Zobrazeno 1 - 10
of 55
pro vyhledávání: '"Jacinta L. Chuang"'
Autor:
Cheng-Yang Wu, Shih-Chia Tso, Jacinta L. Chuang, Wen-Jun Gui, Mingliang Lou, Gaurav Sharma, Chalermchai Khemtong, Xiangbing Qi, R. Max Wynn, David T. Chuang
Publikováno v:
Molecular Metabolism, Vol 12, Iss , Pp 12-24 (2018)
Objective: Mitochondrial pyruvate dehydrogenase kinases 1–4 (PDKs1–4) negatively regulate activity of the pyruvate dehydrogenase complex (PDC) by reversible phosphorylation. PDKs play a pivotal role in maintaining energy homeostasis and contribut
Externí odkaz:
https://doaj.org/article/3a496f86a86b49a19cf3b8bbc9e01009
Autor:
Noelle S. Williams, Lorraine Morlock, Xiangbing Qi, Wen Jun Gui, Cheng Yang Wu, David T. Chuang, R. Max Wynn, Mingliang Lou, Jacinta L. Chuang, Shih Chia Tso
Publikováno v:
Journal of Medicinal Chemistry. 60:1142-1150
Pyruvate dehydrogenase kinases 1–4 (PDK1-4) negatively control activity of the pyruvate dehydrogenase complex (PDC) and are up-regulated in obesity, diabetes, heart failure and cancer. We reported earlier two novel pan-PDK inhibitors PS8 [4-((5-hyd
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::16b3d074c1d16c8a0568cde22c4549a8
https://doi.org/10.1021/acs.jmedchem.6b01540
https://doi.org/10.1021/acs.jmedchem.6b01540
Autor:
Michael K. Rosen, Ranjit K. Deka, Shae B. Padrick, Michael V. Norgard, R. Max Wynn, Jacinta L. Chuang, Chad A. Brautigam, David T. Chuang
Publikováno v:
Analytical Biochemistry. 407:89-103
Determination of the stoichiometry of macromolecular assemblies is fundamental to an understanding of how they function. Many different biophysical methodologies may be used to determine stoichiometry. In the past, both sedimentation equilibrium and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8eb4d301969da6910f7be65cb1a5057e
https://doi.org/10.1016/j.ab.2010.07.017
https://doi.org/10.1016/j.ab.2010.07.017
Autor:
Mark Korson, David T. Chuang, Theodoros Georgiou, Jacinta L. Chuang, Anthi Drousiotou, Goula Stylianidou, R. Max Wynn
Publikováno v:
Genetic Testing and Molecular Biomarkers. 13:657-664
We report five mutations, three of them novel, responsible for maple syrup urine disease in four unrelated Cypriot families. The five children studied are the first cases of classic maple syrup urine disease to be reported among Cypriots. The first n
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c134f7d9026a03c02e40bc4f085a0c6d
https://doi.org/10.1089/gtmb.2009.0065
https://doi.org/10.1089/gtmb.2009.0065
Publikováno v:
Journal of Biological Chemistry. 284:13086-13098
The human pyruvate dehydrogenase complex (PDC) is a 9.5-megadalton catalytic machine that employs three catalytic components, i.e. pyruvate dehydrogenase (E1p), dihydrolipoyl transacetylase (E2p), and dihydrolipoamide dehydrogenase (E3), to carry out
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1f9229698b34f05b14a4286c6dcef71a
https://doi.org/10.1074/jbc.m806563200
https://doi.org/10.1074/jbc.m806563200
Publikováno v:
Journal of Biological Chemistry. 283:25305-25315
Human pyruvate dehydrogenase complex (PDC) is down-regulated by pyruvate dehydrogenase kinase (PDK) isoforms 1–4. PDK4 is overexpressed in skeletal muscle in type 2 diabetes, resulting in impaired glucose utilization. Here we show that human PDK4 h
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1fe4ddde6b9a5dbe853ae73c2288a34b
https://doi.org/10.1074/jbc.m802249200
https://doi.org/10.1074/jbc.m802249200
Publikováno v:
Journal of Biological Chemistry. 282:11904-11913
A long standing controversy is whether an alternating activesite mechanism occurs during catalysis in thiamine diphosphate (ThDP)-dependent enzymes. We address this question by investigating the ThDP-dependent decarboxylase/dehydrogenase (E1b) compon
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c441ddb4ad2ba9f34e87047985c8fd6f
https://doi.org/10.1074/jbc.m610843200
https://doi.org/10.1074/jbc.m610843200
Autor:
Nicholas Ah Mew, Wado Akamatsu, Hasan Orhan Akman, Koji Aoyama, W. David Arnold, Rafael Artuch, Robert M. Bachoo, Sergio E. Baranzini, Michael Beck, Merrill D. Benson, Vladimir M. Berginer, Gerard T. Berry, Kevin M. Biglan, Thomas D. Bird, D. Montgomery Bissell, Michael H. Bloch, Aldobrando Broccolini, Robert H. Brown, Allison Caban-Holt, Brenda Canine, C. Thomas Caskey, Patrick F. Chinnery, David T. Chuang, Jacinta L. Chuang, Bernard A. Cohen, Anne M. Comi, Rody P. Cox, John C. Crabbe, Marie Y. Davis, Darryl C. De Vivo, Robert J. Desnick, Stefano Di Donato, Salvatore DiMauro, Michael M. Dowling, David A. Dyment, Florian S. Eichler, Ramyiadarsini Elangovan, Bernice Elger, Sara Elrefai, Orna Elroy-Stein, Bakri H. Elsheikh, Andrew G. Engel, Patricia Evans, Stanley Fahn, Scott C. Fears, John K. Fink, Theodore Friedmann, Martin J. Gallagher, Àngels García-Cazorla, Jill S. Goldman, Sailaja Golla, Sidney M. Gospe, William D. Graf, Robert C. Griggs, Andrea L. Gropman, Yian Gu, Teresa M. Gunn, David H. Gutmann, Richard Haas, Randi J. Hagerman, Matti J. Haltia, Emma B. Hare, Tamar Harel, Stephen L. Hauser, Elizabeth Head, James E. Hilbert, Eric P. Hoffman, Othon Iliopoulos, Hiroyuki Ishiura, Monica P. Islam, Clifford R. Jack, William G. Johnson, Fabrice Jotterand, Heinz Jungbluth, John P. Kane, Clara van Karnebeek, Saima N. Kayani, Pravin Khemani, Fenella J. Kirkham, A. Yasmine Kirkorian, John T. Kissel, Christine Klein, Kleopas A. Kleopa, Satoshi Kono, Michael C. Kruer, Walter A. Kukull, Jessica B. Lennington, David A. Lewis, Wen-Chen Liang, Katja Lohmann, Paul J. Lombroso, Reymundo Lozano, James R. Lupski, Paola Luzi, Qian Ma, Robert L. Macdonald, Gustavo H.B. Maegawa, Elizabeth A. Maher, Mary J. Malloy, Ami K. Mankodi, Douglas A. Marchek, Isaac Marin-Valencia, Frederick J. Marshall, James A. Mastrianni, Reuben Matalon, Richard Mayeux, Jennifer L. McCurdy, Andrew J. McGarry, John H. Menkes, Giovanni Meola, Ana Metelo, Kimberlee Michals Matalon, Bruce L. Miller, Massimiliano Mirabella, Justin Miron, Jun Mitsui, Hiroaki Miyajima, Shuki Mizutani, Sara E. Mole, Lisa M. Monteggia, Hugo W. Moser, Mary Ann Morris, Richard T. Moxley, Jennifer M. Mueller, Francesco Muntoni, Melissa E. Murray, Toshio Nakaki, Charles B. Nemeroff, Ichizo Nishino, William L. Nyhan, Hideyuki Okano, Jorge R. Oksenberg, Adam P. Ostendorf, Massimo Pandolfo, Maria Belen Pappa, Carmen Paradas, Juan M. Pascual, Gregory M. Pastores, Shailendra B. Patel, Marc C. Patterson, Davut Pehlivan, Scott D. Philibin, Cynthia Picard, Judes Poirier, Louis J. Ptáček, Geetha L. Radhakrishnan, Jeffrey W. Ralph, Sreeram V. Ramagopalan, Gerald V. Raymond, William Renthal, Victor I. Reus, E. Steve Roach, Roger N. Rosenberg, David S. Rosenblatt, Gerald Salen, Konrad Sandhoff, Lawrence D. Scahill, Steven S. Scherer, Raphael Schiffmann, Detlev Schindler, Frederick Schmitt, Susanne A. Schneider, Eric A. Schon, Edward H. Schuchman, Nicole Schupf, Margretta Reed Seashore, Dennis J. Selkoe, Caroline Sewry, Michael Shevell, Shunichiro Shinagawa, Jemeen Sreedharan, Myriam Srour, Kazuma Sugie, Kristen L. Szabla, Steven T. Szabo, Gábor Szuhay, Franco Taroni, Rabi Tawil, Mireia Tondo, Shoji Tsuji, Bjarne Udd, Wendy R. Uhlmann, Flora M. Vaccarino, Prashanthi Vemuri, Charles P. Venditti, David W. Volk, Dong Wang, David Watkins, David A. Wenger, Charles A. Williams, Kathleen S. Wilson, Golder N. Wilson, Barry Wolf, R. Max Wynn, Shihui Yu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b843a1405130c528b83088edd17d968f
https://doi.org/10.1016/b978-0-12-410529-4.09990-3
https://doi.org/10.1016/b978-0-12-410529-4.09990-3
Maple syrup urine disease (MSUD) is an autosomal recessive disorder caused by a deficiency of the branched-chain α-ketoacid dehydrogenase complex (BCKDC). Patients with MSUD show variable degrees of enzyme deficiency leading to several distinct phen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::44161c635a6fcd1ad76dfbb98bb1b4bd
https://doi.org/10.1016/b978-0-12-410529-4.00059-0
https://doi.org/10.1016/b978-0-12-410529-4.00059-0
Autor:
Masato Kato, Chad A. Brautigam, Myra Custorio, David T. Chuang, Jacinta L. Chuang, R. Max Wynn
Publikováno v:
The EMBO Journal. 25:5983-5994
The dihydrolipoamide acyltransferase (E2b) component of the branched-chain alpha-ketoacid dehydrogenase complex forms a cubic scaffold that catalyzes acyltransfer from S-acyldihydrolipoamide to CoA to produce acyl-CoA. We have determined the first cr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::949008d5f29fd53a9bb94fbf9f200cf9
https://doi.org/10.1038/sj.emboj.7601444
https://doi.org/10.1038/sj.emboj.7601444