FuzDB: database of fuzzy complexes, a tool to develop stochastic structure-function relationships for protein complexes and higher-order assemblies
出版年份 2016 全文链接
标题
FuzDB: database of fuzzy complexes, a tool to develop stochastic structure-function relationships for protein complexes and higher-order assemblies
作者
关键词
-
出版物
NUCLEIC ACIDS RESEARCH
Volume 45, Issue D1, Pages D228-D235
出版商
Oxford University Press (OUP)
发表日期
2016-10-22
DOI
10.1093/nar/gkw1019
参考文献
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。- The Structure and Dynamics of Higher-Order Assemblies: Amyloids, Signalosomes, and Granules
- (2016) Hao Wu et al. CELL
- Plasticity of an Ultrafast Interaction between Nucleoporins and Nuclear Transport Receptors
- (2015) Sigrid Milles et al. CELL
- Fuzzy complexes: Specific binding without complete folding
- (2015) Rashmi Sharma et al. FEBS LETTERS
- Intrinsically disordered proteins in cellular signalling and regulation
- (2015) Peter E. Wright et al. NATURE REVIEWS MOLECULAR CELL BIOLOGY
- Structural basis for epitope masking and strain specificity of a conserved epitope in an intrinsically disordered malaria vaccine candidate
- (2015) Rodrigo A. V. Morales et al. Scientific Reports
- Compensatory Adaptations of Structural Dynamics in an Intrinsically Disordered Protein Complex
- (2014) Dennis Kurzbach et al. ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
- Intrinsically Disordered Proteins and Intrinsically Disordered Protein Regions
- (2014) Christopher J. Oldfield et al. Annual Review of Biochemistry
- Classification of Intrinsically Disordered Regions and Proteins
- (2014) Robin van der Lee et al. CHEMICAL REVIEWS
- MobiDB 2.0: an improved database of intrinsically disordered and mobile proteins
- (2014) Emilio Potenza et al. NUCLEIC ACIDS RESEARCH
- Interaction of Nonstructural Protein 5A of the Hepatitis C Virus with Src Homology 3 Domains Using Noncanonical Binding Sites
- (2013) Melanie Schwarten et al. BIOCHEMISTRY
- pE-DB: a database of structural ensembles of intrinsically disordered and of unfolded proteins
- (2013) Mihaly Varadi et al. NUCLEIC ACIDS RESEARCH
- IDEAL in 2014 illustrates interaction networks composed of intrinsically disordered proteins and their binding partners
- (2013) Satoshi Fukuchi et al. NUCLEIC ACIDS RESEARCH
- Interaction of the Eukaryotic Initiation Factor 4E with 4E-BP2 at a Dynamic Bipartite Interface
- (2013) Sabelo Lukhele et al. STRUCTURE
- Intrinsically Disordered Proteins: From Sequence and Conformational Properties toward Drug Discovery
- (2012) Nasrollah Rezaei-Ghaleh et al. CHEMBIOCHEM
- Transient structure and dynamics in the disordered c-Myc transactivation domain affect Bin1 binding
- (2012) Cecilia Andresen et al. NUCLEIC ACIDS RESEARCH
- D2P2: database of disordered protein predictions
- (2012) Matt E. Oates et al. NUCLEIC ACIDS RESEARCH
- Fuzziness: linking regulation to protein dynamics
- (2011) Monika Fuxreiter Molecular BioSystems
- Ensemble modeling of protein disordered states: Experimental restraint contributions and validation
- (2011) Joseph A. Marsh et al. PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
- Tail-Mediated Collapse of HMGB1 Is Dynamic and Occurs via Differential Binding of the Acidic Tail to the A and B Domains
- (2010) Katherine Stott et al. JOURNAL OF MOLECULAR BIOLOGY
- Linking folding and binding
- (2009) Peter E Wright et al. CURRENT OPINION IN STRUCTURAL BIOLOGY
- The Affinity of Ets-1 for DNA is Modulated by Phosphorylation Through Transient Interactions of an Unstructured Region
- (2008) Gregory M. Lee et al. JOURNAL OF MOLECULAR BIOLOGY
- Dynamic equilibrium engagement of a polyvalent ligand with a single-site receptor
- (2008) T. Mittag et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Fuzzy complexes: polymorphism and structural disorder in protein–protein interactions
- (2007) Peter Tompa et al. TRENDS IN BIOCHEMICAL SCIENCES
Discover Peeref hubs
Discuss science. Find collaborators. Network.
Join a conversationAsk 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