High throughput protein fold identification by using experimental constraints derived from intramolecular cross-links and mass spectrometry

By M. Young, Ning Tang, J. Hempel, C. M. Oshiro, E. W. Taylor, Irwin D. Kuntz, B. Gibson, G. Dollinger. Proc. Natl. Acad. Sci. USA, 2000

439 citations recorded by the source corpus.

Subfields: Molecular Biology, Spectroscopy

View Paper: https://www.semanticscholar.org/paper/47f664efe54f7d4c76ad9542b90f2476c0d0b2b6

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Molecular Biology

In Spectroscopy

Citations in the corpus

Probing Native Protein Structures by Chemical Cross-linking, Mass Spectrometry, and Bioinformatics (2010, background): “The concept of protein cross-linking as a (bio)chemical tool to infer structural information about protein conformations and protein-protein interactions in combination with mass spectrometry was introduced at the end of the 1990s (1).”
Outcome of the First wwPDB Hybrid/Integrative Methods Task Force Workshop (2015, neutral): “, 2000), chemical crosslinks (Young et al., 2000), or even chemical shift data alone (Shen et al.”
Crosslinking combined with mass spectrometry for structural proteomics. (2010, background): “Moremodest tasks such as detecting conformers of a single protein or protein fold recognition, as has been illustrated conceptually for the application of crosslinking combined with mass spectrometry data for protein structure analysis (Young et al., 2000), and would be appropriate for when only a f”
The beginning of a beautiful friendship: cross-linking/mass spectrometry and modelling of proteins and multi-protein complexes (2010, methodology): “Accordingly, cross-linked amino acids were identified and used as distance constraints in conjunction with threading to determine the fold of a protein or protein domain (Young et al., 2000).”
Serum Albumin Domain Structures in Human Blood Serum by Mass Spectrometry and Computational Biology (2015, methodology): “Earlier studies used cross-link data to build monomer structure models by threading and homology modeling (18, 19), which requires homologous template structures in the Protein Data Bank.”
Defining an Essence of Structure Determining Residue Contacts in Proteins (2009, background): “From a sufficient number of such experimentally derived constraints, the tertiary structure of the protein can be identified [6].”
Blind testing of cross‐linking/mass spectrometry hybrid methods in CASP11 (2016, methodology): “11,12,17,22,24 It should also be mentioned that CLMS data—at least in this very first inclusion in CASP—did not yet provide a significant advance for the field as a whole.”