Zobrazeno 1 - 10
of 32
pro vyhledávání: '"Jamie A Moroco"'
Publikováno v:
eLife, Vol 9 (2020)
Mitochondria control the activity, quality, and lifetime of their proteins with an autonomous system of chaperones, but the signals that direct substrate-chaperone interactions and outcomes are poorly understood. We previously discovered that the mit
Externí odkaz:
https://doaj.org/article/63ad399fffd242d2b4db620d4cceb0bc
Autor:
Jamie A Moroco, Jodi K Craigo, Roxana E Iacob, Thomas E Wales, John R Engen, Thomas E Smithgall
Publikováno v:
PLoS ONE, Vol 9, Iss 8, p e105629 (2014)
Src-family kinases (SFKs) are non-receptor protein-tyrosine kinases involved in a variety of signaling pathways in virtually every cell type. The SFKs share a common negative regulatory mechanism that involves intramolecular interactions of the SH3 d
Externí odkaz:
https://doaj.org/article/e14dcc7fe6fa4ec0a53c9671ea2bcb36
Autor:
Michelle S. Prew, Christina M. Camara, Thomas Botzanowski, Jamie A. Moroco, Noah B. Bloch, Hannah R. Levy, Hyuk-Soo Seo, Sirano Dhe-Paganon, Gregory H. Bird, Henry D. Herce, Micah A. Gygi, Silvia Escudero, Thomas E. Wales, John R. Engen, Loren D. Walensky
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-12 (2022)
Prew et al. uncovered a structural basis for human VLCAD deficiency that arises from point mutations within the enzyme’s membrane-binding region, which was shown to fold as a putative α-helical hairpin. Helix-breaking mutations selectively disrupt
Externí odkaz:
https://doaj.org/article/e862c131a10741b096477d28809d47d0
Autor:
Peter G. Miller, Murugappan Sathappa, Jamie A. Moroco, Wei Jiang, Yue Qian, Sumaiya Iqbal, Qi Guo, Andrew O. Giacomelli, Subrata Shaw, Camille Vernier, Besnik Bajrami, Xiaoping Yang, Cerise Raffier, Adam S. Sperling, Christopher J. Gibson, Josephine Kahn, Cyrus Jin, Matthew Ranaghan, Alisha Caliman, Merissa Brousseau, Eric S. Fischer, Robert Lintner, Federica Piccioni, Arthur J. Campbell, David E. Root, Colin W. Garvie, Benjamin L. Ebert
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-16 (2022)
In this work, the authors report a sophisticated combination of genetic, biophysical, and biochemical analyses to identifies the cycling conformational states of PPM1D. The findings reveal how an allosteric inhibitor locks the protein into a conforma
Externí odkaz:
https://doaj.org/article/a652e8c526fe4774ba3ec46bd6f06545
Autor:
Ka Ying Sharon Hung, Sven Klumpe, Markus R. Eisele, Suzanne Elsasser, Geng Tian, Shuangwu Sun, Jamie A. Moroco, Tat Cheung Cheng, Tapan Joshi, Timo Seibel, Duco Van Dalen, Xin-Hua Feng, Ying Lu, Huib Ovaa, John R. Engen, Byung-Hoon Lee, Till Rudack, Eri Sakata, Daniel Finley
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-13 (2022)
The interplay of the proteasome and deubiquitinase Ubp6 is crucial for the degradation of ubiquitylated substrates. Here, the authors provide structural insights into the allosteric mechanism by which the activities of both Ubp6 and the proteasome ar
Externí odkaz:
https://doaj.org/article/0db17aeb4b8c4a309992d0d564111f7b
Autor:
Dale Porter, Alessandra Ianari, Merissa Brousseau, Patrick McCarren, Foxy P. Robinson, Adam Skepner, Virendar K. Kaushik, Kathleen M. Mulvaney, Arthur J. Campbell, Martin J Drysdale, Zachary Mullin-Bernstein, Brian J. McMillan, Robert Hilgraf, Ritu Singh, Matthew J. Ranaghan, Meghan O’Keefe, William R. Sellers, David C. McKinney, Jamie A. Moroco, Michael F. Mesleh, David E. Timm, Besnik Bajrami, Florence F. Wagner
Publikováno v:
J Med Chem
PRMT5 and its substrate adaptor proteins (SAPs), pICln and Riok1, are synthetic lethal dependencies in MTAP-deleted cancer cells. SAPs share a conserved PRMT5 binding motif (PBM) which mediates binding to a surface of PRMT5 distal to the catalytic si
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6e2c09646bd9e9db576eb95fa59b4da5
https://doi.org/10.1021/acs.jmedchem.1c00507
https://doi.org/10.1021/acs.jmedchem.1c00507
Autor:
Shoucheng Du, John J. Alvarado, Thomas E. Wales, Jamie A. Moroco, John R. Engen, Thomas E. Smithgall
Publikováno v:
Structure (London, England : 1993). 30(11)
The Src-family kinase Fgr is expressed primarily in myeloid hematopoietic cells and contributes to myeloid leukemia. Here, we present X-ray crystal structures of Fgr bound to the ATP-site inhibitors A-419259 and TL02-59, which show promise as anti-le
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::abc9a7890aec06da36350ba86f59a0ee
https://pubmed.ncbi.nlm.nih.gov/36115344
https://pubmed.ncbi.nlm.nih.gov/36115344
Autor:
Sonia M Vallabh, Arthur J. Campbell, Jayme L. Dahlin, Michael F. Mesleh, Kong T. Nguyen, Dominick Casalena, S. Kirk Wright, Dmitry L. Usanov, Christopher T. Lemke, Jamie A. Moroco, Joshua R. Sacher, Andrew G. Reidenbach, Murugappan Sathappa, Om K. Shrestha, Eric Vallabh Minikel, Jenna B. Yehl, Douglas S. Auld, Stuart L. Schreiber, V.L. Rangel, Alix I. Chan, Rishi N. Shah, Maria Cristina Nonato, David R. Liu, Florence F. Wagner, Alison Leed, Virendar K. Kaushik
Publikováno v:
J Biol Chem
Prion disease is a rapidly progressive neurodegenerative disorder caused by misfolding and aggregation of the prion protein (PrP), and there are currently no therapeutic options. PrP ligands could theoretically antagonize prion formation by protectin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ec8fc34d169f5f23f5d3171c3a119372
https://doi.org/10.1074/jbc.ra120.014905
https://doi.org/10.1074/jbc.ra120.014905
Autor:
Lisl Y. Esherick, Jacquin C. Niles, Patrick McCarren, Thomas C. Atack, Charisse Flerida A. Pasaje, Alessandra Ianari, Debjani Pal, Henock B. Befekadu, Christa Blomquist, Jamie A. Moroco, Donald Raymond, Foxy P. Robinson, William R. Sellers
Publikováno v:
ACS Medicinal Chemistry Letters. 11:2131-2138
FK506-binding protein 35, FKBP35, has been implicated as an essential malarial enzyme. Rapamycin and FK506 exhibit antiplasmodium activity in cultured parasites. However, due to the highly conserved nature of the binding pockets of FKBPs and the immu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c082587dcdacd303fe3a232c3a701fa2
https://doi.org/10.1021/acsmedchemlett.0c00272
https://doi.org/10.1021/acsmedchemlett.0c00272
Autor:
Michelle S, Prew, Christina M, Camara, Thomas, Botzanowski, Jamie A, Moroco, Noah B, Bloch, Hannah R, Levy, Hyuk-Soo, Seo, Sirano, Dhe-Paganon, Gregory H, Bird, Henry D, Herce, Micah A, Gygi, Silvia, Escudero, Thomas E, Wales, John R, Engen, Loren D, Walensky
Publikováno v:
Nature communications. 13(1)
Very long-chain acyl-CoA dehydrogenase (VLCAD) is an inner mitochondrial membrane enzyme that catalyzes the first and rate-limiting step of long-chain fatty acid oxidation. Point mutations in human VLCAD can produce an inborn error of metabolism call
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::a93e95466fd4e43f2a1609195a31e203
https://pubmed.ncbi.nlm.nih.gov/35760926
https://pubmed.ncbi.nlm.nih.gov/35760926