Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Larysa N. Patskovska"'
Autor:
Athiwat Hutchaleelaha, Harris Jason R, Qing Xu, Donna Oksenberg, Matthew P. Jacobson, Carl Johnson, Larysa N. Patskovska, Zhe Li, Joyce James, Qing Lu, Paulvannan Kumar, Chihyuan Chuang, Donghong Xu, Yury Patskovsky, Lan Hua, Abel Silva-Garcia, Kobina Dufu, Brian Metcalf, Bradley P Morgan, James R. Partridge, Stephen L Gwaltney, Calvin Yee, Mira Patel, Steven C. Almo
We report the discovery of a new potent allosteric effector of sickle cell hemoglobin, GBT440 (36), that increases the affinity of hemoglobin for oxygen and consequently inhibits its polymerization when subjected to hypoxic conditions. Unlike earlier
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::474bb23099c36d4a59ac8cad2e76a0d7
https://europepmc.org/articles/PMC5346980/
https://europepmc.org/articles/PMC5346980/
Autor:
David R. Archer, Athiwat Hutchaleelaha, Mira Patel, Brian Metcalf, Larysa N. Patskovska, Chihyuan Chuang, Zhe Li, Qing Xu, Yury Patskovsky, Chengjing Zhou, Steven C. Almo, Donna Oksenberg, Abel Silva-Garcia, Uma Sinha, Kobina Dufu
Publikováno v:
British journal of haematology. 175(1)
Summary A major driver of the pathophysiology of sickle cell disease (SCD) is polymerization of deoxygenated haemoglobin S (HbS), which leads to sickling and destruction of red blood cells (RBCs) and end-organ damage. Pharmacologically increasing the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e3da859d0033d27cb65d4d24bab32e93
https://pubmed.ncbi.nlm.nih.gov/27410726
https://pubmed.ncbi.nlm.nih.gov/27410726
Publikováno v:
Biochemistry. 45:3852-3862
An active site His107 residue distinguishes human glutathione S-transferase hGSTM1-1 from other mammalian Mu-class GSTs. The crystal structure of hGSTM1a-1a with bound glutathione (GSH) was solved to 1.9 A resolution, and site-directed mutagenesis su
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d1ec9a0a69ce479533257d630d3e5224
https://doi.org/10.1021/bi051823+
https://doi.org/10.1021/bi051823+
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 61:566-573
Human hemoglobin binds oxygen cooperatively and functions as a tetramer composed of two identical alphabeta heterodimers. While human hemoglobin is the best characterized allosteric protein, the quaternary R (oxygenated or liganded) to T (deoxygenate
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::78ee5a9286f0ef655ba48f8147e8c63f
https://doi.org/10.1107/s0907444905004622
https://doi.org/10.1107/s0907444905004622
Autor:
Yury Patskovsky, Rhoda Elison Hirsch, John C. Dewan, Larysa N. Patskovska, Angela R. Feeling-Taylor, Steven C. Almo, Ronald L. Nagel, Yoram A. Puius
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 58:2038-2042
Previous studies have demonstrated that in vitro crystallization of R-state liganded hemoglobin C (HbC), a naturally occurring mutant human hemoglobin (betaE6K), in high-phosphate buffer solutions provides a potential model system for the intracellul
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::100b6aba0e8d14484458367facb48360
https://doi.org/10.1107/s0907444902016426
https://doi.org/10.1107/s0907444902016426
Publikováno v:
Journal of Biological Chemistry. 273:9593-9601
A rat testicular Mu-class glutathione S-transferase (GST) resolved by reversed-phase high performance liquid chromatography cross-reacted with peptide sequence-specific antisera raised against the human hGSTM3 subunit. Electrospray ionization mass sp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::460a8918099a64852d9699b97252033b
https://doi.org/10.1074/jbc.273.16.9593
https://doi.org/10.1074/jbc.273.16.9593
Autor:
Yury Patskovsky, Steven C. Almo, Irving Listowsky, Larysa N. Patskovska, Alexander A. Fedorov
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 54:458-460
Human glutathione-S-transferase M2–2 (hGSTM2–2) was expressed in Escherichia coli and purified by GSH-affinity chromatography. The recombinant enzyme and the protein isolated from human tissue were indistinguishable based on physicochemical, enzy
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1ecfbaf7692f00e9cd8d365c2a058a7f
https://doi.org/10.1107/s0907444997011190
https://doi.org/10.1107/s0907444997011190
Publikováno v:
Biochemistry. 38(49)
The hGSTM3 subunit, which is preferentially expressed in germ-line cells, has the greatest sequence divergence among the human mu class glutathione S-transferases. To determine a structural basis for the catalytic differences between hGSTM3-3 and oth
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::84471be0ec02a3b2393f9befbaa9c4d7
https://pubmed.ncbi.nlm.nih.gov/10587441
https://pubmed.ncbi.nlm.nih.gov/10587441
Publikováno v:
Biochemistry. 38(4)
Domain interchange analyses and site-directed mutagenesis indicate that the His107 residue of the human subunit hGSTM1 has a pronounced influence on catalysis of nucleophilic aromatic substitution reactions, and a H107S substitution accounts for the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::98cd4f181f02724fd9de7f65e45ffd78
https://pubmed.ncbi.nlm.nih.gov/9930979
https://pubmed.ncbi.nlm.nih.gov/9930979