Zobrazeno 1 - 10
of 33
pro vyhledávání: '"A E, Granovsky"'
Publikováno v:
Applied Biochemistry and Microbiology. 58:738-743
Abstract A monomeric sensor, TagRFP-23-Ultramarine (TR-23-U), for effector caspase-3 was obtained. The overlap integrals of new pairs of red fluorescent protein TagRFP with four chromoproteins were calculated. The monomeric state of the Ultramarine p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2ce7d5006b73bf8364e20064f0e13cde
https://doi.org/10.1134/s0003683822060084
https://doi.org/10.1134/s0003683822060084
Autor:
Anne N Shemon, Gary L Heil, Alexey E Granovsky, Mathew M Clark, Dan McElheny, Alexander Chimon, Marsha R Rosner, Shohei Koide
Publikováno v:
PLoS ONE, Vol 5, Iss 5, p e10479 (2010)
BackgroundRaf kinase inhibitory protein (RKIP), also known as phoshaptidylethanolamine binding protein (PEBP), has been shown to inhibit Raf and thereby negatively regulate growth factor signaling by the Raf/MAP kinase pathway. RKIP has also been sho
Externí odkaz:
https://doaj.org/article/599a1f1f544e4bb28a7ae4ba60f27bbd
Autor:
I. M. Tsfasman, L. A. Krasovskaya, Irina V. Kudryakova, Igor E. Granovsky, O. A. Stepnaya, Yulia S. Lapteva, Natalia V. Vasilyeva
Publikováno v:
Microbial Physiology. 25:244-252
Development of an efficient expression system for (especially secreted) bacterial lytic enzymes is a complicated task due to the specificity of their action. The substrate for such enzymes is peptidoglycan, the main structural component of bacterial
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5110a85c96001ee644ef4139d55954c0
https://doi.org/10.1159/000381266
https://doi.org/10.1159/000381266
Autor:
T. A. Muranova, I. E. Granovsky, I. M. Tsfasman, M. G. Shlyapnikov, Yu. S. Lapteva, O. E. Zolova, Igor S. Kulaev, O. A. Stepnaya
Publikováno v:
Applied and Environmental Microbiology. 78:7082-7089
Lytic enzymes are the group of hydrolases that break down structural polymers of the cell walls of various microorganisms. In this work, we determined the nucleotide sequences of the Lysobacter sp. strain XL1 alpA and alpB genes, which code for, resp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::997e3b18e4c87261c49c93d1e2d2fe77
https://doi.org/10.1128/aem.01621-12
https://doi.org/10.1128/aem.01621-12
Autor:
Irina M, Tsfasman, Yulia S, Lapteva, Ludmila A, Krasovskaya, Irina V, Kudryakova, Natalia V, Vasilyeva, Igor E, Granovsky, Olga A, Stepnaya
Publikováno v:
Journal of molecular microbiology and biotechnology. 25(4)
Development of an efficient expression system for (especially secreted) bacterial lytic enzymes is a complicated task due to the specificity of their action. The substrate for such enzymes is peptidoglycan, the main structural component of bacterial
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::df3a78ce763a446cbb01f51fb762fb37
https://pubmed.ncbi.nlm.nih.gov/26138026
https://pubmed.ncbi.nlm.nih.gov/26138026
Publikováno v:
Biochemistry. 42:3305-3310
Photoreceptor cGMP phosphodiesterase (PDE6) is the effector enzyme in the vertebrate visual transduction cascade. The activity of rod PDE6 catalytic alpha- and beta-subunits is blocked in the dark by two inhibitory Pgamma-subunits. The inhibition is
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::274278a33bf73f6b956e8f6c24c008bf
https://doi.org/10.1021/bi027095x
https://doi.org/10.1021/bi027095x
Publikováno v:
Biochemistry. 40:13209-13215
In response to light, a photoreceptor G protein, transducin, activates cGMP-phosphodiesterase (PDE6) by displacing the inhibitory gamma-subunits (Pgamma) from the enzyme's catalytic sites. Evidence suggests that the activation of PDE6 involves a conf
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aeac95b1897eead6fa2c0a6610359774
https://doi.org/10.1021/bi011127j
https://doi.org/10.1021/bi011127j
Publikováno v:
Journal of Biological Chemistry. 276:21698-21703
Photoreceptor cGMP phosphodiesterases (PDE6) are uniquely qualified to serve as effector enzymes in the vertebrate visual transduction cascade. In the dark-adapted photoreceptors, the activity of PDE6 is blocked via tight association with the inhibit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d082a10ae5674eb7719862aeb30357ea
https://doi.org/10.1074/jbc.m100626200
https://doi.org/10.1074/jbc.m100626200
Publikováno v:
Journal of Biological Chemistry. 274:7865-7869
The visual GTP-binding protein, transducin, couples light-activated rhodopsin (R*) with the effector enzyme, cGMP phosphodiesterase in vertebrate photoreceptor cells. The region corresponding to the alpha4-helix and alpha4-beta6 loop of the transduci
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9d092a0dde9c584a668ef091384399db
https://doi.org/10.1074/jbc.274.12.7865
https://doi.org/10.1074/jbc.274.12.7865
Autor:
Alexey E. Granovsky, Tamara L. Haik, Nikolai O. Artemyev, Jackie D. Corbin, Randall L. McEntaffer, Sharron H. Francis, Michael Natochin
Publikováno v:
Journal of Biological Chemistry. 273:24485-24490
Chimeric cGMP phosphodiesterases (PDEs) have been constructed using components of the cGMP-binding PDE (PDE5) and cone photoreceptor phosphodiesterase (PDE6alpha') in order to study structure and function of the photoreceptor enzyme. A fully function
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8633d961bf86099b4dcf2ce628417572
https://doi.org/10.1074/jbc.273.38.24485
https://doi.org/10.1074/jbc.273.38.24485