Zobrazeno 1 - 10
of 32
pro vyhledávání: '"A. H. Pekar"'
Additional file 1: Figure S1. Temporal distribution of cyanobacteria in the focused 9 lakes. Figure S2. Correlation matrix between all water factors concerned. Figure S3. PCA biplot which graphically demonstrates the first and second main components
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7b1ec0a6e2cde44cc06c9bf888f2cc77
Autor:
Ronald E. Chance, James M. Pettee, Allen H. Pekar, Elmer M. Schirmer, Melvin G. Johnson, Bruce H. Frank
Publikováno v:
International Journal of Peptide and Protein Research. 23:506-515
A genetic variant of bovine proinsulin has been isolated using preparative reverse-phase HPLC. The new proinsulin (bovine proinsulin II) differs from the known proinsulin (bovine proinsulin I) by a single amino acid residue at position C-48 in the co
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::906e2e9dbd9559391796e52f1d40f5dd
https://doi.org/10.1111/j.1399-3011.1984.tb02751.x
https://doi.org/10.1111/j.1399-3011.1984.tb02751.x
Autor:
Mark L. Brader, Michael L. Roy, Allen H. Pekar, Brandon Doyle, Beth Ann Thomas, Mark J. Pollo
Publikováno v:
Journal of Pharmaceutical Sciences. 94:2749-2763
LY307161 is a 31 amino acid analog of glucagonlike peptide-1(7-37)OH susceptible to physical instability associated with pharmaceutical processing. Orthogonal biophysical studies were conducted to explore the origins of this physical instability and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c45a321a0f2753362e7c9ea42470c08e
https://doi.org/10.1002/jps.20420
https://doi.org/10.1002/jps.20420
Publikováno v:
Pharmaceutical Research. 21:1087-1093
Purpose. Therapeutic antibodies are often formulated at a high concentration where they may have an opalescent appearance. The aim of this study is to understand the origin of this opalescence, especially its relationship to noncovalent association a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ea08f7d931cbf1a389d4fca0c5347196
https://doi.org/10.1023/b:pham.0000032993.98705.73
https://doi.org/10.1023/b:pham.0000032993.98705.73
Autor:
Amy L. Cox, Ronald E. Chance, David S. McClellan, Sharon R. Myers, Mark L. Brader, Allen H. Pekar, David B. Flora, Lynnie A. Irwin, Muppalla Sukumar
Publikováno v:
Nature Biotechnology. 20:800-804
The ability to tailor the release profile of a drug by manipulating its formulation matrix offers important therapeutic advantages. We show here that human insulin can be cocrystallized at preselected ratios with the fully active lipophilically modif
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8790eb3ca0b2a121ab35819f7e94f75a
https://doi.org/10.1038/nbt722
https://doi.org/10.1038/nbt722
Autor:
Kevin A. Destrampe, Dawn Marie Rebhun, Dean K. Clodfelter, Allen H. Pekar, Sharon R. Myers, Henry A. Havel, Mark L. Brader
Publikováno v:
Pharmaceutical Research. 15:254-262
Purpose. To utilize an acylated peptide as a model system to investigate the relationships among solution peptide conformation, non-covalent self-association, subcutaneous absorption and bioavailability under pharmaceutically relevant solution formul
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9ddb2e63eb4d17339e3b31c3ec05dd98
https://doi.org/10.1023/a:1011918719017
https://doi.org/10.1023/a:1011918719017
Autor:
David N. Brems, Steven Witt Dodd, Jerry Radziuk, Shun Li, Diane Lee Bakaysa, Allen H. Pekar, John Michael Beals, Mark L. Brader, Henry A. Havel
Publikováno v:
Protein Science. 5:2521-2531
The rate-limiting step for the absorption of insulin solutions after subcutaneous injection is considered to be the dissociation of self-associated hexamers to monomers. To accelerate this absorption process, insulin analogues have been designed that
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::09510b7233cf72524da7698df4d99daa
https://doi.org/10.1002/pro.5560051215
https://doi.org/10.1002/pro.5560051215
Autor:
Alita Miller, Steven R. Maple, Allen H. Pekar, Donald B. Spencer, David N. Brems, Christopher Bryant, Diane Lee Bakaysa, Karen S. McCune
Publikováno v:
Biochemistry. 32:8075-8082
The effect of pH on the conformational stability of insulin was studied. Surprisingly, the Gibbs free energy of unfolding increased approximately 30% by acidification. pH titration of insulin's conformational stability is described by a transition in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ebbfb6fb7d884e176aa2a23207375ba8
https://doi.org/10.1021/bi00083a004
https://doi.org/10.1021/bi00083a004
Publikováno v:
Biochemistry. 32:1555-1562
It has been previously shown, by equilibrium denaturation, that human growth hormone (hGH) folds by a cooperative two-state process. This is in contrast to the folding pathways of other nonhuman growth hormones that contain stable monomeric and multi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::379b38371942fda3da6918d2db064eb0
https://doi.org/10.1021/bi00057a021
https://doi.org/10.1021/bi00057a021
Autor:
David N. Brems, Harlan B. Long, Christopher Bryant, Ronald E. Chance, L. Kenney Green, Leila A. Alter, Alan H. Pekar, Margaret Strohl
Publikováno v:
Biochemistry. 31:5692-5698
To determine the conformational properties of the C-terminal region of the insulin B-chain relative to the helical core of the molecule, we have investigated the fluorescence properties of an insulin analog in which amino acids B28 and B29 have been
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e08b50c2f8123e355453ad496ccccb09
https://doi.org/10.1021/bi00140a002
https://doi.org/10.1021/bi00140a002