Zobrazeno 1 - 10
of 26
pro vyhledávání: '"Daniel M. Himmel"'
Autor:
Daniel M. Himmel, Eddy Arnold
Publikováno v:
Pharmaceuticals, Vol 13, Iss 6, p 122 (2020)
In the treatment of acquired immune deficiency syndrome (AIDS), the diarylpyrimidine (DAPY) analogs etravirine (ETR) and rilpivirine (RPV) have been widely effective against human immunodeficiency virus (HIV) variants that are resistant to other non-
Externí odkaz:
https://doaj.org/article/8bb5475f0f5d4cf6bad959576696e40f
Autor:
Eddy Arnold, Daniel M. Himmel
Publikováno v:
Pharmaceuticals
Pharmaceuticals, Vol 13, Iss 122, p 122 (2020)
Pharmaceuticals, Vol 13, Iss 122, p 122 (2020)
In the treatment of acquired immune deficiency syndrome (AIDS), the diarylpyrimidine (DAPY) analogs etravirine (ETR) and rilpivirine (RPV) have been widely effective against human immunodeficiency virus (HIV) variants that are resistant to other non-
Autor:
Tatiana V Ilina, Michael A. Parniak, Eddy Arnold, Daniel M. Himmel, William C. Ho, Alexander Van Ry, Nataliya S. Myshakina
Publikováno v:
Journal of Molecular Biology. 426:2617-2631
Human immunodeficiency virus (HIV) encodes four essential enzymes: protease, integrase, reverse transcriptase (RT)-associated DNA polymerase, and RT-associated ribonuclease H (RNase H). Current clinically approved anti-AIDS drugs target all HIV enzym
Autor:
Carolyn Cohen, Suet Mui, Daniel M. Himmel, Elizabeth O'Neall-Hennessey, Andrew G. Szent-Györgyi
Publikováno v:
Journal of Molecular Biology. 394:496-505
In regulated myosin, motor and enzymatic activities are toggled between the on-state and off-state by a switch located on its lever arm domain, here called the regulatory domain (RD). This region consists of a long alpha-helical "heavy chain" stabili
Autor:
Kalyan Das, Stefan G. Sarafianos, Michael A. Parniak, Bruno Marchand, Daniel M. Himmel, Stephen H. Hughes, Edward Arnold
Publikováno v:
Journal of Molecular Biology. 385:693-713
The rapid replication of HIV-1 and the errors made during viral replication, cause the virus to evolve rapidly in patients, making the problems of vaccine development and drug therapy particularly challenging. In the absence of an effective vaccine,
Autor:
Daniel M. Himmel, William C. Ho, Deena A. Oren, Arthur D. Clark, Stephen H. Hughes, Eddy Arnold, Kalyan Das, Paul L. Boyer, Joseph D. Bauman, Aaron J. Shatkin, Mukta Baweja
Publikováno v:
Nucleic Acids Research
HIV-1 reverse transcriptase (RT) is a primary target for anti-AIDS drugs. Structures of HIV-1 RT, usually determined at approximately 2.5-3.0 A resolution, are important for understanding enzyme function and mechanisms of drug resistance in addition
Autor:
Mohammed M. Hossain, Karsten Krogh-Jespersen, Patrick K. Clark, Sanjeewa Dharmasena, Ronald M. Levy, Michael A. Parniak, Daniel M. Himmel, John G. Julias, Kessler McCoy-Simandle, Stephen H. Hughes, Tatiana V Ilina, Arthur D. Clark, Jennifer L. Knight, Eddy Arnold, Stefan G. Sarafianos
Publikováno v:
ACS Chemical Biology. 1:702-712
The rapid emergence of drug-resistant variants of human immunodeficiency virus, type 1 (HIV-1), has limited the efficacy of anti-acquired immune deficiency syndrome (AIDS) treatments, and new lead compounds that target novel binding sites are needed.
Autor:
Chi Hung Nguyen, Edward Arnold, Alain Philippe Poncelet, David Grierson, Stephen H. Hughes, Daniel M. Himmel, Said Oumouch, Christophe Meyer, Sophie Coupa, Jerome Guillemont, Abdellah Benjahad, Koen Andries, Kalyan Das, Arthur D. Clark, Csoka Imre Christian Francis
Publikováno v:
Journal of medicinal chemistry
In the treatment of AIDS, the efficacy of all drugs, including non-nucleoside inhibitors (NNRTIs) of HIV-1 reverse transcriptase (RT), has been limited by the rapid appearance of drug-resistant viruses. Lys103Asn, Tyr181Cys, and Tyr188Leu are some of
Publikováno v:
Proceedings of the National Academy of Sciences. 101:8930-8935
Structural studies of myosin have indicated some of the conformational changes that occur in this protein during the contractile cycle, and we have now observed a conformational change in a bound nucleotide as well. The 3.1-Å x-ray structure of the
Autor:
Samudrala Gourinath, Jerry H. Brown, Ludmilla Reshetnikova, Daniel M. Himmel, Andrew G. Szent-Györgyi, Carolyn Cohen
Publikováno v:
Structure. 11(12):1621-1627
We have extended the X-ray structure determination of the complete scallop myosin head in the pre-power stroke state to 2.6 A resolution, allowing an atomic comparison of the three major (weak actin binding) states of various myosins. We can now acco