Výsledky vyhledávání - "Frank J. Bruzzese"

Characterization of a new series of non-covalent proteasome inhibitors with exquisite potency and selectivity for the 20S β5-subunit

Autor: Edward J. Olhava, Paul Hales, Cynthia Barrett, Jane X. Liu, Matthew Jones, Frank J. Bruzzese, Kenneth M. Gigstad, Khristofer Garcia, Christopher Tsu, Darshan S. Sappal, Teresa A. Soucy, Paul E. Fleming, Christopher Blackburn, Michael D. Sintchak, Jonathan L. Blank, Nancy Bump, Lawrence R. Dick

Publikováno v: Biochemical Journal

The mammalian 26S proteasome is a 2500 kDa multi-catalytic complex involved in intracellular protein degradation. We describe the synthesis and properties of a novel series of non-covalent di-peptide inhibitors of the proteasome based [corrected] on

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9f48642b351f04b2dc37016661e3f601
https://doi.org/10.1042/bj20100383

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Evaluation of the Proteasome Inhibitor MLN9708 in Preclinical Models of Human Cancer

Publikováno v: Cancer Research. 70:1970-1980

The proteasome was validated as an oncology target following the clinical success of VELCADE (bortezomib) for injection for the treatment of multiple myeloma and recurring mantle cell lymphoma. Consequently, severalgroups are pursuing the development

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d49c1d0fb74b2b38a3e9c3578fb11fe2
https://doi.org/10.1158/0008-5472.can-09-2766

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Identification and application of NEDD8 E1 inhibitors

Autor: Frank J, Bruzzese, Michael A, Milhollen, James M, Gavin, Helen R, Josephine, James E, Brownell

Publikováno v: Methods in molecular biology (Clifton, N.J.). 832

The NEDD8 conjugation pathway is initiated by the NEDD8 E1, also known as NEDD8 activating enzyme (NAE) or APPBP1/UBA3 (Gong, Yeh. J Biol Chem 274:12063-12042, 1999). The best described biological role for NEDD8 conjugation is to regulate the activit

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::17c7905a642c15531b125a11417e0469
https://pubmed.ncbi.nlm.nih.gov/22350913

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Identification and Application of NEDD8 E1 Inhibitors

Autor: Michael Milhollen, Frank J. Bruzzese, Helen R. Josephine, James M. Gavin, James E. Brownell

Publikováno v: Methods in Molecular Biology ISBN: 9781617794735

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::74968cc19dc75958ed74cfc5ba6e5f19
https://doi.org/10.1007/978-1-61779-474-2_40

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Enthalpy of hydrogen bond formation in aprotein-ligand binding reaction

Autor: Shigeru Itoh, Mark A. Fleming, Frank J. Bruzzese, David J. Livingston, Matthew J. Fitzgibbon, John A. Thomson, Stephen P. Chambers, Patrick R. Connelly, R A Aldape, Manuel A. Navia

Publikováno v: Proceedings of the National Academy of Sciences. 91:1964-1968

Parallel measurements of the thermodynamics (free-energy, enthalpy, entropy and heat-capacity changes) of ligand binding to FK506 binding protein (FKBP-12) in H2O and D2O have been performed in an effort to probe the energetic contributions of single

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5d888ba7711d1d3d2cea5363a8cd4727
https://doi.org/10.1073/pnas.91.5.1964

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Probing hydration contributions to the thermodynamics of ligand binding by proteins. Enthalpy and heat capacity changes of tacrolimus and rapamycin binding to FK506 binding protein in deuterium oxide and water

Autor: Frank J. Bruzzese, Matthew J. Fitzgibbon, John A. Thomson, Patrick R. Connelly

Publikováno v: Biochemistry. 32:5583-5590

The stabilities of native proteins and protein-ligand complexes result from differential interactions among numerous polar and nonpolar atoms within the proteins and ligands and of these atoms with water. Delineation of the various energetic contribu

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::af22401502fb01ed93e12e5a66730b23
https://doi.org/10.1021/bi00072a013

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Optimization of a series of dipeptides with a P3 threonine residue as non-covalent inhibitors of the chymotrypsin-like activity of the human 20S proteasome

Autor: Kenneth M. Gigstad, Khristofer Garcia, Paul Hales, Nancy Bump, Frank J. Bruzzese, Paul E. Fleming, Lawrence R. Dick, Zhigen Hu, Christopher Blackburn, Matthew Jones, Christopher Tsu, Michael D. Sintchak, Cynthia Barrett, Jane X. Liu, Jonathan L. Blank, Darshan S. Sappal

Publikováno v: Bioorganicmedicinal chemistry letters. 20(22)

Starting from a tripeptide screening hit, a series of dipeptide inhibitors of the proteasome with Thr as the P3 residue has been optimized with the aid of crystal structures in complex with the β-5/6 active site of y20S. Derivative 25, (β5 IC(50)=7

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aed960939ca4ea0080006c362ffe95f3
https://pubmed.ncbi.nlm.nih.gov/20875739

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