Protein Regulation by Intrinsically Disordered Regions: A Role for Subdomains in the IDR of the HIV-1 Rev Protein
Published 2018 View Full Article
- Home
- Publications
- Publication Search
- Publication Details
Title
Protein Regulation by Intrinsically Disordered Regions: A Role for Subdomains in the IDR of the HIV-1 Rev Protein
Authors
Keywords
-
Journal
CHEMBIOCHEM
Volume -, Issue -, Pages -
Publisher
Wiley
Online
2018-05-24
DOI
10.1002/cbic.201800192
References
Ask authors/readers for more resources
Related references
Note: Only part of the references are listed.- Amyloid-β adopts a conserved, partially folded structure upon binding to zwitterionic lipid bilayers prior to amyloid formation
- (2016) Kyle J. Korshavn et al. CHEMICAL COMMUNICATIONS
- Fuzzy complexes: Specific binding without complete folding
- (2015) Rashmi Sharma et al. FEBS LETTERS
- The multifaceted roles of intrinsic disorder in protein complexes
- (2015) Vladimir N. Uversky FEBS LETTERS
- Intrinsically Disordered Proteins and Intrinsically Disordered Protein Regions
- (2014) Christopher J. Oldfield et al. Annual Review of Biochemistry
- A role of disordered domains in regulating protein oligomerization and stability
- (2014) Ofrah Faust et al. CHEMICAL COMMUNICATIONS
- Under-folded proteins: Conformational ensembles and their roles in protein folding, function, and pathogenesis
- (2013) Vladimir N. Uversky BIOPOLYMERS
- Regulation of ASPP2 Interaction with p53 Core Domain by an Intramolecular Autoinhibitory Mechanism
- (2013) Shahar Rotem-Bamberger et al. PLoS One
- Sweeping Away Protein Aggregation with Entropic Bristles: Intrinsically Disordered Protein Fusions Enhance Soluble Expression
- (2012) Aaron A. Santner et al. BIOCHEMISTRY
- Thermodynamic Dissection of the Intrinsically Disordered N-terminal Domain of Human Glucocorticoid Receptor
- (2012) Jing Li et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Continuous Thermal Collapse of the Intrinsically Disordered Protein Tau Is Driven by Its Entropic Flexible Domain
- (2012) Gabriele Ciasca et al. LANGMUIR
- Chemical Synthesis and Expression of the HIV-1 Rev Protein
- (2011) Peter Siman et al. CHEMBIOCHEM
- Intrinsically disordered proteins from A to Z
- (2011) Vladimir N. Uversky INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY
- Structural Basis for Activation of Calcineurin by Calmodulin
- (2011) Julie Rumi-Masante et al. JOURNAL OF MOLECULAR BIOLOGY
- Intrinsically disordered regions as affinity tuners in protein–DNA interactions
- (2011) Dana Vuzman et al. Molecular BioSystems
- Attributes of short linear motifs
- (2011) Norman E. Davey et al. Molecular BioSystems
- Fuzziness: linking regulation to protein dynamics
- (2011) Monika Fuxreiter Molecular BioSystems
- Understanding protein non-folding
- (2010) Vladimir N. Uversky et al. BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
- Protein binding specificity versus promiscuity
- (2010) Gideon Schreiber et al. CURRENT OPINION IN STRUCTURAL BIOLOGY
- Implications of the HIV-1 Rev dimer structure at 3.2 A resolution for multimeric binding to the Rev response element
- (2010) M. A. DiMattia et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Identification, analysis, and prediction of protein ubiquitination sites
- (2009) Predrag Radivojac et al. PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
- Flexible nets: disorder and induced fit in the associations of p53 and 14-3-3 with their partners
- (2008) Christopher J Oldfield et al. BMC GENOMICS
- The Structure and Interactions of the Proline-rich Domain of ASPP2
- (2008) Shahar Rotem et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Intrinsic disorder in scaffold proteins: Getting more from less
- (2008) Marc S. Cortese et al. PROGRESS IN BIOPHYSICS & MOLECULAR BIOLOGY
- Fuzzy complexes: polymorphism and structural disorder in protein–protein interactions
- (2007) Peter Tompa et al. TRENDS IN BIOCHEMICAL SCIENCES
Add your recorded webinar
Do you already have a recorded webinar? Grow your audience and get more views by easily listing your recording on Peeref.
Upload NowAsk a Question. Answer a Question.
Quickly pose questions to the entire community. Debate answers and get clarity on the most important issues facing researchers.
Get Started