Výsledky vyhledávání - "J R, Vandenheede"

The somatostatin analogue TT-232 induces apoptosis in A431 cells: sustained activation of stress-activated kinases and inhibition of signalling to extracellular signal-regulated kinases

Autor: T, Vántus, G, Kéri, Z, Krivickiene, M, Valius, A, Steták, S, Keppens, P, Csermely, P I, Bauer, G, Bökönyi, W, Declercq, P, Vandenabeele, W, Merlevede, J R, Vandenheede

Publikováno v: Cellular signalling. 13(10)

TT-232 is a somatostatin analogue containing a five-residue ring structure. The present report describes TT-232-induced signalling events in A431 cells, where a 4-h preincubation with the peptide irreversibly induced a cell death program, which invol

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::bb8a67f0ebdb7fc61f9ed691c0e19652
https://pubmed.ncbi.nlm.nih.gov/11602182

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Regulation of protein kinase D by multisite phosphorylation. Identification of phosphorylation sites by mass spectrometry and characterization by site-directed mutagenesis

Autor: D, Vertommen, M, Rider, Y, Ni, E, Waelkens, W, Merlevede, J R, Vandenheede, J, Van Lint

Publikováno v: The Journal of biological chemistry. 275(26)

Activation of the serine/threonine kinase, protein kinase D (PKD/PKC mu) via a phorbol ester/PKC-dependent pathway involves phosphorylation events. The present study identifies five in vivo phosphorylation sites by mass spectrometry, and the role of

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::5662dddd9c8cdc832928744c9117a885
https://pubmed.ncbi.nlm.nih.gov/10867018

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Tumor necrosis factor stimulates multiple serine/threonine protein kinases in Swiss 3T3 and L929 cells. Implication of casein kinase-2 and extracellular signal-regulated kinases in the tumor necrosis factor signal transduction pathway

Autor: J, Van Lint, P, Agostinis, V, Vandevoorde, G, Haegeman, W, Fiers, W, Merlevede, J R, Vandenheede

Publikováno v: The Journal of biological chemistry. 267(36)

Incubation of Swiss 3T3 or L929 cells with tumor necrosis factor (TNF) leads to the rapid stimulation of several cytosolic Ser/Thr kinases active toward myelin basic protein, the S6 peptide (RRLSSLR), the G peptide (SPQPSRRGSESSEE), and Kemptide (LRR

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::164c50f0497d1432df0cbf6e7a741ac0
https://pubmed.ncbi.nlm.nih.gov/1281478

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Rapid stimulation of Ser/Thr protein kinases following treatment of Swiss 3T3 cells with bombesin. Involvement of casein kinase-2 in the signaling pathway of bombesin

Autor: P, Agostinis, J, Van Lint, S, Sarno, P, De Witte, J R, Vandenheede, W, Merlevede

Publikováno v: The Journal of biological chemistry. 267(14)

Treatment of quiescent Swiss 3T3 mouse fibroblasts with bombesin resulted in a rapid 6-8-fold stimulation of cytosolic Ser/Thr kinase activities toward the S6 peptide (RRLSSLR), myelin basic protein (MBP), and the G peptide (SPQPSRRGSESSEE). Anion ex

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::64fc9208b68ed578666fdb08cc08bd62
https://pubmed.ncbi.nlm.nih.gov/1577810

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Studies on the role of adenosine 3':5'-monophosphate in the activation of liver phosphorylase

Autor: J R, Vandenheede, R L, Khandelwal, E G, Krebs

Publikováno v: The Journal of biological chemistry. 252(21)

Crude extracts of rabbit liver, preincubated to promote the dephosphorylation of enzymes or other regulatory proteins, were used to study the role of cyclic AMP in the activation of glycogen phosphorylase. Inasmuch as endogenous liver phosphorylase w

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::5fab5dfa556c4867cbccea148aa74d6d
https://pubmed.ncbi.nlm.nih.gov/199589

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ATP x Mg-dependent protein phosphatase from rabbit skeletal muscle. II. Purification of the activating factor and its characterization as a bifunctional protein also displaying synthase kinase activity

Autor: J R, Vandenheede, S D, Yang, J, Goris, W, Merlevede

Publikováno v: The Journal of biological chemistry. 255(24)

A protein (FA) has been isolated from rabbit muscle which has two functions: one is the activation of the ATP x Mg-dependent phosphatase (see previous paper) (1) and the second is the phosphorylation and concomitant inactivation of glycogen synthase,

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::cc78762ce88c1c880379a12a57e5bde5
https://pubmed.ncbi.nlm.nih.gov/6254982

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A synthetic peptide substrate specific for casein kinase I

Autor: P, Agostinis, L A, Pinna, F, Meggio, O, Marin, J, Goris, J R, Vandenheede, W, Merlevede

The synthetic peptide, Asp-Asp-Asp-Glu-Glu-Ser-Ile-Thr-Arg-Arg, derived from the phosphorylation site of casein kinase-1 (CK-1) in beta-casein A(2), is readily phosphorylated by CK-1, but not by casein kinase-2(CK-2), cyclic AMP-dependent protein kin

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::009f65b205ea3928cf2155437cd914af
http://hdl.handle.net/11577/2509182

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