Alexander Schug

Molecular Biology · 2009–2017

A researcher in the Science corpus: 6 papers; trusts 13 researchers and is trusted by 9 researchers here, as inferred from the citation graph.

Subfields

• Molecular Biology — 130 citations into it; #4,040 of 17,773 by trust here, #5,405 by citations
• Genetics — 49 citations into it; #1,663 of 6,854 by trust here, #1,511 by citations
• Computational Biology & Bioinformatics — 48 citations into it
• Materials Chemistry — 34 citations into it; #4,922 of 11,513 by trust here, #7,718 by citations
• Spectroscopy — 15 citations into it

Whom Alexander Schug trusts overall

Their strongest outbound trust, strongest first, inferred from their citations.

1. Martin Weigt
2. J. Hoch
3. Junmei Wang
4. Robert A. H. White
5. W. L. Jorgensen
6. H. Szurmant
7. José N. Onuchic
8. D. van der Spoel
9. Terence Hwa
10. Robert C. Edgar

Who trusts Alexander Schug overall

1. Ryan R. Cheng
2. Martin Weigt
3. Faruck Morcos
4. Guido Uguzzoni
5. Matteo Figliuzzi
6. A. E. Dago
7. H. Szurmant
8. Tatjana Braun
9. Shalini John Lovis
10. Sergey Ovchinnikov

Papers from Alexander Schug's perspective

Ordered by how strongly the researchers Alexander Schug trusts endorse each paper. Same corpus, a different order for every researcher.

1. The Pfam protein families database
2. Identification of direct residue contacts in protein–protein interaction by message passing
3. Direct-coupling analysis of residue coevolution captures native contacts across many protein families
4. Two-component and phosphorelay signal transduction.
5. Biological Sequence Analysis: Probabilistic Models of Proteins and Nucleic Acids
6. MUSCLE: a multiple sequence alignment method with reduced time and space complexity
7. Comparison of simple potential functions for simulating liquid water
8. Accurate prediction of protein–protein interactions from sequence alignments using a Bayesian method
9. Protein 3D Structure Computed from Evolutionary Sequence Variation
10. Molecular dynamics: survey of methods for simulating the activity of proteins. (Chemical Reviews)

Their papers

• High-resolution protein complexes from integrating genomic information with molecular simulation (2009) — 149 citations
• Structural basis of histidine kinase autophosphorylation deduced by integrating genomics, molecular dynamics, and mutagenesis (2012) — 143 citations
• Computational modeling of phosphotransfer complexes in two-component signaling. (2010) — 19 citations
• Coevolutionary Landscape Inference and the Context-Dependence of Mutations in Beta-Lactamase TEM-1 (2015) — 252 citations
• Large-scale identification of coevolution signals across homo-oligomeric protein interfaces by direct coupling analysis (2017) — 97 citations
• An All-atom Structure-Based Potential for Proteins: Bridging Minimal Models with All-atom Empirical Forcefields (2009) — 357 citations