Zobrazeno 1 - 10
of 148
pro vyhledávání: '"Rands, E"'
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America, 1970 Dec . 67(4), 1789-1796.
Externí odkaz:
https://www.jstor.org/stable/60570
Autor:
S J deSolms, Rands E, Jackson B. Gibbs, Catherine M. Wiscount, Scholz Th, Robert L. Smith, Kenneth S. Koblan, Nancy E. Kohl, E A Giuliani, David L. Pompliano, Scott D. Mosser, Oliff Allen I, Samuel L. Graham
Publikováno v:
Journal of Medicinal Chemistry. 41:2651-2656
Inhibitors of Ras protein farnesyltransferase are described which are reduced pseudopeptides related to the C-terminal tetrapeptide of the Ras protein that signals farnesylation. Reduction of the carbonyl groups linking the first three residues of th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8f669f5680f64cda6fe287560a76428f
https://doi.org/10.1021/jm9800907
https://doi.org/10.1021/jm9800907
Autor:
Theresa M. Williams, Rands E, Nancy E. Kohl, George D. Hartman, Samuel L. Graham, Kelly Hamilton, Timothy J. O'Neill, Oliff Allen I, Christopher J. Dinsmore, Kenneth S. Koblan, Jackson B. Gibbs
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 7:1345-1348
The design and synthesis of simple nonpeptide inhibitors of farnesyl-protein transferase (FTase) are described. Cysteine-derived diarylether frameworks are appropriate structural replacements for the C -terminal tetrapeptide portion of the Ras protei
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2dd7b69649d3202b5e1985676c23a1eb
https://doi.org/10.1016/s0960-894x(97)00225-4
https://doi.org/10.1016/s0960-894x(97)00225-4
Autor:
Dona L. Bamberger, Jackson B. Gibbs, Oliff Allen I, Nancy E. Kohl, Samuel L. Graham, Rands E, Thorsten E. Fisher, Robert L. Smith, Scott D. Mosser, John S. Wai, David L. Pompliano
Publikováno v:
Bioorganic & Medicinal Chemistry. 2:939-947
Replacement of the central amino methylene linkage of C[psi CH2NH]A[psi CH2NH]AX tetrapeptide inhibitors with carbon tethers led to compounds with potency in the nanomolar range. Some of the more potent olefinic compounds inhibit Ras processing in in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b0f12a4866dd3e02468fdf30eda06577
https://doi.org/10.1016/s0968-0896(00)82043-x
https://doi.org/10.1016/s0968-0896(00)82043-x
Autor:
Michael J. Breslin, Samuel L. Graham, Scott D. Mosser, Deana Aa, Rands E, Oliff Allen I, S J deSolms, Nancy E. Kohl, David L. Pompliano, E A Giuliani
Publikováno v:
Journal of Medicinal Chemistry. 37:725-732
Inhibitors of Ras farnesyl-protein transferase are described. These are reduced pseudopeptides related to the C-terminal tetrapeptide of the Ras protein that signals farnesylation. Deletion of the carbonyl groups between the first two residues of the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::694220638d203e2b4a9bf3af58e0ae80
https://doi.org/10.1021/jm00032a004
https://doi.org/10.1021/jm00032a004
Autor:
Scott D. Mosser, Sheo B. Singh, Russell B. Lingham, Jackson B. Gibbs, Rands E, Edward M. Scolnick, David L. Pompliano, Oliff Allen I, Nancy E. Kohl
Publikováno v:
Journal of Biological Chemistry. 268:7617-7620
The ras oncogene product, Ras, is synthesized in vivo as a precursor protein that requires post-translational processing to become biologically active and to be capable of transforming mammalian cells. Farnesylation appears to be a critical modificat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0269c733afb5faa972e12c9961ab15ca
https://doi.org/10.1016/s0021-9258(18)52998-7
https://doi.org/10.1016/s0021-9258(18)52998-7
Autor:
Robert B. Lobell, J. Christopher Culberson, Jackson B. Gibbs, Christopher J. Dinsmore, Kenneth S. Koblan, Theresa M. Williams, Nancy E. Kohl, Dongming Liu, Rands E, Timothy J. O'Neill
Publikováno v:
ChemInform. 31
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e6eb01d4b86d19f516aa3aa8ac4a48ae
https://doi.org/10.1002/chin.200009242
https://doi.org/10.1002/chin.200009242
Autor:
Rands E, Kenneth S. Koblan, Robert B. Lobell, Samuel L. Graham, Dongming Liu, Jackson B. Gibbs, J. Christopher Culberson, George D. Hartman, Theresa M. Williams, Nancy E. Kohl, Christopher J. Dinsmore, Oliff Allen I, Timothy J. O'Neill
Publikováno v:
Bioorganicmedicinal chemistry letters. 9(23)
The design and syntheses of non-thiol inhibitors of farnesyl-protein transferase are described. Optimization of cysteine-substituted diarylethers led to highly potent imidazole-containing diarylethers and diarylsulfones. Polar diaryl linkers dramatic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::64e9d100b2f603dc26fa32d0b97700b3
https://pubmed.ncbi.nlm.nih.gov/10612589
https://pubmed.ncbi.nlm.nih.gov/10612589
Autor:
Rands E, Samuel L. Graham, George D. Hartman, Nancy E. Kohl, Micheal D. Schaber, Robert P. Gomez, Oliff Allen I, Daksha Shah, Neville J. Anthony, Scott D. Mosser, Kelly Hamilton, Timothy J. O'Neil, Kenneth S. Koblan, Jackson B. Gibbs
Publikováno v:
Journal of medicinal chemistry. 42(17)
Inhibitors of farnesyl protein transferase (FPTase) based upon a pseudotripeptide template are described that comprise an imidazole group substituted with a hydrophobic substituent. (1, 5)-Disubstitution of the imidazole group is shown to be the opti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3ab156de66cea84036f95e950bd24518
https://pubmed.ncbi.nlm.nih.gov/10464022
https://pubmed.ncbi.nlm.nih.gov/10464022
Autor:
Scott D. Mosser, Samuel L. Graham, Oliff Allen I, E A Giuliani, Rands E, S J deSolms, Deana Aa, David L. Pompliano, Nancy E. Kohl, Scholz Th
Publikováno v:
Journal of medicinal chemistry. 38(20)
A series of pseudodipeptide amides are described that inhibit Ras protein farnesyltransferase (PFTase). These inhibitors are truncated versions of the C-terminal tetrapeptide (CAAX motif) of Ras that serves as the signal sequence for PFTase-catalyzed
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::912a6d48b28dbd68348a68f3b3e36737
https://pubmed.ncbi.nlm.nih.gov/7562930
https://pubmed.ncbi.nlm.nih.gov/7562930