about
The Protein Model Portal--a comprehensive resource for protein structure and model informationExpansion and Function of Repeat Domain Proteins During Stress and Development in PlantsThree dimensional electron microscopy and in silico tools for macromolecular structure determinationCrystallographic model validation: from diagnosis to healingStructure ofVibrio choleraeribosome hibernation promoting factorShared resources, shared costs--leveraging biocuration resourcesThe Protein Data Bank archive as an open data resourceThe MIntAct project--IntAct as a common curation platform for 11 molecular interaction databasesOneDep: Unified wwPDB System for Deposition, Biocuration, and Validation of Macromolecular Structures in the PDB ArchiveRepeatsDB: a database of tandem repeat protein structuresModelling three-dimensional protein structures for applications in drug design.Redundancy-weighting for better inference of protein structural features.An algorithm to enumerate all possible protein conformations verifying a set of distance constraintsPrioritization of active antimalarials using structural interaction profile of Plasmodium falciparum enoyl-acyl carrier protein reductase (PfENR)-triclosan derivatives.PDBe: Protein Data Bank in EuropeEMDataBank unified data resource for 3DEM.The evolution of enzyme function in the isomerases.Focused chemical libraries--design and enrichment: an example of protein-protein interaction chemical space.Towards precision medicine: advances in computational approaches for the analysis of human variants2P2Idb v2: update of a structural database dedicated to orthosteric modulation of protein-protein interactions.Octopus: a platform for the virtual high-throughput screening of a pool of compounds against a set of molecular targets.A novel approach to represent and compare RNA secondary structures.Structure-based drug design studies of the interactions of ent-kaurane diterpenes derived from Wedelia paludosa with the Plasmodium falciparum sarco/endoplasmic reticulum Ca²⁺-ATPase PfATP6.X-ray refinement significantly underestimates the level of microscopic heterogeneity in biomolecular crystals.Dependence of protein crystal stability on residue charge states and ion content of crystal solvent.PTMcode v2: a resource for functional associations of post-translational modifications within and between proteins.Bioinformatics Analysis of Functional Associations of PTMs.Overview of the structure-based non-genomic effects of the nuclear receptor RXRαAdvances in Human Biology: Combining Genetics and Molecular Biophysics to Pave the Way for Personalized Diagnostics and Medicine
P2860
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P2860
description
2013 nî lūn-bûn
@nan
2013 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2013 թվականի մարտին հրատարակված գիտական հոդված
@hy
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
name
The future of the Protein Data Bank
@ast
The future of the Protein Data Bank
@en
The future of the Protein Data Bank
@nl
type
label
The future of the Protein Data Bank
@ast
The future of the Protein Data Bank
@en
The future of the Protein Data Bank
@nl
prefLabel
The future of the Protein Data Bank
@ast
The future of the Protein Data Bank
@en
The future of the Protein Data Bank
@nl
P2860
P50
P921
P356
P1433
P1476
The future of the Protein Data Bank
@en
P2860
P304
P356
10.1002/BIP.22132
P407
P577
2013-03-01T00:00:00Z