DOI: 10.1074/mcp.t100003-mcp200. Chemical Approaches for Functionally Probing the Proteome

Chemical Approaches for Functionally Probing the Proteome

10.1074/mcp.t100003-mcp200

Crossref journal-article

Elsevier BV

Molecular & Cellular Proteomics (78)

Bibliography

Greenbaum, D., Baruch, A., Hayrapetian, L., Darula, Z., Burlingame, A., Medzihradszky, K. F., & Bogyo, M. (2002). Chemical Approaches for Functionally Probing the Proteome. Molecular & Cellular Proteomics, 1(1), 60â68.

Authors 7

Doron Greenbaum (first)
Amos Baruch (additional)
Linda Hayrapetian (additional)
Zsuzsanna Darula (additional)
Alma Burlingame (additional)
Katlin F. Medzihradszky (additional)
Matthew Bogyo (additional)

References 26 Referenced 260

10.1038/47048 / Nature / A combined algorithm for genome-wide prediction of protein function by Marcotte (1999)
10.1038/35015694 / Nature / Protein function in the post-genomic era by Eisenberg (2000)
10.1073/pnas.95.25.14863 / Proc. Natl. Acad. Sci. U. S. A. / Cluster analysis and display of genome-wide expression patterns by Eisen (1998)
10.1038/6972 / Nat. Biotechnol. / Proteomics: translating genomics into products? by Dove (1999)
10.1038/35015709 / Nature / Proteomics to study genes and genomes by Pandey (2000)
10.1128/MCB.19.3.1720 / Mol. Cell. Biol. / Correlation between protein and mRNA abundance in yeast by Gygi (1999)
10.1016/S0167-7799(00)01499-2 / Trends Biotechnol. / Frontiers in chemical genetics by Stockwell (2000)
10.1016/S0968-0896(98)00126-6 / Bioorg. Med. Chem. / Chemical genetics resulting from a passion for synthetic organic chemistry by Schreiber (1998)
10.1016/S0969-2126(96)00046-9 / Structure / Structure of rat procathepsin B: model for inhibition of cysteine protease activity by the proregion by Cygler (1996)
10.1002/j.1460-2075.1996.tb00934.x / EMBO J. / Structure of human procathepsin L reveals the molecular basis of inhibition by the prosegment by Coulombe (1996)
10.1146/annurev.physiol.59.1.63 / Annu. Rev. Physiol. / Emerging roles for cysteine proteases in human biology by Chapman (1997)
10.1016/0076-6879(94)44048-4 / Methods Enzymol. / Peptidyl diazomethanes as inhibitors of cysteine and serine proteinases by Shaw (1994)
{'key': '10.1074/mcp.T100003-MCP200_bib13', 'first-page': '113', 'article-title': 'Cathepsin B and human tumor progression', 'volume': '379', 'author': 'Yan', 'year': '1998', 'journal-title': 'Biol. Chem.'} / Biol. Chem. / Cathepsin B and human tumor progression by Yan (1998)
10.1126/science.273.5279.1236 / Science / Pycnodysostosis, a lysosomal disease caused by cathepsin K deficiency by Gelb (1996)
10.1002/art.1780400316 / Arthritis Rheum. / Macrophage cathepsin L, a factor in the erosion of subchondral bone in rheumatoid arthritis by Iwata (1997)
10.1073/pnas.96.26.14694 / Proc. Natl. Acad. Sci. U. S. A. / Activity-based protein profiling: the serine hydrolases by Liu (1999)
10.1021/bi002579j / Biochemistry / Profiling serine hydrolase activities in complex proteomes by Kidd (2001)
10.1016/S1074-5521(00)00061-2 / Chem. Biol. / Selective targeting of lysosomal cysteine proteases with radiolabeled electrophilic substrate analogs by Bogyo (2000)
10.1016/S1074-5521(00)00014-4 / Chem. Biol. / Epoxide electrophiles as activity-dependent cysteine protease profiling and discovery tools by Greenbaum (2000)
10.1093/emboj/16.9.2271 / EMBO J. / Multiple species of CPP32 and Mch2 are the major active caspases present in apoptotic cells by Faleiro (1997)
10.1016/S1074-5521(00)90060-7 / Chem. Biol. / Profiling the specific reactivity of the proteome with non-directed activity-based probes by Adam (2001)
10.1074/jbc.M103628200 / J. Biol. Chem. / Defining a link between gap junction communication, proteolysis, and cataract formation by Baruch (2001)
10.1016/S0968-0896(97)00105-3 / Bioorg. Med. Chem. / E-64 analogues as inhibitors of cathepsin B on the role of the absolute configuration of the epoxysuccinyl group by Schaschke (1997)
10.1002/bip.360341212 / Biopolymers / Peptide libraries: determination of relative reaction rates of protected amino acids in competitive couplings by Ostresh (1994)
10.1016/S1074-5521(98)90169-7 / Chem. Biol. / Substrate binding and sequence preference of the proteasome revealed by active site-directed affinity probes by Bogyo (1998)
10.1073/pnas.061028898 / Proc. Natl. Acad. Sci. U. S. A. / Global analysis of proteasomal substrate specificity using positional-scanning libraries of covalent inhibitors by Nazif (2001)

Dates

Type	When
Created	22 years, 5 months ago (April 2, 2003, 4:49 p.m.)
Deposited	4 years, 1 month ago (July 30, 2021, 1:09 a.m.)
Indexed	1 month, 4 weeks ago (July 7, 2025, 7:25 a.m.)
Issued	23 years, 8 months ago (Jan. 1, 2002)
Published	23 years, 8 months ago (Jan. 1, 2002)
Published Print	23 years, 8 months ago (Jan. 1, 2002)

Funders 0

None

BibTeX

@article{Greenbaum_2002, title={Chemical Approaches for Functionally Probing the Proteome}, volume={1}, ISSN={1535-9476}, url={http://dx.doi.org/10.1074/mcp.t100003-mcp200}, DOI={10.1074/mcp.t100003-mcp200}, number={1}, journal={Molecular & Cellular Proteomics}, publisher={Elsevier BV}, author={Greenbaum, Doron and Baruch, Amos and Hayrapetian, Linda and Darula, Zsuzsanna and Burlingame, Alma and Medzihradszky, Katlin F. and Bogyo, Matthew}, year={2002}, month=jan, pages={60–68} }

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