Zobrazeno 1 - 10
of 52
pro vyhledávání: '"F J Kézdy"'
Publikováno v:
Journal of Lipid Research, Vol 20, Iss 2, Pp 143-153 (1979)
Externí odkaz:
https://doaj.org/article/ac7efccf6ed34c018cb491f76c112605
Autor:
Paul Greengard, F J Kézdy, M F Ho, Emil Thomas Kaiser, Andrew J. Czernik, W Schiebler, Martin Bähler
Publikováno v:
Journal of Biological Chemistry. 266:5600-5607
Synapsin I is a neuron-specific phosphoprotein localized on the surface of small synaptic vesicles to which it binds with high affinity (Kd = 10 nM). Synapsin I exhibits a tendency to self-associate, suggesting that it might have amphiphilic properti
Autor:
F J Kézdy, Shinji Yokoyama
Publikováno v:
Journal of Biological Chemistry. 266:4303-4308
The behavior of phosphatidylcholine monolayers at the air/water interface was studied by measuring their surface isotherm, surface potential, surface viscosity, and rate of hydrolysis by the dimeric phospholipase A2 from the venom of Crotalus atrox.
Publikováno v:
Journal of Biological Chemistry. 265:3628-3635
The covalent structure of bovine lens aldose reductase (alditol-NADP+ oxidoreductase, EC 1.1.1.21) was determined by sequence analysis of peptides generated by specific and chemical cleavage of the homogeneous apoenzyme. Peptides, purified by reverse
Publikováno v:
Glycoconjugate journal. 16(2)
The in vitro and in vivo specificity of the family of peptide:N-acetylgalactosaminyltransferases (GalNAcT) is analyzed on the basis of the reactivity and/or inhibitory activity of peptides and protein segments. The transferases appear to be multi-sub
Publikováno v:
The Journal of biological chemistry. 268(14)
The acceptor substrate specificity of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase (GalNAc-transferase) was inferred from the amino acid sequences surrounding 196 O-glycosylation sites extracted from the National Biomedical Research Found
Publikováno v:
Biotechnology and applied biochemistry. 17(1)
The polymerase domain of the human immunodeficiency virus type 1 (HIV-1) reverse transcriptase, called the p51 reverse transcriptase (p51 RT), was expressed in Escherichia coli. The recombinant protein also contained an N-terminal affinity tag design
Publikováno v:
The Journal of biological chemistry. 267(1)
The bisheteroarylpiperazines (BHAPs) are potent inhibitors of human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) and specifically block HIV-1 replication (Romero, D. L., Busso, M., Tan, C.-K., Reusser, F., Palmer, J. R., Poppe, S.
Publikováno v:
The Journal of biological chemistry. 266(24)
Human immunodeficiency virus 1 (HIV-1) protease is an aspartyl protease composed of two identical protomers linked by a four-stranded antiparallel beta-sheet consisting of the NH2- and COOH-terminal segments (Weber, I.T. (1990) J. Biol. Chem. 265, 10
Publikováno v:
The Journal of biological chemistry. 266(22)
Statistical analysis of an expanded data base of regions in viral polyproteins and in non-viral proteins that are sensitive to hydrolysis by the protease from human immunodeficiency virus (HIV) type 1 has generated a model which characterizes the sub