Zobrazeno 1 - 10
of 21
pro vyhledávání: '"G T Burke"'
Autor:
G T, Burke
Publikováno v:
The Indian Medical Gazette
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::1c5f227568e1eeb227234f5214caadd1
https://pubmed.ncbi.nlm.nih.gov/29009513
https://pubmed.ncbi.nlm.nih.gov/29009513
Publikováno v:
International Journal of Peptide and Protein Research. 30:460-473
Hydrogen bonding involving peptide bonds of the backbone of the insulin molecule may play an important role in insulin-receptor interaction. Our previous work suggested that the A2-A8 helical segment of the hormone molecule participates in this inter
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::284c8c685ea59b3752099b5ba02b4da9
https://doi.org/10.1111/j.1399-3011.1987.tb03354.x
https://doi.org/10.1111/j.1399-3011.1987.tb03354.x
Autor:
D. F. Steiner, Mohammad Pashmforoush, P. G. Katsoyannis, T. Kurose, Y. Yoshimasa, G. P. Schwartz, G T Burke, Ronan K. Carroll
Publikováno v:
Journal of Biological Chemistry. 269:29190-29197
To identify a site within the insulin receptor ectodomain which forms a binding pocket for B25 Phe and is responsible for initiating conformational changes required for high affinity binding of insulin we have used a novel photoreactive insulin, desp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::154aa9beec5fdb038ea5aed4f9cc47d2
https://doi.org/10.1016/s0021-9258(19)62029-6
https://doi.org/10.1016/s0021-9258(19)62029-6
Autor:
Donald F. Steiner, G. T. Burke, Ying Chi Chu, P. G. Katsoyannis, Shi Quan Hu, S. Gammeltoft, Zong L, Chan Sj
Publikováno v:
Biochemistry. 33:11278-11285
Three insulin-like compounds consisting of two disulfide-linked polypeptide chains have been synthesized. The A-chains of these compounds correspond either to the A- or to the A + D-domain of the putative amphioxus insulin-like peptide (amphioxus ILP
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::35391b33e3ac5c1717ba59b421d33bcb
https://doi.org/10.1021/bi00203a025
https://doi.org/10.1021/bi00203a025
Autor:
G. T. Burke, E. Rusinova, William R. Laws, Panayotis G. Katsoyannis, J.B.A. Ross, Ying-Chi Chu, Gerald P. Schwartz
Publikováno v:
Journal of protein chemistry. 14(4)
Use of insulin's intrinsic tyrosine absorption and fluorescence to monitor its interaction with the insulin receptor is limited because the spectral properties of the receptor tryptophan residues mask the spectral properties of the hormone tyrosine r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3c5f8ee27455142e23a1ad152653d8d8
https://pubmed.ncbi.nlm.nih.gov/7662110
https://pubmed.ncbi.nlm.nih.gov/7662110
Autor:
T, Kurose, M, Pashmforoush, Y, Yoshimasa, R, Carroll, G P, Schwartz, G T, Burke, P G, Katsoyannis, D F, Steiner
Publikováno v:
The Journal of biological chemistry. 269(46)
To identify a site within the insulin receptor ectodomain which forms a binding pocket for B25 Phe and is responsible for initiating conformational changes required for high affinity binding of insulin we have used a novel photoreactive insulin, desp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::26e30f3918eabbc6c447a940a8b0d66e
https://pubmed.ncbi.nlm.nih.gov/7961885
https://pubmed.ncbi.nlm.nih.gov/7961885
Publikováno v:
Biochemistry. 33(44)
We describe the synthesis and biological evaluation of five two-chain, insulin-like compounds structurally related both to insulin and to a putative insulin like peptide (ILP) whose sequence was deduced from a cDNA cloned from Branchiostoma californi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1f1041b90a61fa9668cbc4f250ec73d6
https://pubmed.ncbi.nlm.nih.gov/7947713
https://pubmed.ncbi.nlm.nih.gov/7947713
Autor:
G. T. Burke, P. G. Katsoyannis, Gerald P. Schwartz, J. B. A. Ross, Shi-Quan Hu, N. Ferderigos
Publikováno v:
Biochemistry. 32(10)
The alpha-helix formed by the amino acid residues 9-19 of the B-chain of insulin is involved in the stabilization of its three-dimensional structure. We have shown that modification at positions B9, B10, B12, and B16 results in analogues possessing b
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4111ba4e0bbf8036a65f2c8ce01ee95b
https://pubmed.ncbi.nlm.nih.gov/8448120
https://pubmed.ncbi.nlm.nih.gov/8448120
Publikováno v:
Biochemistry. 26:6975-6979
We have synthesized [21-desasparagine,20-cysteine ethylamide-A]insulin and [21-desasparagine,20-cysteine 2,2,2-trifluoroethylamide-A]insulin, which differ from natural insulin in that the C-terminal amino residue of the A chain, asparagine, has been
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7ef6e0e1a83236f3e9c5e27e4a9b1098
https://doi.org/10.1021/bi00396a018
https://doi.org/10.1021/bi00396a018
Publikováno v:
Biochemistry. 27:6105-6111
A two-chain, disulfide linked, insulin-like compound embodying the A-domain of insulin-like growth factor I (IGF-I) and the B-chain of insulin has been synthesized and characterized with respect to insulin-like biological activity and growth-promotin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::75d8d0f3f2119af83bee011d55f06134
https://doi.org/10.1021/bi00416a041
https://doi.org/10.1021/bi00416a041