Kinetic versus thermodynamic control of mutational effects on protein homeostasis: A perspective from computational modeling and experiment

Regulated Proteolysis in Bacteria

(2018) Samar A. Mahmoud et al.   Annual Review of Biochemistry

Thermal proteome profiling in bacteria: probing protein state in vivo

(2018) André Mateus et al.   Molecular Systems Biology

How Do Chaperones Protect a Cell's Proteins from Oxidative Damage?

(2018) Mantu Santra et al.   Cell Systems

Tafamidis Treatment for Patients with Transthyretin Amyloid Cardiomyopathy

(2018) Mathew S. Maurer et al.   NEW ENGLAND JOURNAL OF MEDICINE

Recent advances in the structural and mechanistic aspects of Hsp70 molecular chaperones

(2018) Matthias P Mayer et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Ligand-promoted protein folding by biased kinetic partitioning

(2017) Karan S Hingorani et al.   Nature Chemical Biology

Bacterial proteostasis balances energy and chaperone utilization efficiently

(2017) Mantu Santra et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Cell-wide analysis of protein thermal unfolding reveals determinants of thermostability

(2017) Pascal Leuenberger et al.   SCIENCE

Regulating Secretory Proteostasis through the Unfolded Protein Response: From Function to Therapy

(2017) Lars Plate et al.   TRENDS IN CELL BIOLOGY

Treatment of Fabry’s Disease with the Pharmacologic Chaperone Migalastat

(2016) Dominique P. Germain et al.   NEW ENGLAND JOURNAL OF MEDICINE

Hsp70 biases the folding pathways of client proteins

(2016) Ashok Sekhar et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Small molecule proteostasis regulators that reprogram the ER to reduce extracellular protein aggregation

(2016) Lars Plate et al.   eLife

How Hsp70 Molecular Machines Interact with Their Substrates to Mediate Diverse Physiological Functions

(2015) Eugenia M. Clerico et al.   JOURNAL OF MOLECULAR BIOLOGY

Transthyretin (ATTR) amyloidosis: clinical spectrum, molecular pathogenesis and disease-modifying treatments

(2015) Yoshiki Sekijima   JOURNAL OF NEUROLOGY NEUROSURGERY AND PSYCHIATRY

The quantitative and condition-dependent Escherichia coli proteome

(2015) Alexander Schmidt et al.   NATURE BIOTECHNOLOGY

Proteostasis control by the unfolded protein response

(2015) Claudio Hetz et al.   NATURE CELL BIOLOGY

Targeting protein aggregation for the treatment of degenerative diseases

(2015) Yvonne S. Eisele et al.   NATURE REVIEWS DRUG DISCOVERY

Mapping the conformation of a client protein through the Hsp70 functional cycle

(2015) Ashok Sekhar et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Individual and Collective Contributions of Chaperoning and Degradation to Protein Homeostasis in E. coli

(2015) Younhee Cho et al.   Cell Reports

Quantification of Transthyretin Kinetic Stability in Human Plasma Using Subunit Exchange

(2014) Irit Rappley et al.   BIOCHEMISTRY

GroEL/ES Chaperonin Modulates the Mechanism and Accelerates the Rate of TIM-Barrel Domain Folding

(2014) Florian Georgescauld et al.   CELL

Molecular chaperones are nanomachines that catalytically unfold misfolded and alternatively folded proteins

(2014) Rayees U. H. Mattoo et al.   CELLULAR AND MOLECULAR LIFE SCIENCES

The amyloid state and its association with protein misfolding diseases

(2014) Tuomas P. J. Knowles et al.   NATURE REVIEWS MOLECULAR CELL BIOLOGY

The network simulation method: a useful tool for locating the kinetic–thermodynamic switching point in complex kinetic schemes

(2014) Manuel Caravaca et al.   PHYSICAL CHEMISTRY CHEMICAL PHYSICS

Proteome Folding Kinetics Is Limited by Protein Halflife

(2014) Taisong Zou et al.   PLoS One

Single-molecule spectroscopy reveals chaperone-mediated expansion of substrate protein

(2014) Ruth Kellner et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Proteostasis impairment in protein-misfolding and -aggregation diseases

(2014) Mark S. Hipp et al.   TRENDS IN CELL BIOLOGY

Protein rescue from aggregates by powerful molecular chaperone machines

(2013) Shannon M. Doyle et al.   NATURE REVIEWS MOLECULAR CELL BIOLOGY

Early Folding Events Protect Aggregation-Prone Regions of a β-Rich Protein

(2013) Ivan L. Budyak et al.   STRUCTURE

Hsp70 chaperone dynamics and molecular mechanism

(2013) Matthias P. Mayer   TRENDS IN BIOCHEMICAL SCIENCES

Stress-Independent Activation of XBP1s and/or ATF6 Reveals Three Functionally Diverse ER Proteostasis Environments

(2013) Matthew D. Shoulders et al.   Cell Reports

Quantifying Chaperone-Mediated Transitions in the Proteostasis Network of E. coli

(2013) Alex Dickson et al.   PLoS Computational Biology

Why and how does native topology dictate the folding speed of a protein?

(2012) Mark Rustad et al.   JOURNAL OF CHEMICAL PHYSICS

The Transthyretin Amyloidoses: From Delineating the Molecular Mechanism of Aggregation Linked to Pathology to a Regulatory-Agency-Approved Drug

(2012) Steven M. Johnson et al.   JOURNAL OF MOLECULAR BIOLOGY

Global analysis of chaperone effects using a reconstituted cell-free translation system

(2012) T. Niwa et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Tafamidis, a potent and selective transthyretin kinetic stabilizer that inhibits the amyloid cascade

(2012) C. E. Bulawa et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

FoldEco: A Model for Proteostasis in E. coli

(2012) Evan T. Powers et al.   Cell Reports

Autophagy: Renovation of Cells and Tissues

(2011) Noboru Mizushima et al.   CELL

Condition-Dependent Cell Volume and Concentration of Escherichia coli to Facilitate Data Conversion for Systems Biology Modeling

(2011) Benjamin Volkmer et al.   PLoS One

A systematic survey of in vivo obligate chaperonin-dependent substrates

(2010) Kei Fujiwara et al.   EMBO JOURNAL

Kinetic and Thermodynamic Aspects of Enzyme Control and Regulation†

(2010) Johann M. Rohwer et al.   JOURNAL OF PHYSICAL CHEMISTRY B

The kinetic parameters and energy cost of the Hsp70 chaperone as a polypeptide unfoldase

(2010) Sandeep K Sharma et al.   Nature Chemical Biology

Intrinsic tryptophans of CRABPI as probes of structure and folding

(2010) Patricia L. Clark et al.   PROTEIN SCIENCE

Biological and Chemical Approaches to Diseases of Proteostasis Deficiency

(2009) Evan T. Powers et al.   Annual Review of Biochemistry

Bimodal protein solubility distribution revealed by an aggregation analysis of the entire ensemble of Escherichia coli proteins

(2009) T. Niwa et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Chaperonin-mediated protein folding: using a central cavity to kinetically assist polypeptide chain folding

(2009) Arthur L. Horwich et al.   QUARTERLY REVIEWS OF BIOPHYSICS

The two faces of protein misfolding: gain- and loss-of-function in neurodegenerative diseases

(2008) Konstanze F Winklhofer et al.   EMBO JOURNAL

Convergence of Molecular, Modeling, and Systems Approaches for an Understanding of the Escherichia coli Heat Shock Response

(2008) E. Guisbert et al.   MICROBIOLOGY AND MOLECULAR BIOLOGY REVIEWS

Chaperonin chamber accelerates protein folding through passive action of preventing aggregation

(2008) A. C. Apetri et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Predicting protein folding rates from geometric contact and amino acid sequence

(2008) Zheng Ouyang et al.   PROTEIN SCIENCE

Adapting Proteostasis for Disease Intervention

(2008) William E. Balch et al.   SCIENCE