From words to literature in structural proteomics View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2003-03

AUTHORS

Andrej Sali, Robert Glaeser, Thomas Earnest, Wolfgang Baumeister

ABSTRACT

Technical advances on several frontiers have expanded the applicability of existing methods in structural biology and helped close the resolution gaps between them. As a result, we are now poised to integrate structural information gathered at multiple levels of the biological hierarchy — from atoms to cells — into a common framework. The goal is a comprehensive description of the multitude of interactions between molecular entities, which in turn is a prerequisite for the discovery of general structural principles that underlie all cellular processes. More... »

PAGES

216-225

References to SciGraph publications

  • 1999-11. Protein interaction maps for complete genomes based on gene fusion events in NATURE
  • 2002-01. Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry in NATURE
  • 1997-03. Determination of the fold of the core protein of hepatitis B virus by electron cryomicroscopy in NATURE
  • 2001-11-05. Correlation between transcriptome and interactome mapping data from Saccharomyces cerevisiae in NATURE GENETICS
  • 1998-01. Structure of the αβ tubulin dimer by electron crystallography in NATURE
  • 2000-11. A new era in NATURE STRUCTURAL & MOLECULAR BIOLOGY
  • 1999-11. Identification of in vivo substrates of the chaperonin GroEL in NATURE
  • 1999-10. Structural genomics: beyond the Human Genome Project in NATURE GENETICS
  • 2000-10. Structural determinants of water permeation through aquaporin-1 in NATURE
  • 2000-06. Genomics, gene expression and DNA arrays in NATURE
  • 1998-09. Mass spectrometry and EST-database searching allows characterization of the multi-protein spliceosome complex in NATURE GENETICS
  • 2002-03. Nmr in drug discovery in NATURE REVIEWS DRUG DISCOVERY
  • 1997-03. Visualization of a 4-helix bundle in the hepatitis B virus capsid by cryo-electron microscopy in NATURE
  • 2002-06. The society of proteins in NATURE
  • 2001-06. Completeness in structural genomics in NATURE STRUCTURAL & MOLECULAR BIOLOGY
  • 1999-11. A combined algorithm for genome-wide prediction of protein function in NATURE
  • 2002-01. Protein complexes take the bait in NATURE
  • 2000-11. Automation of X-ray crystallography in NATURE STRUCTURAL & MOLECULAR BIOLOGY
  • 2000-02. A comprehensive analysis of protein–protein interactions in Saccharomyces cerevisiae in NATURE
  • 2002-01. Functional organization of the yeast proteome by systematic analysis of protein complexes in NATURE
  • 2002-07. NMR analysis of a 900K GroEL–GroES complex in NATURE
  • 1994-02. Atomic model of plant light-harvesting complex by electron crystallography in NATURE
  • 1996-03. Molecular docking programs successfully predict the binding of a β-lactamase inhibitory protein to TEM-1 β-lactamase in NATURE STRUCTURAL & MOLECULAR BIOLOGY
  • 2000-09. Structure of the 30S ribosomal subunit in NATURE
  • 2002-05-08. Comparative assessment of large-scale data sets of protein–protein interactions in NATURE
  • Journal

    TITLE

    Nature

    ISSUE

    6928

    VOLUME

    422

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/nature01513

    DOI

    http://dx.doi.org/10.1038/nature01513

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1034051355

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/12634795


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    39 schema:description Technical advances on several frontiers have expanded the applicability of existing methods in structural biology and helped close the resolution gaps between them. As a result, we are now poised to integrate structural information gathered at multiple levels of the biological hierarchy — from atoms to cells — into a common framework. The goal is a comprehensive description of the multitude of interactions between molecular entities, which in turn is a prerequisite for the discovery of general structural principles that underlie all cellular processes.
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