José N. Onuchic
Molecular Biology · 1997–2016
A researcher in the Science corpus: 15 papers; trusts 37 researchers and is trusted by 46 researchers here, as inferred from the citation graph.
Subfields
- Molecular Biology — 204 citations into it; #725 of 17,773 by trust here, #1,398 by citations
- Computational Biology & Bioinformatics — 68 citations into it; #240 of 660 by trust here, #204 by citations
- Genetics — 57 citations into it; #1,365 of 6,854 by trust here, #2,093 by citations
- Materials Chemistry — 40 citations into it; #1,582 of 11,513 by trust here, #4,660 by citations
- Spectroscopy — 29 citations into it
- Atomic and Molecular Physics, and Optics — 15 citations into it; #5,839 of 7,135 by trust here, #6,080 by citations
Whom José N. Onuchic trusts overall
Their strongest outbound trust, strongest first, inferred from their citations.
- Martin Weigt
- Cecilia Clementi
- J. Hoch
- Faruck Morcos
- W. L. Jorgensen
- Debora Marks
- Robert A. H. White
- H. Szurmant
- Yang Zhang
- Alexander Schug
Who trusts José N. Onuchic overall
- Hannah K. Wayment-Steele
- Yaakov Levy
- Ryan R. Cheng
- Faruck Morcos
- Alexander Schug
- Sergey Ovchinnikov
- Martin Weigt
- Joanna I. Sulkowska
- Adedolapo M. Ojoawo
- Anne-Florence Bitbol
Papers from José N. Onuchic's perspective
Ordered by how strongly the researchers José N. Onuchic trusts endorse each paper. Same corpus, a different order for every researcher.
- Identification of direct residue contacts in protein–protein interaction by message passing
- The Pfam protein families database
- Direct-coupling analysis of residue coevolution captures native contacts across many protein families
- Protein 3D Structure Computed from Evolutionary Sequence Variation
- Profile hidden Markov models
- Comparison of simple potential functions for simulating liquid water
- Two-component and phosphorelay signal transduction.
- Correlations among amino acid sites in bHLH protein domains: an information theoretic analysis.
- Accurate prediction of protein–protein interactions from sequence alignments using a Bayesian method
- Accurate de novo structure prediction of large transmembrane protein domains using fragment-assembly and correlated mutation analysis
Their papers
- Direct-coupling analysis of residue coevolution captures native contacts across many protein families (2011) — 1,436 citations
- Genomics-aided structure prediction (2012) — 222 citations
- High-resolution protein complexes from integrating genomic information with molecular simulation (2009) — 149 citations
- Coevolutionary signals across protein lineages help capture multiple protein conformations (2013) — 174 citations
- Computational modeling of phosphotransfer complexes in two-component signaling. (2010) — 19 citations
- An All-atom Structure-Based Potential for Proteins: Bridging Minimal Models with All-atom Empirical Forcefields (2009) — 357 citations
- Topological and energetic factors: what determines the structural details of the transition state ensemble and "en-route" intermediates for protein folding? An investigation for small globular proteins. (2000) — 1,186 citations
- Toward rationally redesigning bacterial two-component signaling systems using coevolutionary information (2014) — 113 citations
- Coevolutionary information, protein folding landscapes, and the thermodynamics of natural selection (2014) — 139 citations
- Water mediation in protein folding and molecular recognition. (2006) — 936 citations
- Folding a protein in a computer: An atomic description of the folding/unfolding of protein A (2003) — 305 citations
- Implications of the Hybrid Epithelial/Mesenchymal Phenotype in Metastasis (2015) — 662 citations
- Faculty Opinions recommendation of Three-dimensional structures of membrane proteins from genomic sequencing. (2016) — 23 citations
- Connecting the Sequence-Space of Bacterial Signaling Proteins to Phenotypes Using Coevolutionary Landscapes (2016) — 55 citations
- Theory of protein folding: the energy landscape perspective. (1997)