Zobrazeno 1 - 10
of 19
pro vyhledávání: '"Kendra E Hightower"'
Autor:
Felix DeAnda, Kendra E Hightower, Robert T Nolte, Kazunari Hattori, Tomokazu Yoshinaga, Takashi Kawasuji, Mark R Underwood
Publikováno v:
PLoS ONE, Vol 8, Iss 10, p e77448 (2013)
Signature HIV-1 integrase mutations associated with clinical raltegravir resistance involve 1 of 3 primary genetic pathways, Y143C/R, Q148H/K/R and N155H, the latter 2 of which confer cross-resistance to elvitegravir. In accord with clinical findings
Externí odkaz:
https://doaj.org/article/c236911bda2245a0833c118568cf3e4c
Autor:
Brian A. Johns, Emile Johann Velthuisen, Kendra E. Hightower, John W. Seal, Peter Gerondelis, Kevin K. Brown, Ming Li, Lisa A. Leesnitzer, Wenwen Zhang, Yan Chen, Sonia R. Miranda, Ke Mou
Publikováno v:
European journal of medicinal chemistry. 83
Using a structure based pharmacophore design, a weak inhibitor of RNase H, identified from a small library of two metal binding HIV-1 integrase inhibitors, was optimized for potency and physicochemical properties. This manuscript describes the SAR an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2bd973f72221ddfffa959c04284f6b71
https://pubmed.ncbi.nlm.nih.gov/24997293
https://pubmed.ncbi.nlm.nih.gov/24997293
Lysine164α of protein farnesyltransferase is important for both CaaX substrate binding and catalysis
Publikováno v:
Biochemical Journal. 360:625-631
Protein farnesyltransferase (FTase) catalyses the formation of a thioether linkage between proteins containing a C-terminal CaaX motif and a 15-carbon isoprenoid. The involvement of substrates such as oncogenic Ras proteins in tumour formation has le
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8bf11d78c9217dcd7ee9ea824cbe60bb
https://doi.org/10.1042/bj3600625
https://doi.org/10.1042/bj3600625
Publikováno v:
Biochemistry. 39:2593-2602
Protein farnesyltransferase is a zinc metalloenzyme that catalyzes the transfer of a 15-carbon farnesyl group to a conserved cysteine residue of a protein substrate. Both electrophilic and nucleophilic mechanisms have been proposed for this enzyme. I
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9055f950b20f99efcdd7fd02b8d3deac
https://doi.org/10.1021/bi992356x
https://doi.org/10.1021/bi992356x
Autor:
Kendra E. Hightower, Carol A. Fierke
Publikováno v:
Current Opinion in Chemical Biology. 3:176-181
Zinc metalloenzymes catalyze many important cellular reactions. Recently, the involvement of zinc in the catalysis of alkylation of sulfur groups has gained prominence. Current studies of the zinc metalloenzyme protein farnesyltransferase have shed l
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1d343ce736e458e8e46007b02a64417a
https://doi.org/10.1016/s1367-5931(99)80030-1
https://doi.org/10.1016/s1367-5931(99)80030-1
Autor:
Mark R. Underwood, Felix Deanda, Kazunari Hattori, Tomokazu Yoshinaga, Kendra E. Hightower, Robert T. Nolte, Takashi Kawasuji
Publikováno v:
PLoS ONE, Vol 8, Iss 10, p e77448 (2013)
PLoS ONE
PLoS ONE
Signature HIV-1 integrase mutations associated with clinical raltegravir resistance involve 1 of 3 primary genetic pathways, Y143C/R, Q148H/K/R and N155H, the latter 2 of which confer cross-resistance to elvitegravir. In accord with clinical findings
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6ebb3a1c25b0c0f5d4b9387efa9a6d8c
http://europepmc.org/articles/PMC3797783?pdf=render
http://europepmc.org/articles/PMC3797783?pdf=render
Autor:
Marlys Hammond, David G. Washburn, Angela Smallwood, Tram H. Hoang, Nicholas J. Laping, Rebecca Trejo, Hiroko Nakamura, James S. Frazee, Martha S. Head, Scott K. Thompson, Kendra E. Hightower, Charlene Wu, Rakesh Nagilla, Jaclyn R. Patterson, Melanie Nord, Walter Trizna, Baoguang Zhao, Sharada Manns, Leonard M. Azzarano, Christine G. Schnackenberg
Publikováno v:
Bioorganicmedicinal chemistry letters. 19(15)
The lead serum and glucocorticoid-related kinase 1 (SGK1) inhibitors 4-(5-phenyl-1H-pyrrolo[2,3-b]pyridin-3-yl)benzoic acid (1) and {4-[5-(2-naphthalenyl)-1H-pyrrolo[2,3-b]pyridin-3-yl]phenyl}acetic acid (2) suffer from low DNAUC values in rat, due i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::523f8d46c823349d7ef17b1b17b5356f
https://pubmed.ncbi.nlm.nih.gov/19497745
https://pubmed.ncbi.nlm.nih.gov/19497745
Autor:
Margarete Neu, Donald O. Somers, Gladstone Thompson, Richard Martyn Angell, Kendra E. Hightower, Jeffery L. Smith, Maria Cichy-Knight, Tsu Tshen Chuang, Ruolan Wang, Murray J. B. Brown, Sonia Thomas, Allison K. Dunn, Robyn L. Shea, Susanna Malkakorpi, James R. Musgrave, Francis Louis Atkinson, John A. Christopher, Paul Rowland
Publikováno v:
Bioorganicmedicinal chemistry letters. 17(5)
The identification and exploration of a novel, potent and selective series of N-(3-cyano-4,5,6,7-tetrahydro-1-benzothien-2-yl)amide inhibitors of JNK2 and JNK3 kinases is described. Compounds 5a and 11a were identified as potent inhibitors of JNK3 (p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cca2005b257f5ed43bfb9a7fb771da90
https://pubmed.ncbi.nlm.nih.gov/17194588
https://pubmed.ncbi.nlm.nih.gov/17194588
Publikováno v:
Peptides for the New Millennium ISBN: 0792364457
The zinc metalloenzyme protein farnesyltransferase (FTase) catalyzes the farnesylation of a cysteine residue of protein or peptide substrates containing the "CaaX" motif using farnesyl pyrophosphate (FPP) [1], FTase has been hypothesized to utilize a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::83d374741083f6fae49c52c19d7ea270
https://doi.org/10.1007/0-306-46881-6_184
https://doi.org/10.1007/0-306-46881-6_184
