Analysis of proteins and proteomes by mass spectrometry.

By M. Mann, Ronald C. Hendrickson, A. Pandey. Annual Review of Biochemistry, 2001

1,191 citations recorded by the source corpus.

Subfields: Molecular Biology, Spectroscopy

View Paper: https://www.semanticscholar.org/paper/01dc2ca1523ec24d37e41dae7adb873b3d3ae270

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Citations in the corpus

Compatibility of plant protein extraction methods with mass spectrometry for proteome analysis (2009, background): “The identity of fewer protein spots from gels with Methods C and D can be attributed to impurities in protein samples [26,27], and is not directly related to spot intensity.”
Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry (2002, methodology): “With the advent of ultrasensitive mass spectrometric protein identification methods, it is feasible to identify directly protein complexes on a proteome-wide scal”
High-throughput peptide mass fingerprinting of soybean seed proteins: automated workflow and utility of UniGene expressed sequence tag databases for protein identification. (2004, neutral): “Although PMF is a facile approach well-suited for au- tomation it is strongly dependent upon high quality protein databases for making accurate assignments (Cottrell, 1994; Wilkins et al., 1995; Mann et al., 2001).”
Associating Genes and Protein Complexes with Disease via Network Propagation (2010, methodology): “2: The co-IP paradigm (figure taken from [14]).”
Metabolomics by numbers: acquiring and understanding global metabolite data. (2004, neutral): “To measure the amount of, say, a specific fructose 1,6-bisphosphatase from different organisms, one has to know a priori the DNA sequences or protein sequences (plus post-translational modifications) from each organism to design suitable complementary oligonucleotides to capture mRNA on a nucleotide”
Physiology and molecular biology of stress tolerance in plants (2006, background): “MS is a high throughput technique making possible the analysis of hundreds of proteins in short time and with picomole amounts of protein (Burlingame et al., 1996; Blackstock and Mann, 2001; Mann et al., 2001; Mann and Pandey, 2001).”
Mimicking cellular sorting improves prediction of subcellular localization. (2005, background): “The importance of post-translational modifications in altering these sequence signals as a means to increase the “fitness” for other compartments might explain the difference between these two extreme opposite perceptions of proteins as native to “one native compartment” and as “frequent travelers b”