about
Swaposins: circular permutations within genes encoding saposin homologuesTopic pages: PLoS Computational Biology meets WikipediaPrinciples of microRNA-target recognitionIdentification of Drosophila MicroRNA targetsStructure of the full-length HPr kinase/phosphatase from Staphylococcus xylosus at 1.95 A resolution: Mimicking the product/substrate of the phospho transfer reactions.A systematic screen for protein-lipid interactions in Saccharomyces cerevisiaeDissecting the genomic complexity underlying medulloblastomaDILIMOT: discovery of linear motifs in proteins3did: interacting protein domains of known three-dimensional structureGenomics, proteomics and bioinformatics: all in the same boatSystematic discovery of new recognition peptides mediating protein interaction networksSuperTarget and Matador: resources for exploring drug-target relationshipsCrystal structure of an archaeal class I aldolase and the evolution of (betaalpha)8 barrel proteinsProteome survey reveals modularity of the yeast cell machinery.bantam encodes a developmentally regulated microRNA that controls cell proliferation and regulates the proapoptotic gene hid in DrosophilaPredictions without templates: new folds, secondary structure, and contacts in CASP5Combinations of protein-chemical complex structures reveal new targets for established drugsProteome organization in a genome-reduced bacteriumContent disputes in Wikipedia reflect geopolitical instabilityAn organelle-specific protein landscape identifies novel diseases and molecular mechanismsProtein disorder prediction: implications for structural proteomicsMultiple protein sequence alignment from tertiary structure comparison: assignment of global and residue confidence levelsAnimal MicroRNAs confer robustness to gene expression and have a significant impact on 3'UTR evolutionWD40 proteins propel cellular networks.Interactions between the Fyn SH3-domain and adaptor protein Cbp/PAG derived ligands, effects on kinase activity and affinity.The limits of protein secondary structure prediction accuracy from multiple sequence alignment.Predicting function from structure: examples of the serine protease inhibitor canonical loop conformation found in extracellular proteins.Classification of protein folds.Structural similarity to link sequence space: new potential superfamilies and implications for structural genomics.A structural perspective on protein-protein interactions.Mechismo: predicting the mechanistic impact of mutations and modifications on molecular interactions.Modular architecture of nucleotide-binding pockets.Insights into cancer severity from biomolecular interaction mechanisms.Structural features can be unconserved in proteins with similar folds. An analysis of side-chain to side-chain contacts secondary structure and accessibility.Computational identification of novel amino-acid interactions in HIV Gag via correlated evolution.Protein fold recognition by mapping predicted secondary structures.Detection of protein three-dimensional side-chain patterns: new examples of convergent evolution.Combining specificity determining and conserved residues improves functional site predictionSubunit architecture of intact protein complexes from mass spectrometry and homology modeling.Accurate prediction of peptide binding sites on protein surfaces.
P50
Q21045384-01ADD850-826A-42B5-86E0-00896BD7D73FQ21092570-312BBBE2-9A25-436D-B66C-68464E32BF38Q21146368-03B9C798-04C6-4813-9535-A9058E5FBDF2Q21146437-2B208CD2-9ED0-491E-8A9B-125A20E0A340Q24531444-F0915BFD-01A0-45A4-87C8-4722157D1619Q24621326-6E936209-5297-4D60-B707-3D8BDC58F0CFQ24621907-4B6CD4C7-5617-4E65-B11A-8C1C87ADD435Q24680237-157203A3-2E64-4F46-87E9-15914C0A43CEQ24793936-3BFF12CA-AF9E-40E1-99B6-76DB9E5A01F6Q24806254-3BF39980-EF20-4C84-88D5-97BB9FD66D97Q24817114-40E46F3F-60CD-48A8-A21B-5797741B2683Q27136964-035759FA-F476-46E7-BFB3-76C5F1EFD273Q27641913-7FCF41E6-871F-43DE-AA23-93B6F25285D7Q27929510-024C9FAF-4162-4835-B96E-D2B9D296D48AQ28131827-0CF85F61-62DD-47B3-9AE5-5EFD76514331Q28212631-C1E13766-E1DA-418E-9940-C844C3A26F9CQ28478053-1FC7BE96-EBAA-49E7-973D-D721A4F83248Q28484727-665A289E-B214-4FFA-80CF-FB2934EEF8A2Q28743342-32A42A0F-93CC-4713-8381-75ACBD867C02Q29147481-48507D81-8D9C-409F-978F-4F3DEDAEACCFQ29615736-8AF2DC06-9E61-4C8D-BB52-1F09151149D7Q29615743-2D89FC0C-4A06-4964-B4D1-79359A2605BAQ29616370-EF3B3499-E989-4584-928B-6326D83B65FAQ30156873-DC44A437-6F72-4B41-B3DF-94D6D89BFC03Q30157613-4B95476C-853B-4054-A5FF-A4512AC8CFBCQ30194628-EC00D64B-B2B2-4070-99A3-0FC399128F7FQ30329327-3D7BEDF4-AD64-4E4D-92FE-F27C53D5535DQ30329804-238FB998-5F02-4CD7-8725-6336D886787FQ30330199-FDFF68CC-5DFB-493F-9962-98C91F7C9F43Q30341837-DDDE63D6-07B2-4018-8C81-5D79F6758155Q30368617-8CFD6CCF-9F94-44B1-93EA-2759629C9D32Q30386066-14477BFC-A105-4E0D-947F-96461D49D144Q30393703-E18B08AB-6B4D-4A55-8609-CD4617995657Q30420113-5AD9D627-F807-46E6-B5C3-172782E4033AQ30420213-F426EA67-EE15-41D3-89E8-6F6546E428F1Q30424108-C5022B65-B874-42F9-9935-742519BAF7DBQ30430831-8E65A55E-1C4E-458B-8EB3-0F7B2A26FF03Q30488780-B11D3784-A133-4E9A-9F92-6095F9271692Q33322101-AB78451B-99EC-45BC-A228-425AB057D292Q33422930-68659EEE-0EDA-42AD-8F1A-6A0945FA16BB
P50
description
hulumtues
@sq
researcher
@en
ricercatore
@it
wetenschapper
@nl
հետազոտող
@hy
name
Robert B. Russell
@ast
Robert B. Russell
@en
Robert B. Russell
@es
Robert B. Russell
@nl
Robert B. Russell
@sl
type
label
Robert B. Russell
@ast
Robert B. Russell
@en
Robert B. Russell
@es
Robert B. Russell
@nl
Robert B. Russell
@sl
altLabel
Rob
@en
Robert B Russell
@en
Robert Bruce Russell
@en
Russell RB
@en
prefLabel
Robert B. Russell
@ast
Robert B. Russell
@en
Robert B. Russell
@es
Robert B. Russell
@nl
Robert B. Russell
@sl
P108
P214
P106
P21
P214
P2456
P31
P4012
P496
0000-0002-7213-1398
P734
P735
P7859
viaf-217554459