Zobrazeno 1 - 10
of 49
pro vyhledávání: '"T.-B. Shih"'
Autor:
Daniel T.-b. Shih, Khoon Tee Chong, Satoru Unzai, Gentaro Miyazaki, Takeshi Yokoyama, Jeremy R. H. Tame, Sam-Yong Park, Hideki Morimoto
Publikováno v:
Journal of Biological Chemistry. 279:28632-28640
The crystal structure of hemoglobin has been known for several decades, yet various features of the molecule remain unexplained or controversial. Several animal hemoglobins have properties that cannot be readily explained in terms of their amino acid
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::18d983e13fe82a4e824cf42096be71c5
https://doi.org/10.1074/jbc.m401740200
https://doi.org/10.1074/jbc.m401740200
Altered Ligand Rebinding Kinetics Due to Distal-side Effects in Hemoglobin Chico (Lysβ66(E10) → Thr)
Publikováno v:
Journal of Biological Chemistry. 274:8686-8693
Hb Chico is an unusual human hemoglobin variant that has lowered oxygen affinity, but unaltered cooperativity and anion sensitivity. Previous studies showed these features to be associated with distal-side heme pocket alterations that confer increase
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6e7e0eeeb0cc0fcefde06ffa2db7b0bd
https://doi.org/10.1074/jbc.274.13.8686
https://doi.org/10.1074/jbc.274.13.8686
Autor:
Richard T. Jones, Kathleen S. Kubik, Norman B. Roberts, D. Harvey, Allen B. Horne, Terry R.J. Lappin, Benjamin J. Madden, James D. Hoyer, Daniel J. McCormick, Brian N. Green, Virgil F. Fairbanks, Charlotte G. Head, Daniel T.-B. Shih, Paul C. Winter, G. Elizabeth Elder, Timothy M. Reynolds
Publikováno v:
Mayo Clinic Proceedings. 73:321-328
•Objective To determine the nature and characteristics of a unique hemoglobin variant that causes a spurious increase in glycated hemoglobin (Hb A lc ). •Material and Methods Blood specimens from four unrelated persons with this hemoglobin varian
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3783284ef4a9d36ee2934f54867b19a9
https://doi.org/10.1016/s0025-6196(11)63697-5
https://doi.org/10.1016/s0025-6196(11)63697-5
Publikováno v:
Journal of Biological Chemistry. 266:23033-23040
Hemoglobin (Hb) Chico (Lys beta 66----Thr at E10) has a diminished oxygen affinity (Shih, D. T.-b., Jones, R. T., Shih, M. F.-C., Jones, M. B., Koler, R. D., and Howard, J. (1987) Hemoglobin 11, 453-464). Our studies show that its P50 is about twice
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ef377d4c6069ab0374ebdc19d36b895e
https://doi.org/10.1016/s0021-9258(18)54459-8
https://doi.org/10.1016/s0021-9258(18)54459-8
Autor:
Daniel T.-b. Shih, Yoshinao Wada, Gentaro Miyazaki, Kenzo Fushitani, Teizo Kitagawa, Koichiro Ishimori, Hideki Morimoto, Isao Morishima, Kiyohiro Imai, Jeremy R. H. Tame
Publikováno v:
Journal of Molecular Biology. 218:769-778
To clarify the functional role of Tyr-42(C7)α, which forms a hydrogen bond with Asp-99(G1)β at the α1-β2 interface of human deoxyhaemoglobin, we engineered two artificial mutant haemoglobins (Hb), in which Tyr-42α was replaced by Phe (Hb Phe-42
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::eb85337457425642069365e557eff69e
https://doi.org/10.1016/0022-2836(91)90265-8
https://doi.org/10.1016/0022-2836(91)90265-8
Autor:
D. T. B. Shih, C. C. Hsiao, E. Y. Shen, D. C. Lee, W. T. Chiu, C. T. Huang, S. M. Weng, C. S. Hsu
Publikováno v:
Neuropediatrics. 37
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::67ba4930bfe0a0a25679e88f24f5410e
https://doi.org/10.1055/s-2006-943698
https://doi.org/10.1055/s-2006-943698
Autor:
Takeshi, Yokoyama, Khoon Tee, Chong, Gentaro, Miyazaki, Hideki, Morimoto, Daniel T-B, Shih, Satoru, Unzai, Jeremy R H, Tame, Sam-Yong, Park
Publikováno v:
The Journal of biological chemistry. 279(27)
The crystal structure of hemoglobin has been known for several decades, yet various features of the molecule remain unexplained or controversial. Several animal hemoglobins have properties that cannot be readily explained in terms of their amino acid
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::12a410863ce1914f824692ffc2084170
https://pubmed.ncbi.nlm.nih.gov/15117955
https://pubmed.ncbi.nlm.nih.gov/15117955
Publikováno v:
Journal of molecular biology. 230(4)
We have examined the contribution of His(HC3)146 beta to the alkaline Bohr effect of human haemoglobin (HbA) by replacing it with Gln, using site-directed mutagenesis, and studying the structural and functional consequences. Oxygen equilibrium curves
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7f34f73d22846a1af88472c3b8dc7c1e
https://pubmed.ncbi.nlm.nih.gov/8487305
https://pubmed.ncbi.nlm.nih.gov/8487305
Autor:
Charlotte Head, Thomas S. Fujita, Jolanta Wodzinska, Daniel T. B. Shih, Ronald Kluger, Richard T. Jones
Publikováno v:
Biochemistry. 32(1)
Human hemoglobin was reacted with five dicarboxylic acid bis(methyl phosphate) reagents under different ligand conditions. The bis(methyl phosphate) reagents tested were derived from fumaric, isophthalic, terephthalic, trans-stilbene-3,3'-dicarboxyli
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7a2884789798358cd5fe2447c7fb60e6
https://pubmed.ncbi.nlm.nih.gov/8418841
https://pubmed.ncbi.nlm.nih.gov/8418841
Publikováno v:
Nature. 352(6333)
Proteins in the globin family are found in a variety of species from bacteria to man. From the many globin sequences known, evolutionary trees have been constructed showing that alpha and beta globins diverged from a common ancestor between 425 and 5
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8ad4b6282781f45c6cd8065ad0e35812
https://pubmed.ncbi.nlm.nih.gov/1852211
https://pubmed.ncbi.nlm.nih.gov/1852211