ArticleNucleic acids research2010
PROSESS: a protein structure evaluation suite and server.
Article in Nucleic acids research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed.
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- Evolutionary and Structural Assessment of the Human Secreted Frizzled-Related Protein (SFRP) Family.Journal of molecular evolution · 2025Article
- Human small-intestinal gluten-degrading bacteria and its potential implication in celiac disease.Journal of biosciences · 2023Article
- Tick-borne encephalitis virus capsid protein induces translational shutoff as revealed by its structural-biological analysis.The Journal of biological chemistry · 2022Article
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- Cloning, Characterization, Expression Analysis, and Agglutination Studies of Novel Gene Encoding β-D-Galactose, N-Acetyl-D-Glucosamine and Lactose-Binding Lectin from Rice Bean (Vigna umbellata).Molecular biotechnology · 2022Article
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- Defining a novel domain that provides an essential contribution to site-specific interaction of Rep protein with DNA.Nucleic acids research · 2021Article
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- A method for validating the accuracy of NMR protein structures.Nature communications · 2020Article
- Enhancing Catecholase Activity of a Recombinant Human Tyrosinase Through Multiple Strategies.Iranian journal of biotechnology · 2020Article
- Molecular characterization of RNase III protein of Asaia sp. for developing a robust RNAi-based paratransgensis tool to affect the sexual life-cycle of Plasmodium or Anopheles fitness.Parasites & vectors · 2020Article
- Computational Approach for Rational Design of Fusion Uricase with PAS Sequences.International journal of molecular and cellular medicine · 2020Article
- Three genetically distinct ferlaviruses have varying effects on infected corn snakes (Pantherophis guttatus).PloS one · 2019Article
- Structural and dynamic characterization of human Wnt2-Fzd7 complex using computational approaches.Journal of molecular modeling · 2018Article
- Structural insights into the Middle East respiratory syndrome coronavirus 4a protein and its dsRNA binding mechanism.Scientific reports · 2017Article
- The C-terminal domain of TPX2 is made of alpha-helical tandem repeats.BMC structural biology · 2016Article
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- Protein expression, characterization and activity comparisons of wild type and mutant DUSP5 proteins.BMC biochemistry · 2014Article
Corrections and comments
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Authors and funding
11 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
PROSESS (PROtein Structure Evaluation Suite and Server) is a web server designed to evaluate and validate protein structures generated by X-ray crystallography, NMR spectroscopy or computational modeling. While many structure evaluation packages have been developed over the past 20 years, PROSESS is unique in its comprehensiveness, its capacity to evaluate X-ray, NMR and predicted structures as well as its ability to evaluate a variety of experimental NMR data. PROSESS integrates a variety of previously developed, well-known and thoroughly tested methods to evaluate both global and residue specific: (i) covalent and geometric quality; (ii) non-bonded/packing quality; (iii) torsion angle quality; (iv) chemical shift quality and (v) NOE quality. In particular, PROSESS uses VADAR for coordinate, packing, H-bond, secondary structure and geometric analysis, GeNMR for calculating folding, threading and solvent energetics, ShiftX for calculating chemical shift correlations, RCI for correlating structure mobility to chemical shift and PREDITOR for calculating torsion angle-chemical shifts agreement. PROSESS also incorporates several other programs including MolProbity to assess atomic clashes, Xplor-NIH to identify and quantify NOE restraint violations and NAMD to assess structure energetics. PROSESS produces detailed tables, explanations, structural images and graphs that summarize the results and compare them to values observed in high-quality or high-resolution protein structures. Using a simplified red-amber-green coloring scheme PROSESS also alerts users about both general and residue-specific structural problems. PROSESS is intended to serve as a tool that can be used by structure biologists as well as database curators to assess and validate newly determined protein structures. PROSESS is freely available at http://www.prosess.ca.
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