Overall Rationale for the Resource The overall rationale for the National Resource for the Mass Spectrometric Analysis of Biological Macromolecules is to develop instrumentation and methodology that facilitates biological and biomedical research;test and apply these developments on important problems of biomedical interest;disseminate our developments to the biomedical community at large;and train scientists in these advanced techniques. Our goal is to push the envelope in terms of sensitivity, accuracy and breadth of application, so that mass spectrometry can be applied more and more broadly for uncovering new biology and become an increasingly important facilitator of biomedical research.

National Institute of Health (NIH)
National Institute of General Medical Sciences (NIGMS)
Biotechnology Resource Grants (P41)
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Special Emphasis Panel (ZRG1-BCMB-H (40))
Program Officer
Sheeley, Douglas
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Rockefeller University
Other Domestic Higher Education
New York
United States
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Subbotin, Roman I; Chait, Brian T (2014) A pipeline for determining protein-protein interactions and proximities in the cellular milieu. Mol Cell Proteomics 13:2824-35
Anand, Prachi; Grigoryan, Alexandre; Bhuiyan, Mohammed H et al. (2014) Sample limited characterization of a novel disulfide-rich venom peptide toxin from terebrid marine snail Terebra variegata. PLoS One 9:e94122
Li, Yinyin; Cross, Frederick R; Chait, Brian T (2014) Method for identifying phosphorylated substrates of specific cyclin/cyclin-dependent kinase complexes. Proc Natl Acad Sci U S A 111:11323-8
Algret, Romain; Fernandez-Martinez, Javier; Shi, Yi et al. (2014) Molecular architecture and function of the SEA complex, a modulator of the TORC1 pathway. Mol Cell Proteomics 13:2855-70
Shi, Yi; Fernandez-Martinez, Javier; Tjioe, Elina et al. (2014) Structural characterization by cross-linking reveals the detailed architecture of a coatomer-related heptameric module from the nuclear pore complex. Mol Cell Proteomics 13:2927-43
Zhong, Yu; Morris, Deanna H; Jin, Lin et al. (2014) Nrbf2 protein suppresses autophagy by modulating Atg14L protein-containing Beclin 1-Vps34 complex architecture and reducing intracellular phosphatidylinositol-3 phosphate levels. J Biol Chem 289:26021-37
Fridy, Peter C; Li, Yinyin; Keegan, Sarah et al. (2014) A robust pipeline for rapid production of versatile nanobody repertoires. Nat Methods 11:1253-60
Cevher, Murat A; Shi, Yi; Li, Dan et al. (2014) Reconstitution of active human core Mediator complex reveals a critical role of the MED14 subunit. Nat Struct Mol Biol 21:1028-34
Holden, Jennifer M; Koreny, Ludek; Obado, Samson et al. (2014) Nuclear pore complex evolution: a trypanosome Mlp analogue functions in chromosomal segregation but lacks transcriptional barrier activity. Mol Biol Cell 25:1421-36
Holden, Jennifer M; Koreny, Ludek; Kelly, Steven et al. (2014) Touching from a distance: Evolution of interplay between the nuclear pore complex, nuclear basket, and the mitotic spindle. Nucleus 5:

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