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Structure of a human common cold virus and functional relationship to other picornaviruses
- M. Rossmann, E. Arnold, G. Vriend
- BiologyNature
- 12 September 1985
We report the first atomic resolution structure of an animal virus, human rhinovirus 14. It is strikingly similar to known icosahedral plant RNA viruses. Four neutralizing immunogenic regions have…
Quality control of protein models : directional atomic contact analysis
Branden & Jones state, in Nature: `Protein crystallography is an exacting trade, and the results may contain errors that are difficult to identify. It is the crystallographer's responsibility to make…
New POU dimer configuration mediates antagonistic control of an osteopontin preimplantation enhancer by Oct-4 and Sox-2.
- V. Botquin, H. Hess, H. Schöler
- BiologyGenes & development
- 1 July 1998
The POU transcription factor Oct-4 is expressed specifically in the germ line, pluripotent cells of the pregastrulation embryo and stem cell lines derived from the early embryo. Osteopontin (OPN) is…
Prediction of protein conformational freedom from distance constraints
- B. L. de Groot, D. V. van Aalten, R. Scheek, A. Amadei, G. Vriend, H. Berendsen
- BiologyProteins
- 1 October 1997
TLDR
Rubredoxin reductase of Pseudomonas oleovorans. Structural relationship to other flavoprotein oxidoreductases based on one NAD and two FAD fingerprints.
- G. Eggink, H. Engel, G. Vriend, P. Terpstra, B. Witholt
- Biology, ChemistryJournal of molecular biology
- 1 March 1990
The site of attachment in human rhinovirus 14 for antiviral agents that inhibit uncoating.
TLDR
Generic GPCR residue numbers - aligning topology maps while minding the gaps.
- V. Ísberg, C. de Graaf, D. Gloriam
- BiologyTrends in pharmacological sciences
- 2015
Synergism with the Coactivator OBF-1 (OCA-B, BOB-1) Is Mediated by a Specific POU Dimer Configuration
- A. Tomilin, A. Reményi, H. Schöler
- BiologyCell
- 8 December 2000
Positioning hydrogen atoms by optimizing hydrogen‐bond networks in protein structures
- R. Hooft, Chris Sander, G. Vriend
- ChemistryProteins
- 1 December 1996
A method is presented that positions polar hydrogen atoms in protein structures by optimizing the total hydrogen bond energy. For this goal, an empirical hydrogen bond force field was derived from…
Refined 1.83 A structure of trypanosomal triosephosphate isomerase crystallized in the presence of 2.4 M-ammonium sulphate. A comparison with the structure of the trypanosomal triosephosphate…
- R. Wierenga, M. Noble, G. Vriend, S. Nauche, W. Hol
- ChemistryJournal of molecular biology
- 1 August 1991
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