Zobrazeno 1 - 10
of 35
pro vyhledávání: '"Gary S. Laco"'
Autor:
Gary S. Laco
Publikováno v:
BioChem, Vol 1, Iss 3, Pp 190-209 (2021)
HIV-1 protease active site inhibitors are a key part of antiretroviral therapy, though resistance can evolve rendering therapy ineffective. Protease inhibitor resistance typically starts with primary mutations around the active site, which reduces in
Externí odkaz:
https://doaj.org/article/1a21b9c3fefa48f8a3a360c11322b3a2
Autor:
Gary S Laco
Publikováno v:
PLoS ONE, Vol 6, Iss 8, p e24314 (2011)
Human topoisomerase I (Top1) relaxes supercoiled DNA during cell division. Camptothecin stabilizes Top1/dsDNA covalent complexes which ultimately results in cell death, and this makes Top1 an anti-cancer target. There are two current models for how c
Externí odkaz:
https://doaj.org/article/72ce730480d249d0865f59cb29192363
Autor:
Laila Abdullah, Gary S. Laco, Jon Reed, Joseph O. Ojo, Benoit Mouzon, Michael Mullan, Fiona Crawford, Gogce Crynen, James E. Evans, Tanja Emmerich, Thinh H. Nguyen
Publikováno v:
NeuroMolecular Medicine. 19:122-135
Neurophysiological and neurological dysfunction is usually experienced for a short period of time in patients with mild traumatic brain injury (mTBI). However, around 15 % of patients exhibit symptoms months after TBI. Phospholipid (PL) changes have
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cbc6ea6239d7960f7566dbbc9dfdc392
https://doi.org/10.1007/s12017-016-8436-4
https://doi.org/10.1007/s12017-016-8436-4
Autor:
Gary S. Laco
Publikováno v:
Biochimie. 118:90-103
A key target in the treatment of HIV-1/AIDS has been the viral protease. Here we first studied in silico the evolution of protease resistance. Primary active site resistance mutations were found to weaken interactions between protease and both inhibi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3db64f8b43506ca243167b3b5238f5d2
https://doi.org/10.1016/j.biochi.2015.08.009
https://doi.org/10.1016/j.biochi.2015.08.009
Autor:
Gary S. Laco, James E. Evans, Tanja Emmerich, Ashok K. Shetty, Fiona Crawford, Laila Abdullah, Kimberly Sullivan, Nancy G. Klimas, Bharathi Hattiangady, Gogce Crynen, Zuchra Zakirova, Geetha A. Shetty, Michael Mullan, Ghania Ait-Ghezala
Publikováno v:
PLoS ONE
PLoS ONE, Vol 12, Iss 4, p e0176634 (2017)
PLoS ONE, Vol 12, Iss 4, p e0176634 (2017)
Gulf War Illness (GWI), which affects at least one fourth of the 700,000 veterans deployed to the Gulf War (GW), is characterized by persistent and heterogeneous symptoms, including pain, fatigue and cognitive problems. As a consequence, this illness
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f6cbc80272f5b8aea7943ae1258b0368
https://pubmed.ncbi.nlm.nih.gov/28453542
https://pubmed.ncbi.nlm.nih.gov/28453542
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 62:208-215
Crystals of human T-cell leukemia virus protease (HTLV-1 PR) have been very difficult to prepare and only native data extending to 2.6 angstroms resolution could be collected. Initial attempts to solve the structure with a variety of low-sequence-ide
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::024d84eb5e4932804947e6a0b5634a89
https://doi.org/10.1107/s0907444905040655
https://doi.org/10.1107/s0907444905040655
Crystal structure of human T cell leukemia virus protease, a novel target for anticancer drug design
Autor:
Jan Rozycki, Alla Gustchina, Alexander Wlodawer, Mi Li, Jerry Alexandratos, Gary S. Laco, Mariusz Jaskolski
Publikováno v:
Proceedings of the National Academy of Sciences. 102:18332-18337
The successful development of a number of HIV-1 protease (PR) inhibitors for the treatment of AIDS has validated the utilization of retroviral PRs as drug targets and necessitated their detailed structural study. Here we report the structure of a com
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d8994691ec57f948e7a36a8f2ff6756a
https://doi.org/10.1073/pnas.0509335102
https://doi.org/10.1073/pnas.0509335102
Autor:
Paola B. Arimondo, Christian Bailly, Craig J. Thomas, Thérèse Garestier, Jian Sheng Sun, Ludovic Halby, Didier Pez, Sidney M. Hecht, Alexandre Boutorine, Yves Pommier, Gary S. Laco, Philippe Schmitt
Publikováno v:
Biochemistry. 44:4171-4180
Topoisomerase I (topo I) is a ubiquitous DNA-cleaving enzyme and an important therapeutic target in cancer chemotherapy. Camptothecins (CPTs) reversibly trap topo I in covalent complex with DNA but exhibit limited sequence preference. The utilization
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ce6ff156c212636e7d1884b9594dfe9c
https://doi.org/10.1021/bi048031k
https://doi.org/10.1021/bi048031k
Phosphorylation of DNA Topoisomerase I by the c-Abl Tyrosine Kinase Confers Camptothecin Sensitivity
Autor:
Glenda Kohlhagen, James Lee, Ajit Bharti, Ehsan Khan, Surender Kharbanda, Donghui Yu, Yves Pommier, Gary S. Laco, Abdul Khaleque, Yung-Chi Cheng
Publikováno v:
Journal of Biological Chemistry. 279:51851-51861
DNA topoisomerase I (topo I) is involved in the regulation of DNA supercoiling, gene transcription, recombination, and DNA repair. The anticancer agent camptothecin specifically targets topo I. The mechanisms responsible for the regulation of topo I
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::65f79487a08db65b8380fdc14fc312ae
https://doi.org/10.1074/jbc.m404396200
https://doi.org/10.1074/jbc.m404396200
Autor:
Glenda Kohlhagen, Donald M. Jerina, Gary S. Laco, Jane M. Sayer, Thomas G. Burke, Wu Du, Yves Pommier, Dennis P. Curran
Publikováno v:
Bioorganic & Medicinal Chemistry. 12:5225-5235
Human topoisomerase I (Top1) plays a pivotal role in cell replication and transcription, and therefore is an important anti-cancer target. Homocamptothecin is a lead compound for inhibiting Top1, and is composed of five conjugated planar rings (A-E).
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f30b7d2596eba4c1cc22feb89ccb1f00
https://doi.org/10.1016/j.bmc.2004.06.046
https://doi.org/10.1016/j.bmc.2004.06.046