Results 331 to 340 of about 8,324,980 (383)
Disrupting ZBTB7A or BCL11A binding sites reactivates fetal hemoglobin in erythroblasts from healthy and β<sup>0</sup>-thalassemia/HbE individuals. [PDF]
Sci RepWongborisuth C +11 more
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Nucleosome binding by TP53, TP63, and TP73 is determined by the composition, accessibility, and helical orientation of their binding sites. [PDF]
Genome ResWilson PD, Yu X, Handelmann CR, Buck MJ.
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Localization of the binding site on fibrin for the secondary binding site of thrombin
Biochemistry, 1988Affinity chromatography of active site inhibited thrombin on immobilized fragments derived from the central (desAB-NDSK) and terminal (D1) globular domains of fibrinogen revealed that the site responsible for the binding of thrombin at its secondary fibrin binding site is located in the central domain.
Zsofia Vali, Harold A. Scheraga
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Brain leukotriene C4 binding sites are S-alkylglutathione binding sites
European Journal of Pharmacology, 1989Leukotriene C4 binding to mouse brain membranes was readily displaced by S-alkylglutathione derivatives, with the affinity of the test compound increasing as the alkyl chain length increases. S-decylglutathione was as potent as leukotriene C4. These data suggest that brain membrane leukotriene C4 binding sites are S-alkylglutathione binding sites ...
Ahn Nguyen, AndréM. Goffinet
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Cancer Letters, 1996
Cryptophycin 1 is a new cytotoxic antimicrotubule agent with excellent antitumor activity. The methods of Sackett (Biochemistry, 34, 7010-7019, 1995), utilizing the selective and specific proteolysis of alpha- and beta-tubulin by trypsin and chymotrypsin, was used to identify the cryptophycin 1 binding site on tubulin.
Christy R. Taoka +2 more
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Cryptophycin 1 is a new cytotoxic antimicrotubule agent with excellent antitumor activity. The methods of Sackett (Biochemistry, 34, 7010-7019, 1995), utilizing the selective and specific proteolysis of alpha- and beta-tubulin by trypsin and chymotrypsin, was used to identify the cryptophycin 1 binding site on tubulin.
Christy R. Taoka +2 more
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Anatomy of lipase binding sites: the scissile fatty acid binding site
Chemistry and Physics of Lipids, 1998Shape and physico-chemical properties of the scissile fatty acid binding sites of six lipases and two serine esterases were analyzed and compared in order to understand the molecular basis of substrate specificity. All eight serine esterases and lipases have similar architecture and catalytic mechanism of ester hydrolysis, but different substrate ...
Markus Fischer +2 more
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Biochemical and Biophysical Research Communications, 1980
Abstract An examination of the effect of dibutylchloromethyltin/chloride on the carbodiimide binding proteolipid of mitrochondrial ATPase has revealed that in the presence of the alkyltin, (1) binding of dicyclohexycarbodiimide is decreased (2) the electron spin resonance spectrum of a nitroxide analogue of dicyclohexylcarbodiimide exhibits line ...
Michael D. Partis +3 more
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Abstract An examination of the effect of dibutylchloromethyltin/chloride on the carbodiimide binding proteolipid of mitrochondrial ATPase has revealed that in the presence of the alkyltin, (1) binding of dicyclohexycarbodiimide is decreased (2) the electron spin resonance spectrum of a nitroxide analogue of dicyclohexylcarbodiimide exhibits line ...
Michael D. Partis +3 more
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1996
This chapter assesses advances in the understanding and manipulation of antibody binding sites and variable regions. The antigen binding region of an antibody reduced to a 25-kDa minimum comprises of a noncovalent heterodimer of V H and V L domains.
Edgar Haber +2 more
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This chapter assesses advances in the understanding and manipulation of antibody binding sites and variable regions. The antigen binding region of an antibody reduced to a 25-kDa minimum comprises of a noncovalent heterodimer of V H and V L domains.
Edgar Haber +2 more
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What makes a binding site a binding site?
Current Opinion in Structural Biology, 1995Organic probe molecules have recently been used to define hydrophobic binding sites on the surface of proteins. It appears that the presence of water on the surface of a protein plays a crucial role in the interaction between that protein and its binding site.
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