Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Sesha I Natarajan"'
Autor:
Claudio Mapelli, Sesha I. Natarajan, Jean-Philippe Meyer, Margarita M. Bastos, Michael S. Bernatowicz, Ving G. Lee, Jelka Pluscec, Douglas J. Riexinger, Ellen S. Sieber-McMaster, Keith L. Constantine, Constance A. Smith-Monroy, Rajasree Golla, Zhengping Ma, Daniel A. Longhi, Dan Shi, Li Xin, Joseph R. Taylor, Barry Koplowitz, Cecilia L. Chi, Ashish Khanna
Publikováno v:
Journal of Medicinal Chemistry; Dec2009, Vol. 52 Issue 23, p7788-7799, 12p
Autor:
Sesha I Natarajan, J.D. Godfrey, Harold N. Weller, K. Niemela, David W. Cushman, M.B. Rom, E. F. Sabo, Jelka Pluščec, Eric M. Gordon
Publikováno v:
Bioorganic Chemistry. 14:148-156
Several series of tripeptide modeled angiotensin-converting enzyme (ACE) inhibitors have been reported which contain an N-terminal acylamino substituent as an essential structural component for conservation of biological activity. The results of a st
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::94512b1ba6cfaf53ebe03b77b67154de
https://doi.org/10.1016/0045-2068(86)90024-6
https://doi.org/10.1016/0045-2068(86)90024-6
Autor:
David W. Cushman, Eric M. Gordon, Donald S. Karanewsky, Ondetti Ma, John Krapcho, Sesha I Natarajan, E W Petrillo
Publikováno v:
Journal of Cardiovascular Pharmacology. 10:17-30
Angiotensin-converting enzyme (ACE), the receptor for an important new class of antihypertensive drugs, is now one of the better studied zinc metallopeptidases. The development of several classes of tightly binding competitive inhibitors of ACE has l
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6344baede1a45ee86b4f2b4849cf5c14
https://doi.org/10.1097/00005344-198706107-00004
https://doi.org/10.1097/00005344-198706107-00004
Autor:
J. Engebrecht, M.B. Rom, E. F. Sabo, Sesha I Natarajan, Eric M. Gordon, David W. Cushman, J.D. Godfrey, Harold N. Weller, Jelka Pluščec
Publikováno v:
Biochemical and Biophysical Research Communications. 124:148-155
Results of an investigation aimed at identifying the consequences of chemical modifications of the alpha-aminoketone moiety of ketomethyldipeptides on angiotensin converting enzyme (ACE) inhibition are reported. These studies lead to the conclusion t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::27f0a514e4c2f51e2685419fdc91cc3e
https://doi.org/10.1016/0006-291x(84)90929-x
https://doi.org/10.1016/0006-291x(84)90929-x
Publikováno v:
Tetrahedron Letters. 25:3277-3280
Amino acid derived chloromethyl ketones are shown to undergo a general dehydrohalogenation reaction under mild, basic, nonnucleophilic conditions to afford α-β-unsaturated ketones.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::630c97f442db68aa65d1b7353d90721e
https://doi.org/10.1016/s0040-4039(01)81363-0
https://doi.org/10.1016/s0040-4039(01)81363-0
Autor:
J.D. Godfrey, David W. Cushman, M.B. Rom, Eric M. Gordon, Harold N. Weller, Jelka Pluščec, Sesha I Natarajan, E. F. Sabo
Publikováno v:
Biochemical and biophysical research communications. 124(1)
The design rationale for a new series of angiotensin-converting enzyme (ACE) inhibitors which incorporate a ketone substituent into a peptide backbone is described. Molecular regions which were expected to mimic the binding of an N-acyl tripeptide su
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d9c1a10852d970405a0e2f63da131892
https://pubmed.ncbi.nlm.nih.gov/6093782
https://pubmed.ncbi.nlm.nih.gov/6093782
Autor:
J.D. Godfrey, Jack M. DeForrest, Jelka Pluščec, E. F. Sabo, M.B. Rom, J. Engebrecht, Sesha I Natarajan, Eric M. Gordon, Harold N. Weller, David W. Cushman, J. Powell
Publikováno v:
Journal of enzyme inhibition. 2(2)
The design rationale for a new series of tripeptide derived angiotensin converting enzyme (ACE) inhibitors, which we term “ketomethylureas”, is described. Analogs of tripeptide substrates (i.e. N-benzoyl-Phe-Ala-Pro) in which the nitrogen atom of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a0f3e37c0b8931d3bb6a865e275eaaf9
https://pubmed.ncbi.nlm.nih.gov/3236070
https://pubmed.ncbi.nlm.nih.gov/3236070