • Proceedings of the National Academy of Sciences, Vol. 106, Issue 32
  • DOI: 10.1073/pnas.0902651106

Balance between Folding and Degradation for Hsp90-Dependent Client Proteins: A Key Role for CHIP
journal, September 2010

  • Kundrat, Lenka; Regan, Lynne
  • Biochemistry, Vol. 49, Issue 35
  • DOI: 10.1021/bi100386w

Small heat shock proteins: Simplicity meets complexity
journal, October 2018

  • Haslbeck, Martin; Weinkauf, Sevil; Buchner, Johannes
  • Journal of Biological Chemistry, Vol. 294, Issue 6
  • DOI: 10.1074/jbc.REV118.002809

MEMBRANE PROTEIN FOLDING AND STABILITY: Physical Principles
journal, June 1999


The diversity of the DnaJ/Hsp40 family, the crucial partners for Hsp70 chaperones
journal, September 2006


The Mechanism and Function of Group II Chaperonins
journal, September 2015


Protein–Protein Interactions in the Molecular Chaperone Network
journal, March 2018


Aging and Proteins: What Does Proteostasis Have to Do with Age?
journal, September 2018


Changes in Oligomerization Are Essential for the Chaperone Activity of a Small Heat Shock Protein in Vivo and in Vitro
journal, September 2002

  • Giese, Kim C.; Vierling, Elizabeth
  • Journal of Biological Chemistry, Vol. 277, Issue 48
  • DOI: 10.1074/jbc.M208926200

The weighted sum method for multi-objective optimization: new insights
journal, December 2009

  • Marler, R. Timothy; Arora, Jasbir S.
  • Structural and Multidisciplinary Optimization, Vol. 41, Issue 6
  • DOI: 10.1007/s00158-009-0460-7

The Hsp70 chaperone network
journal, June 2019

  • Rosenzweig, Rina; Nillegoda, Nadinath B.; Mayer, Matthias P.
  • Nature Reviews Molecular Cell Biology, Vol. 20, Issue 11
  • DOI: 10.1038/s41580-019-0133-3

Hsp104, Hsp70, and Hsp40
journal, July 1998


Stress-Activated Chaperones: A First Line of Defense
journal, November 2017


A new look at an old view of denaturant induced protein unfolding
journal, February 2018


Engineered Hsp70 chaperones prevent Aβ42-induced memory impairments in a Drosophila model of Alzheimer’s disease
journal, July 2018

  • Martín-Peña, Alfonso; Rincón-Limas, Diego E.; Fernandez-Fúnez, Pedro
  • Scientific Reports, Vol. 8, Issue 1
  • DOI: 10.1038/s41598-018-28341-w

Hsp26: a temperature-regulated chaperone
journal, December 1999


Macromolecular crowding: qualitative and semiquantitative successes, quantitative challenges
journal, July 2003

  • Hall, Damien; Minton, Allen P.
  • Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, Vol. 1649, Issue 2
  • DOI: 10.1016/S1570-9639(03)00167-5

Effects of inert volume-excluding macromolecules on protein fiber formation. II. Kinetic models for nucleated fiber growth
journal, February 2004


Individual and Collective Contributions of Chaperoning and Degradation to Protein Homeostasis in E. coli
journal, April 2015


Prohibitins act as a membrane-bound chaperone for the stabilization of mitochondrial proteins
journal, June 2000


Denatured States of Proteins
journal, June 1991


Molecular chaperones in protein folding and proteostasis
journal, July 2011

  • Hartl, F. Ulrich; Bracher, Andreas; Hayer-Hartl, Manajit
  • Nature, Vol. 475, Issue 7356
  • DOI: 10.1038/nature10317

How Evolutionary Pressure Against Protein Aggregation Shaped Chaperone Specificity
journal, February 2006

  • Rousseau, Frederic; Serrano, Luis; Schymkowitz, Joost W. H.
  • Journal of Molecular Biology, Vol. 355, Issue 5
  • DOI: 10.1016/j.jmb.2005.11.035

Crystal structure of an Hsp90–nucleotide–p23/Sba1 closed chaperone complex
journal, April 2006

  • Ali, Maruf M. U.; Roe, S. Mark; Vaughan, Cara K.
  • Nature, Vol. 440, Issue 7087
  • DOI: 10.1038/nature04716

Solid-state NMR and SAXS studies provide a structural basis for the activation of αB-crystallin oligomers
journal, August 2010

  • Jehle, Stefan; Rajagopal, Ponni; Bardiaux, Benjamin
  • Nature Structural & Molecular Biology, Vol. 17, Issue 9
  • DOI: 10.1038/nsmb.1891

FoldEco: A Model for Proteostasis in E. coli
journal, March 2012


Proteomic data from human cell cultures refine mechanisms of chaperone-mediated protein homeostasis
journal, February 2013


Differential Scales of Protein Quality Control
journal, March 2014


The crystal structure of the asymmetric GroEL–GroES–(ADP)7 chaperonin complex
journal, August 1997

  • Xu, Zhaohui; Horwich, Arthur L.; Sigler, Paul B.
  • Nature, Vol. 388, Issue 6644
  • DOI: 10.1038/41944

Munc18-1 is a molecular chaperone for α-synuclein, controlling its self-replicating aggregation
journal, September 2016

  • Chai, Ye Jin; Sierecki, Emma; Tomatis, Vanesa M.
  • The Journal of Cell Biology, Vol. 214, Issue 6
  • DOI: 10.1083/jcb.201512016

CryoEM structure of Hsp104 and its mechanistic implication for protein disaggregation
journal, April 2010

  • Lee, S.; Sielaff, B.; Lee, J.
  • Proceedings of the National Academy of Sciences, Vol. 107, Issue 18
  • DOI: 10.1073/pnas.1003572107

Use of Optical Biosensors for the Study of Mechanistically Concerted Surface Adsorption Processes
journal, January 2001


The effects of Tubulin denaturation on the characterization of its polymerization behavior
journal, July 2003


Quantitative proteomics of heat-treated human cells show an across-the-board mild depletion of housekeeping proteins to massively accumulate few HSPs
journal, April 2015

  • Finka, Andrija; Sood, Vishal; Quadroni, Manfredo
  • Cell Stress and Chaperones, Vol. 20, Issue 4
  • DOI: 10.1007/s12192-015-0583-2

Chaperone Activity with a Redox Switch
journal, February 1999


Natively unfolded proteins
journal, February 2005


Heat shock and the sorting of luminal ER proteins.
journal, November 1989


Supervising the fold: functional principles of molecular chaperones.
journal, January 1996


Ageing and vision: structure, stability and function of lens crystallins
journal, November 2004


Macromolecular Crowding Stabilizes the Molten Globule Form of Apomyoglobin with Respect to Both Cold and Heat Unfolding
journal, August 2006

  • McPhie, Peter; Ni, Yi-sheng; Minton, Allen P.
  • Journal of Molecular Biology, Vol. 361, Issue 1
  • DOI: 10.1016/j.jmb.2006.05.075

Recognizing and analyzing variability in amyloid formation kinetics: Simulation and statistical methods
journal, October 2016


Ionic liquids and protein folding—old tricks for new solvents
journal, March 2019


Serum Albumin Prevents Protein Aggregation and Amyloid Formation and Retains Chaperone-like Activity in the Presence of Physiological Ligands
journal, May 2012

  • Finn, Thomas E.; Nunez, Andrea C.; Sunde, Margaret
  • Journal of Biological Chemistry, Vol. 287, Issue 25
  • DOI: 10.1074/jbc.M112.372961

Discovery of molecular chaperones
journal, January 1996


Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and Mg-ATP
journal, December 1989

  • Goloubinoff, Pierre; Christeller, John T.; Gatenby, Anthony A.
  • Nature, Vol. 342, Issue 6252
  • DOI: 10.1038/342884a0

Heparin-dependent aggregation of hen egg white lysozyme reveals two distinct mechanisms of amyloid fibrillation
journal, November 2017

  • Nitani, Ayame; Muta, Hiroya; Adachi, Masayuki
  • Journal of Biological Chemistry, Vol. 292, Issue 52
  • DOI: 10.1074/jbc.M117.813097

Role of sHsps in organizing cytosolic protein aggregation and disaggregation
journal, January 2017


A new puffing pattern induced by temperature shock and DNP in drosophila
journal, December 1962


The Dynamics of Hsp25 Quaternary Structure: STRUCTURE AND FUNCTION OF DIFFERENT OLIGOMERIC SPECIES
journal, May 1999

  • Ehrnsperger, Monika; Lilie, Hauke; Gaestel, Matthias
  • Journal of Biological Chemistry, Vol. 274, Issue 21
  • DOI: 10.1074/jbc.274.21.14867

Beyond Transcription—New Mechanisms for the Regulation of Molecular Chaperones
journal, January 2004

  • Winter, Jeannette; Jakob, Ursula
  • Critical Reviews in Biochemistry and Molecular Biology, Vol. 39, Issue 5-6
  • DOI: 10.1080/10409230490900658

A thermodynamic approach to the problem of stabilization of globular protein structure: A calorimetric study
journal, July 1974


Absolute protein quantification of the yeast chaperome under conditions of heat shock
journal, July 2016

  • Mackenzie, Rebecca J.; Lawless, Craig; Holman, Stephen W.
  • PROTEOMICS, Vol. 16, Issue 15-16
  • DOI: 10.1002/pmic.201500503

Computational modeling of the relationship between amyloid and disease
journal, September 2012


Involvement of ATP in the nuclear and nucleolar functions of the 70 kd heat shock protein.
journal, December 1985


Ligand-promoted protein folding by biased kinetic partitioning
journal, February 2017

  • Hingorani, Karan S.; Metcalf, Matthew C.; Deming, Derrick T.
  • Nature Chemical Biology, Vol. 13, Issue 4
  • DOI: 10.1038/nchembio.2303

Measurement of amyloid formation by turbidity assay—seeing through the cloud
journal, November 2016


The Chemical Biology of Molecular Chaperones—Implications for Modulation of Proteostasis
journal, September 2015

  • Brandvold, Kristoffer R.; Morimoto, Richard I.
  • Journal of Molecular Biology, Vol. 427, Issue 18
  • DOI: 10.1016/j.jmb.2015.05.010

Structural basis of nucleotide exchange and client binding by the Hsp70 cochaperone Bag2
journal, November 2008

  • Xu, Zhen; Page, Richard C.; Gomes, Michelle M.
  • Nature Structural & Molecular Biology, Vol. 15, Issue 12
  • DOI: 10.1038/nsmb.1518

Exploring the Denatured State Ensemble by Single-Molecule Chemo-Mechanical Unfolding: The Effect of Force, Temperature, and Urea
journal, February 2018


Estimation of macromolecule concentrations and excluded volume effects for the cytoplasm of Escherichia coli
journal, December 1991


It takes a dimer to tango: Oligomeric small heat shock proteins dissociate to capture substrate
journal, October 2018

  • Santhanagopalan, Indu; Degiacomi, Matteo T.; Shepherd, Dale A.
  • Journal of Biological Chemistry, Vol. 293, Issue 51
  • DOI: 10.1074/jbc.RA118.005421

The Chaperone Activity and Substrate Spectrum of Human Small Heat Shock Proteins
journal, November 2016

  • Mymrikov, Evgeny V.; Daake, Marina; Richter, Bettina
  • Journal of Biological Chemistry, Vol. 292, Issue 2
  • DOI: 10.1074/jbc.M116.760413

Protein synthesis in salivary glands of Drosophila melanogaster: Relation to chromosome puffs
journal, April 1974

  • Tissiéres, Alfred; Mitchell, Herschel K.; Tracy, Ursula M.
  • Journal of Molecular Biology, Vol. 84, Issue 3
  • DOI: 10.1016/0022-2836(74)90447-1

Sick Chaperones, Cellular Stress, and Disease
journal, October 2005

  • Macario, Alberto J. L.; de Macario, Everly Conway
  • New England Journal of Medicine, Vol. 353, Issue 14
  • DOI: 10.1056/NEJMra050111

The GroEL–GroES Chaperonin Machine: A Nano-Cage for Protein Folding
journal, January 2016

  • Hayer-Hartl, Manajit; Bracher, Andreas; Hartl, F. Ulrich
  • Trends in Biochemical Sciences, Vol. 41, Issue 1
  • DOI: 10.1016/j.tibs.2015.07.009

Hold 'em and fold 'em: chaperones and signal transduction
journal, June 1995


Protein self-association in the cell: a mechanism for fine tuning the level of macromolecular crowding?
journal, October 2005


Effects of inert volume-excluding macromolecules on protein fiber formation. I. Equilibrium models
journal, July 2002


Unified theoretical description of the kinetics of protein aggregation
journal, March 2019


α-Crystallin as a molecular chaperone
journal, January 1999


Calnexin: a membrane-bound chaperone of the endoplasmic reticulum
journal, March 1994

  • Bergeron, John J. M.; Brenner, Michael B.; Thomas, David Y.
  • Trends in Biochemical Sciences, Vol. 19, Issue 3
  • DOI: 10.1016/0968-0004(94)90205-4

Steric Effects on Multivalent Ligand-Receptor Binding: Exclusion of Ligand Sites by Bound Cell Surface Receptors
journal, June 1999


Theory for the folding and stability of globular proteins
journal, March 1985


Principles that Govern the Folding of Protein Chains
journal, July 1973


Effect of Lipid Type on the Binding of Lipid Vesicles to Islet Amyloid Polypeptide Amyloid Fibrils
journal, April 2010

  • Sasahara, Kenji; Hall, Damien; Hamada, Daizo
  • Biochemistry, Vol. 49, Issue 14
  • DOI: 10.1021/bi9019252

Targeting hsp90 family members: A strategy to improve cancer cell death
journal, June 2019

  • Buc Calderon, Pedro; Beck, Raphaël; Glorieux, Christophe
  • Biochemical Pharmacology, Vol. 164
  • DOI: 10.1016/j.bcp.2019.04.010

Toward an understanding of biochemical equilibria within living cells
journal, December 2017


Global Profiling of the Cell Surface Proteome of Cancer Cells Uncovers an Abundance of Proteins with Chaperone Function
journal, December 2002

  • Shin, Bong Kyung; Wang, Hong; Yim, Anne Marie
  • Journal of Biological Chemistry, Vol. 278, Issue 9
  • DOI: 10.1074/jbc.M210455200

Effects of macromolecular crowding on intracellular diffusion from a single particle perspective
journal, February 2010


Modulation and elimination of yeast prions by protein chaperones and co-chaperones.
journal, October 2011


Silent Prions Lying in Wait: A Two-hit Model of Prion/Amyloid Formation and Infection
journal, February 2004


Protein aggregate turbidity: Simulation of turbidity profiles for mixed-aggregation reactions
journal, April 2016


A multi-pathway perspective on protein aggregation: Implications for control of the rate and extent of amyloid formation
journal, January 2015


A Toy Model for Predicting the Rate of Amyloid Formation from Unfolded Protein
journal, August 2005

  • Hall, Damien; Hirota, Nami; Dobson, Christopher M.
  • Journal of Molecular Biology, Vol. 351, Issue 1
  • DOI: 10.1016/j.jmb.2005.05.013

Oligomerization of a molecular chaperone modulates its activity
journal, May 2018


Experimental Milestones in the Discovery of Molecular Chaperones as Polypeptide Unfolding Enzymes
journal, June 2016


Expression profiles of heat shock protein 27 and αB-crystallin and their effects on heat-stressed rat myocardial cells in vitro and in vivo
journal, December 2015

  • Tang, Shu; Chen, Hongbo; Cheng, Yanfen
  • Molecular Medicine Reports, Vol. 13, Issue 2
  • DOI: 10.3892/mmr.2015.4693

Adapting the machine: adaptor proteins for Hsp100/Clp and AAA+ proteases
journal, August 2009

  • Kirstein, Janine; Molière, Noël; Dougan, David A.
  • Nature Reviews Microbiology, Vol. 7, Issue 8
  • DOI: 10.1038/nrmicro2185

Global analysis of chaperone effects using a reconstituted cell-free translation system
journal, May 2012

  • Niwa, T.; Kanamori, T.; Ueda, T.
  • Proceedings of the National Academy of Sciences, Vol. 109, Issue 23
  • DOI: 10.1073/pnas.1201380109

HEAT-SHOCK PROTEINS, MOLECULAR CHAPERONES, AND THE STRESS RESPONSE: Evolutionary and Ecological Physiology
journal, March 1999


Amyloid pores from pathogenic mutations
journal, July 2002

  • Lashuel, Hilal A.; Hartley, Dean; Petre, Benjamin M.
  • Nature, Vol. 418, Issue 6895
  • DOI: 10.1038/418291a

A biosensor-based framework to measure latent proteostasis capacity
journal, January 2018


A Novel Mechanism for Small Heat Shock Proteins to Function as Molecular Chaperones
journal, March 2015

  • Zhang, Kaiming; Ezemaduka, Anastasia N.; Wang, Zhao
  • Scientific Reports, Vol. 5, Issue 1
  • DOI: 10.1038/srep08811

Multi-scale modelling of amyloid formation from unfolded proteins using a set of theory derived rate constants
journal, March 2009


Homologous plant and bacterial proteins chaperone oligomeric protein assembly
journal, May 1988

  • Hemmingsen, Sean M.; Woolford, Carol; van der Vies, Saskia M.
  • Nature, Vol. 333, Issue 6171
  • DOI: 10.1038/333330a0

Thermal denaturation and folding rates of single domain proteins: size matters
journal, January 2004


Disaggregating Chaperones: An Unfolding Story
journal, October 2009

  • Sharma, Sandeep; Christen, Philipp; Goloubinoff, Pierre
  • Current Protein & Peptide Science, Vol. 10, Issue 5
  • DOI: 10.2174/138920309789351930