Zobrazeno 1 - 10
of 83
pro vyhledávání: '"Clark W. Smith"'
Publikováno v:
International Journal of Peptide and Protein Research. 45:1-10
Two stereoselective syntheses of a new pseudodipeptide isostere, the right-hand hydroxyethylene dipeptido-mimetic (Xaaψ[CH2CH(OH)]Yaa), are presented. In one method readily available amino acids are used as starting materials for Evans chiral aldol
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8c86eb91e33be43f72df87d08840ba81
https://doi.org/10.1111/j.1399-3011.1995.tb01561.x
https://doi.org/10.1111/j.1399-3011.1995.tb01561.x
Publikováno v:
International Journal of Peptide and Protein Research. 21:127-134
The protected peptide, Ac-Glu(OBut)-D-Phe-D-Trp-Ser(But)-Tyr(But)-D-Lys (Z)-Leu-Arg(Tos)-Pro-Gly-NH2 was synthesized in a stepwise manner on a resin of poly-N-acrylylpyrrolidine using both acid cleavable N alpha-tert.-butyloxycarbonyl and base cleava
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bfc51410c96951f6e744e1a1b881a072
https://doi.org/10.1111/j.1399-3011.1983.tb03086.x
https://doi.org/10.1111/j.1399-3011.1983.tb03086.x
BIDIRECTIONAL SYNTHESIS OF [5-ASPARTIC ACID] ARGININE VASOPRESSIN ON POLY-N-ACRYLYLPYRROLIDINE RESIN
Publikováno v:
International Journal of Peptide and Protein Research. 16:365-371
In the proposed biologically active conformation of vasopressin at its antidiuretic receptor, the side-chain carboxamide moiety of the 5-position asparaginyl residue has been suggested to be an active element for the initiation of the antidiuretic re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fb28ae52fff8e7d03e0a8a80467bd408
https://doi.org/10.1111/j.1399-3011.1980.tb02960.x
https://doi.org/10.1111/j.1399-3011.1980.tb02960.x
Publikováno v:
International Journal of Peptide and Protein Research. 13:109-112
Entirely beaded poly-N-acrylylpyrrolidine-co-bisacrylyl-1, 2-diaminoethane-co-N-acrylyl-1, 6-diaminohexane-HCl(PAP), a new resin on which to perform peptide chemistry, has been prepared by reverse phase suspension polymerization in quantitative yield
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1226eb1ca0966ed2666ee61207b6c422
https://doi.org/10.1111/j.1399-3011.1979.tb01857.x
https://doi.org/10.1111/j.1399-3011.1979.tb01857.x
Publikováno v:
International Journal of Peptide and Protein Research. 15:331-334
Three beaded poly-N-acrylyldialkylamine resins have been systematically compared with polystyrene-co-1%-divinylbenzene for their ability to interact with solvents that are useful in peptide synthesis. The three resins have the same cross-linking mono
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cddfe2dbc626374d400f8fe20c0c27c8
https://doi.org/10.1111/j.1399-3011.1980.tb02909.x
https://doi.org/10.1111/j.1399-3011.1980.tb02909.x
Autor:
June M. Lull, Carol A. Bannow, Riqiang Yan, Alfredo G. Tomasselli, Thomas L. Emmons, Isam Qahwash, Michael Jerome Bienkowski, Kam F. Fok, Clark W. Smith, Joseph W. Leone, Yifeng Lu, Robert L. Heinrikson
Publikováno v:
Journal of Neurochemistry. 84:1006-1017
The involvement of β-secretase (BACE1; β-site APP-cleaving enzyme) in producing the β-amyloid component of plaques found in the brains of Alzheimer's patients, has fueled a major research effort to characterize this protease. Here, we describe wor
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::918f105b854f505ed1ea7223d2f1ff7c
https://doi.org/10.1046/j.1471-4159.2003.01597.x
https://doi.org/10.1046/j.1471-4159.2003.01597.x
Autor:
Peggy A. Garner-Hamrick, Gregory A. Waszak, David P. Thompson, Elaine A. Powers, Clark W. Smith, Anthony W. Yem, Douglas J. Staples, Wanxia He, Martin R. Deibel, Chris Fisher, Carol A. Bannow
Publikováno v:
Biochemical Journal. 347:653-660
Glutathione S-transferase (GST)-cdc25B(31-566) induced germinal vesicle breakdown (GVBD) when microinjected into Xenopus oocytes. Purified, N-terminally truncated forms of cdc25B did not induce GVBD, even though many had phosphatase activity and acti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::de84b534ac0318631fc8eed8d773d861
https://doi.org/10.1042/bj3470653
https://doi.org/10.1042/bj3470653
Publikováno v:
Analytical Biochemistry. 239:20-24
A rapid and simple method for quantitating the reaction product of UDP-GalNAc:polypeptide, N -acetylgalactosaminyltransferase (GalNAc-transferase) by scintillation proximity assay (SPA) was developed. The assay quantitates the radioactivity incorpora
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ba3f8da6a2692204bf59546e2f3f7751
https://doi.org/10.1006/abio.1996.0285
https://doi.org/10.1006/abio.1996.0285
Autor:
Satish K. Sharma, Kenneth B. Rank, Carol A. Bannow, Joseph W. Leone, Alfredo G. Tomasselli, Donna J. Rothrock, Robert L. Heinrikson, Clark W. Smith, Susan M. Poppe, David B. Evans, Naisheng Fan, W. Gary Tarpley
Publikováno v:
Journal of Biological Chemistry. 270:13573-13579
Active, recombinant p68 reverse transcriptase (RT) from human immunodeficiency virus type 2 (HIV-2), with an NH2-terminal extension containing a hexahisti-dine sequence was isolated from extracts of Escherichia coli by immobilized metal affinity chro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3f0385378507adbac5194e72c348fbaa
https://doi.org/10.1016/s0021-9258(18)92316-1
https://doi.org/10.1016/s0021-9258(18)92316-1
Autor:
D J Rothrock, Carol A. Bannow, C S Tomich, J M Lull, A. M. Mildner, I M Reardon, J L Sarcich, Clark W. Smith, W J Howe, Joseph W. Leone
Publikováno v:
Biochemistry. 33:9405-9413
Site-directed mutagenesis of autolysis sites in the human immunodeficiency virus type 1 (HIV-1) protease was applied in an analysis of enzyme specificity; the protease served, therefore, as both enzyme and substrate in this study. Inspection of natur
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d1c53661bef00e283b8c61084e47454c
https://doi.org/10.1021/bi00198a005
https://doi.org/10.1021/bi00198a005