Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Garik Y. Gdalevsky"'
Autor:
Garik Y. Gdalevsky, Yehuda Goldgur, Rivka Cohen-Luria, Shmuel Bittner, Abraham H. Parola, Roni Scherzer
Publikováno v:
Journal of Enzyme Inhibition and Medicinal Chemistry. 24:350-355
Tryptophanase (tryptophan indole-lyase, Tnase, EC 4.1.99.1), a bacterial enzyme with no counterpart in eukaryotic cells, produces from L-tryptophan pyruvate, ammonia and indole. It was recently suggested that indole signaling plays an important role
Autor:
Yehuda Goldgur, Rivka Cohen-Luria, Anna Kogan, Juha P. Himanen, Natalia Tsesin, Orna Almog, Garik Y. Gdalevsky, Abraham H. Parola
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 63:969-974
The crystal structure of apo tryptophanase from Escherichia coli (space group F222, unit-cell parameters a = 118.4, b = 120.1, c = 171.2 A) was determined at 1.9 A resolution using the molecular-replacement method and refined to an R factor of 20.3%
Autor:
Yehuda Goldgur, Leah Raznov, Rivka Cohen-Luria, Orna Almog, Garik Y. Gdalevsky, Abraham H. Parola, Anna Kogan
Two crystal forms ofEscherichia colitryptophanase (tryptophan indole-lyase, Trpase) were obtained under the same crystallization conditions. Both forms belonged to the same space groupP43212 but had slightly different unit-cell parameters. The holo c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::74fda128cac643ae7fb969f954b45e37
https://europepmc.org/articles/PMC4356303/
https://europepmc.org/articles/PMC4356303/
Autor:
Stanislav Engel, Robert S. Marks, Alona Kuzmina, Maria Vyazmensky, Karin Vaknin, Ran Taube, Garik Y. Gdalevsky
Publikováno v:
PLoS ONE
PLoS ONE, Vol 10, Iss 12, p e0144043 (2015)
PLoS ONE, Vol 10, Iss 12, p e0144043 (2015)
Chemokine G protein coupled receptors, principally CCR5 or CXCR4, function as co-receptors for HIV-1 entry into CD4+ T cells. Initial binding of the viral envelope glycoprotein (Env) gp120 subunit to the host CD4 receptor induces a cascade of structu
Publikováno v:
Journal of Biological Chemistry. 281:12526-12534
DnaA is the initiator protein for chromosomal replication in bacteria; its activity plays a central role in the timing of the primary initiations within the Escherichia coli cell cycle. A controlled, reversible conversion between the active ATP-DnaA
Autor:
Garik Y. Gdalevsky, J Voorspoels, Joseph Kost, Jean Paul Remon, Julia Peisahov-Korol, Ygal Gilboa, Shimona Geresh
Publikováno v:
Journal of Applied Polymer Science. 86:1157-1162
60Co-gamma-radiation and ceric ammonium nitrate (CAN) redox-induced graft polymerization of acrylic monomers (acrylonitrile, acrylic acid, and methyl acrylate) to starch was performed to produce drug-delivery systems. The grafted starches obtained ma
Autor:
Chithra Hariharan, Dina Pines, Tali Erez, Abraham H. Parola, Ehud Pines, Garik Y. Gdalevsky, Robert S. Phillips, Rivka Cohen-Luria
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1594:335-340
The phenomenon of cold scission or cold lability, which entails a widespread variety of oligomeric enzymes, is still enigmatic. The effect of cooling on the activity and the quaternary structure of the pyridoxal 5'-phosphate (PLP)-dependent enzyme, t
Autor:
Keren Green, Nasrin Qasem, Anna Kogan, Orna Almog, Garik Y. Gdalevsky, Yehuda Goldgur, Ofra Lotan, Abraham H. Parola
Publikováno v:
Biophysical Journal. 112:359a
Tryptophanase (Trpase) is a pyridoxal 5′-phosphate (PLP)-dependent homotetrameric enzyme which catalyzes the degradation of l-tryptophan. Trpase is known for its cold lability, i.e., a reversible loss of activity at low temperature (2°C), associat
Autor:
Robert S. Phillips, Ariela Markel, Yuri M. Torchinsky, Tali Ben-Kasus, Abraham H. Parola, Garik Y. Gdalevsky
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1294:147-152
The reaction of tryptophanase and its W330F and W248F mutant forms with quasi-substrates forming an external pyridoxal phosphate aldimine or quinonoid is accompanied by the appearance of a positive circular dichroism (CD) peak at 290 nm. The peak see
Autor:
Yehuda Goldgur, Robert S. Phillips, Orna Almog, Garik Y. Gdalevsky, Abraham H. Parola, Anna Kogan, Rivka Cohen-Luria
Publikováno v:
BMC Structural Biology, Vol 9, Iss 1, p 65 (2009)
BMC Structural Biology
BMC Structural Biology
Background Oligomeric enzymes can undergo a reversible loss of activity at low temperatures. One such enzyme is tryptophanase (Trpase) from Escherichia coli. Trpase is a pyridoxal phosphate (PLP)-dependent tetrameric enzyme with a Mw of 210 kD. PLP i