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001-es BibID:	BIBFORM102978
035-os BibID:	(WOS)A1985AUT4000020 (Scopus)0022395124
Első szerző:	Gergely Pál (biokémikus)
Cím:	Effect of fructose 1-phosphate on the activation of liver glycogen synthase / Pál Gergely, Béla Tóth, Ilona Farkas, György Bot
Dátum:	1985
ISSN:	0264-6021 1470-8728
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk
Megjelenés:	Biochemical Journal. - 232 : 1 (1985), p. 133-137. -
További szerzők:	Tóth Béla (1954-) (vegyész, biokémikus) Farkas Ilona (1953-) (biokémikus) Bot György (1917-1998) (biokémikus, vegyész)
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001-es BibID:	BIBFORM028726
Első szerző:	Kiss Enikő
Cím:	Integrin-linked kinase phosphorylates the myosin phosphatase target subunit at the inhibitory site in platelet cytoskeleton / Enikő Kiss, Andrea Murányi, Csilla Csortos, Pál Gergely, Masaaki Ito, David J. Hartshorne, Ferenc Erdődi
Dátum:	2002
ISSN:	0264-6021
Megjegyzések:	The myosin phosphatase (MP) composed of the catalytic subunit of type 1 protein phosphatase and myosin phosphatase target subunit isoform 1 (MYPT1) was identified as the major serine/threonine phosphatase component in the platelet-cytoskeleton fraction. MYPT1 was phosphorylated by cytoskeletal kinase(s), but the identity of the kinase(s) and the effect of phosphorylation were not established. Incubation of platelet-cytoskeletal fraction with MgATP or MgATP[S] (magnesium adenosine 5'-[gamma-thio]triphosphate) caused a decrease in the 20 kDa light-chain of smooth-muscle myosin (MLC20) phosphatase and phosphorylase phosphatase activities. MYPT1 contains a phosphorylation site, Thr-695, involved in the inhibition of MP in a RhoA/Rho kinase-dependent manner. The cytoskeletal kinase(s) phosphorylated Thr-695 of glutathione S-transferase (GST)-MYPT1, as determined with an antibody specific for phosphorylated Thr-695. The level of Rho kinase was low in the cytoskeletal fraction and was detected primarily in the membrane and cytosolic fractions. The phosphorylation of Thr-695 by the cytoskeletal kinase(s) was not affected by Rho kinase inhibitor, Y-27632, suggesting that kinase(s) other than Rho kinase were involved. In-gel kinase assay identified a kinase at 54-59 kDa that phosphorylated the C-terminal fragment of MYPT1 (GST-MYPT1(667-1004)). Western blots detected both zipper-interacting protein kinase (ZIPK) and integrin-linked kinase (ILK) at 54-59 kDa in the cytoskeleton and membrane fractions. Cytoskeletal ZIPK and ILK were separated and partially purified by chromatography on SP-Sepharose and on MonoQ. ZIPK preferentially phosphorylated MLC20 and had low activity on MYPT1. ILK phosphorylated both MLC20 and MYPT1 and phosphorylation of MYPT1 occured on Thr-695. The above results raise the potential for regulation of MP activity in platelet cytoskeleton by ILK and suggest an alternative to the Rho-linked pathway.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban egyetemen (Magyarországon) készült közlemény
Megjelenés:	Biochemical Journal. - 365 : 1 (2002), p. 79-87. -
További szerzők:	Murányi Andrea (1966-) (biokémikus) Ito, Masaaki Hartshorne, David J. Erdődi Ferenc (1953-) (biokémikus) Csortos Csilla (1956-) (biokémikus) Gergely Pál (1947-) (biokémikus)
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001-es BibID:	BIBFORM028868
Első szerző:	Murányi Andrea (biokémikus)
Cím:	Identification and localization of myosin phosphatase in human platelets / Andrea Murányi, Ferenc Erdődi, Masaaki Ito, Pál Gergely, David J. Hartshorne
Dátum:	1998
ISSN:	0264-6021
Megjegyzések:	Type 1 (PP1) and type 2A (PP2A) phosphatase activity was measured in three subcellular fractions of human platelets. About 80% of the activity was in the high-speed supernatant. Western blots showed that the catalytic subunit of PP1 (PP1c), including alpha- and delta-isoforms, was present in each fraction, but the level of the catalytic subunit of PP2A was very low in the low-speed pellet (cytoskeletal fraction). Various antibodies detected a subunit similar to the 130 kDa subunit (M130) of myosin phosphatase (MP) of smooth muscle in the low- and the high-speed pellets of human platelets. PP1c and associated proteins were isolated by microcystin-Sepharose. Many proteins were separated from each fraction, including myosin, actin and PP1c. M130 was separated only from the low-speed and the high-speed pellets. Kinase activities were detected in the unbound fractions, and fractions from the low- and high-speed pellets phosphorylated M130 and myosin respectively. Treatment of platelets with calyculin A increased the phosphorylation level of many proteins, including myosin heavy- and light-chains, and caused association of cytoskeletal proteins with the low-speed pellet. No marked change in the distribution of PP1c and M130 was detected. These results suggest that the MP in human platelets is composed of PP1c plus a subunit similar to M130 of the smooth muscle phosphatase.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban egyetemen (Magyarországon) készült közlemény
Megjelenés:	The Biochemical Journal. - 330 : 1 (1998), p. 225-231. -
További szerzők:	Ito, Masaaki Hartshorne, David J. Erdődi Ferenc (1953-) (biokémikus) Gergely Pál (1947-) (biokémikus)
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001-es BibID:	BIBFORM028090
Első szerző:	Zor, Uriel
Cím:	Reactive oxygen species mediate phorbol ester-regulated tyrosine phosphorylation and phospholipase A2 activation : potentiation by vanadate / Uriel Zor, Ernst Ferber, Pál Gergely, Kornélia Szűcs, Viktor Dombrádi, Rachel Goldman
Dátum:	1993
ISSN:	0264-6021
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban phospholipase A2 ROS PLA2
Megjelenés:	Biochemical Journal. - 295 (1993), p. 879-888. -
További szerzők:	Ferber, Ernst Goldman, Rachel Gergely Pál (1947-) (biokémikus) Szűcs Kornélia (1945-) (biokémikus) Dombrádi Viktor (1953-) (biokémikus)
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