Diverse functional manifestations of intrinsic structural disorder in molecular chaperones

Order out of Disorder: Working Cycle of an Intrinsically Unfolded Chaperone

(2012) Dana Reichmann et al.   CELL

Structural Disorder in Eukaryotes

(2012) Rita Pancsa et al.   PLoS One

Charged linker sequence modulates eukaryotic heat shock protein 90 (Hsp90) chaperone activity

(2012) S. Tsutsumi et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

LEA Proteins During Water Stress: Not Just for Plants Anymore

(2011) Steven C. Hand et al.   Annual Review of Physiology

Biochemical characterization of small heat shock protein HspB8 (Hsp22)–Bag3 interaction

(2011) Anton A. Shemetov et al.   ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS

Intrinsically disordered proteins as molecular shields

(2011) Sohini Chakrabortee et al.   Molecular BioSystems

Disorder Targets Misorder in Nuclear Quality Control Degradation: A Disordered Ubiquitin Ligase Directly Recognizes Its Misfolded Substrates

(2011) Joel C. Rosenbaum et al.   MOLECULAR CELL

Insights into Maize LEA Proteins: From Proteomics to Functional Approaches

(2011) Imen Amara et al.   PLANT AND CELL PHYSIOLOGY

LEAPdb: a database for the late embryogenesis abundant proteins

(2010) Gilles Hunault et al.   BMC GENOMICS

Hsp12 Is an Intrinsically Unstructured Stress Protein that Folds upon Membrane Association and Modulates Membrane Function

(2010) Sylvia Welker et al.   MOLECULAR CELL

Catalytic and chaperone-like functions in an intrinsically disordered protein associated with desiccation tolerance

(2010) S. Chakrabortee et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Characterization of a group 1 late embryogenesis abundant protein in encysted embryos of the brine shrimp Artemia franciscana

(2009) Michelle A. Sharon et al.   Biochemistry and Cell Biology

Close encounters of the third kind: disordered domains and the interactions of proteins

(2009) Peter Tompa et al.   BIOESSAYS

Thermally induced structural changes of intrinsically disordered small heat shock protein Hsp22

(2009) Alexey S. Kazakov et al.   BIOPHYSICAL CHEMISTRY

Role of the nucleoplasmin 2 C-terminal domain in the formation of nucleolus-like bodies in mouse oocytes

(2009) Azusa Inoue et al.   FASEB JOURNAL

Caseins: Utilizing Molecular Chaperone Properties to Control Protein Aggregation in Foods

(2009) Yie Hui Yong et al.   JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY

A Mechanism for Histone Chaperoning Activity of Nucleoplasmin: Thermodynamic and Structural Models

(2009) Stefka G. Taneva et al.   JOURNAL OF MOLECULAR BIOLOGY

Chaperonin complex with a newly folded protein encapsulated in the folding chamber

(2009) D. K. Clare et al.   NATURE

The large conformational changes of Hsp90 are only weakly coupled to ATP hydrolysis

(2009) Moritz Mickler et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Dissection of the ATP-induced conformational cycle of the molecular chaperone Hsp90

(2009) Martin Hessling et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

MtPM25 is an atypical hydrophobic late embryogenesis-abundant protein that dissociates cold and desiccation-aggregated proteins

(2009) VIRGINIE BOUCHER et al.   PLANT CELL AND ENVIRONMENT

Substrate binding site flexibility of the small heat shock protein molecular chaperones

(2009) N. Jaya et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Structural plasticity of an acid-activated chaperone allows promiscuous substrate binding

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

Intrinsically Disordered Proteins in Human Diseases: Introducing the D2 Concept

(2008) Vladimir N. Uversky et al.   Annual Review of Biophysics

Evaluation of the Protective Activities of a Late Embryogenesis Abundant (LEA) Related Protein, Cor15am, during Various Stressesin Vitro

(2008) Katsuhiro NAKAYAMA et al.   BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY

Chaperone machines in action

(2008) Helen R Saibil   CURRENT OPINION IN STRUCTURAL BIOLOGY

Function and structure of inherently disordered proteins

(2008) A Keith Dunker et al.   CURRENT OPINION IN STRUCTURAL BIOLOGY

Janus chaperones: Assistance of both RNA- and protein-folding by ribosomal proteins

(2008) Denes Kovacs et al.   FEBS LETTERS

Hydrophilic Residues526KNDAAD531in the Flexible C-terminal Region of the Chaperonin GroEL Are Critical for Substrate Protein Folding within the Central Cavity

(2008) Kodai Machida et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

An Unusual Intrinsically Disordered Protein from the Model LegumeLotus japonicusStabilizes Proteinsin Vitro

(2008) Svend Haaning et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

The Hsp90 Chaperone Machinery

(2008) Sebastian Karl Wandinger et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

The Enigmatic LEA Proteins and Other Hydrophilins

(2008) M. Battaglia et al.   PLANT PHYSIOLOGY

Chaperone Activity of ERD10 and ERD14, Two Disordered Stress-Related Plant Proteins

(2008) D. Kovacs et al.   PLANT PHYSIOLOGY