Zobrazeno 1 - 10
of 186
pro vyhledávání: '"Jane M. Sayer"'
Autor:
John M Louis, Annie Aniana, Katheryn Lohith, Jane M Sayer, Julien Roche, Carole A Bewley, G Marius Clore
Publikováno v:
PLoS ONE, Vol 9, Iss 8, p e104683 (2014)
We previously reported a series of antibodies, in fragment antigen binding domain (Fab) formats, selected from a human non-immune phage library, directed against the internal trimeric coiled-coil of the N-heptad repeat (N-HR) of HIV-1 gp41. Broadly n
Externí odkaz:
https://doaj.org/article/2505e9a47ce943a195d35748e0303366
Autor:
Donald M. Jerina, Chin H. Lin, Nicholas E. Geacintov, Shantu Amin, Yijin Tang, Fabián A. Rodríguez, Jane M. Sayer, Suse Broyde, Shuang Ding, Zhi Liu, Yuqin Cai
Publikováno v:
Biochemistry. 51:9751-9762
The most potent tumorigen identified among the polycyclic aromatic hydrocarbons (PAH) is the nonplanar fjord region dibenzo[a,l]pyrene (DB[a,l]P). It is metabolically activated in vivo through the widely studied diol epoxide (DE) pathway to form cova
Autor:
Robert W. Harrison, Irene T. Weber, Annie Aniana, Joon H. Park, Jane M. Sayer, John M. Louis, Xiaxia Yu
Publikováno v:
Biochemistry. 55(16)
We have systematically validated the activity and inhibition of a HIV-1 protease (PR) variant bearing 17 mutations (PR(S17)), selected to represent high resistance by machine learning on genotype-phenotype data. Three of five mutations in PR(S17) cor
Autor:
Annie Aniana, Irene T. Weber, Chen-Hsiang Shen, Johnson Agniswamy, Jane M. Sayer, John M. Louis
Publikováno v:
Biochemistry. 51:2819-2828
The escape mutant of HIV-1 protease (PR) containing 20 mutations (PR20) undergoes efficient polyprotein processing even in the presence of clinical protease inhibitors (PIs). PR20 shows >3 orders of magnitude decreased affinity for PIs darunavir (DRV
Publikováno v:
Biochemistry. 51:1041-1050
The HIV-1 protease (PR) mediates its own release (autoprocessing) from the polyprotein precursor, Gag-Pol, flanked by the transframe region (TFR) and reverse transcriptase at its N- and C-termini, respectively. Autoprocessing at the N-terminus of PR
Publikováno v:
Protein Science. 19:2055-2072
The mature protease from Group N human immunodeficiency virus Type 1 (HIV-1) (PR1(N)) differs in 20 amino acids from the extensively studied Group M protease (PR1(M)) at positions corresponding to minor drug-resistance mutations (DRMs). The first cry
Publikováno v:
Protein Science. 18:2442-2453
Purification and in vitro protein-folding schemes were developed to produce monodisperse samples of the mature wild-type HIV-2 protease (PR2), enabling a comprehensive set of biochemical and biophysical studies to assess the dissociation of the dimer
Autor:
Jane M. Sayer, John M. Louis
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 75:556-568
The importance of the active site region aspartyl residues 25 and 29 of the mature HIV-1 protease (PR) for the binding of five clinical and three experimental protease inhibitors [symmetric cyclic urea inhibitor DMP323, nonhydrolyzable substrate anal
Publikováno v:
Chemical Research in Toxicology. 20:311-315
A synthetic route to oligonucleotides containing N(2)-deoxyguanosine adducts at C-10 of the enantiomeric 7,8-diol 9,10-epoxides of 7,8,9,10-tetrahydrobenzo[a]pyrene in which the epoxide oxygen and the 7-hydroxyl group are trans is described. The pres
Publikováno v:
Biochemistry. 54(35)
N-Terminal self-cleavage (autoprocessing) of the HIV-1 protease precursor is crucial for liberating the active dimer. Under drug pressure, evolving mutations are predicted to modulate autoprocessing, and the reduced catalytic activity of the mature p