Wyniki wyszukiwania - AGRO

1

Determination of ATP in biological material by a bioluminescence method using a scintillation counter

100%

Skorko R.

Oceanologia

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1984

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tom 18

2

In vitro phosphorylation of alfa-preprotachykinin by protein kinase C

100%

Hrabec E., Hrabec Z., Lachowicz L., Greger J., Plucienniczak G., Plucienniczak A.

Acta Biochimica Polonica

|

1994

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tom 41

|

nr 2

3

Protein phosphorylation and signal transduction

100%

Krebs E. G.

Cellular and Molecular Biology Letters

|

1998

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tom 03

|

nr 3

4

Diacylglycerol signalling: targeting protein kinase C isozymes and 'non-kinase' diacylglycerol effectors

100%

Kazanietz M. G.

Cellular and Molecular Biology Letters

|

2005

|

tom 10

|

nr Suppl.2

5

Dissecting the functions of protein tyrosine phosphatases using chemical approaches

100%

Zhang Z. Y.

Cellular and Molecular Biology Letters

|

2005

|

tom 10

|

nr Suppl.2

6

Phosphorylation of A-proteins by protein kinases bound to yeast ribosomes

100%

Cytrynska M., Jakubowicz T., Gasior E.

Acta Biochimica Polonica

|

1994

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tom 41

|

nr 2

7

Regulation of synaptic functions by modification of postsynaptic density proteins

88%

Sheng M.

Acta Neurobiologiae Experimentalis

|

2009

|

tom 69

|

nr 3

Phosphorylation regulation of postsynaptic density proteins is likely to be a major means of regulating synaptic function. The PSD scaffold PSD-95, a powerful determinant of synaptic strength, is a case in point. Its precise role during synaptic plasticity (LTP versus LTD) has not been easy to interpret from overexpression, RNAi or knockout mice experiments. We found that the PSD scaffold PSD-95 is phosphorylated on multiple sites in cultured neurons and in vivo. Ser-295 phosphorylation, mediated by a Rac1-JNK1 MAP kinase pathway and countered by phosphatases PP1 or PP2A, promotes PSD-95 accumulation in synapses and is associated with LTP-inducing stimuli. More strikingly, LTD-inducing stimuli causes dephosphorylation of ser-295 rapidly and profoundly, correlating with activation of PP1. In addition, LTD was associated with phosphorylation of an N-terminal residue of PSD-95 by the protein kinase GSK3b. This site is also bidirectionally modulated by activity. A phospho-mimicking mutant of PSD-95 (S295DPSD-95; which cannot be “dephosphorylated”) impaired the internalization of AMPA receptors in cultured neurons and blocked the induction of LTD in cultured hippocampal slices. Our data indicate that dephosphorylation of PSD-95 on ser295, and phosphorylation of the N-terminus of PSD-95, is required for mobilization of PSD-95 from the PSD, de-anchoring of AMPA receptors from the PSD for internalization, and hence induction of LTD.

8

Signalling protein inhibitors via the combinatorial modification of peptide scaffolds

88%

Lawrence D. S.

Cellular and Molecular Biology Letters

|

2005

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tom 10

|

nr Suppl.2

9

Deoxycytidine kinase transfection and upregulation of thymidine kinase 2 increased sensitivity to cytidine analogues in resistant cells

88%

Van Der Wilt C. L., Loves W. J. P., Padron J., Talianidis I., Eriksson S., Peters G. J.

Cellular and Molecular Biology Letters

|

1999

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tom 04

|

nr 3

10

Substrate and inhibitor recognition of protein kinases: what in known about the catalytic subunit of phosphorylase kinase?

88%

Graves D. J., Bartleson C., Biorn A., Pete M.

Cellular and Molecular Biology Letters

|

1998

|

tom 03

|

nr 3

11

Bacterial serine and tyrosine protein kinases containing a walker motif

88%

Deutscher J.

Cellular and Molecular Biology Letters

|

2003

|

tom 08

|

nr 2A

12

Phosphorylation of yeast ribosomal proteins by CKI and CHII in the presence of heparin

88%

Wojda I., Cytrynska M., Frajnt M., Jakubowicz T.

Cellular and Molecular Biology Letters

|

1998

|

tom 03

|

nr 3

13

Crystal structure and function of 14-3-3 proteins: Role in coordinating signal transduction pathways

88%

Aitken A., Chaudhri M., Dubois T., Howell S., Kerai P., Scarabel M., Soneji Y., Rittinger K.

Cellular and Molecular Biology Letters

|

1997

|

tom 02

|

nr 2

14

Manipulation of alternative splicing by specific inhibitors of SR protein kinases

88%

Hagiwara M.

Cellular and Molecular Biology Letters

|

2005

|

tom 10

|

nr Suppl.2

15

Melatonin stimulates HSP27 phosphorylation in human pancreatic carcinoma cells [PANC-1]

75%

Leja-Szpak A., Jaworek J., Szklarczyk J., Konturek S. J., Pawlik W. W.

Journal of Physiology and Pharmacology. Supplement

|

2007

|

tom 58

|

nr 3

177-188

16

EHDs are serine phosphoproteins: EHD1 phosphorylation is enhanced by serum stimulation

75%

Fichtman B., Ravid L., Rapaport D., Horowitz M.

Cellular and Molecular Biology Letters

|

2008

|

tom 13

|

nr 4

632-648

Endocytic processes are mediated by multiple protein-protein interacting modules and regulated by phosphorylation and dephosphorylation. The Eps15 homology domain containing protein 1 (EHD1) has been implicated in regulating recycling of proteins, internalized both in clathrin-dependent and clathrin-independent endocytic pathways, from the recycling compartment to the plasma membrane. EHD1 was found in a complex with clathrin, adaptor protein complex-2 (AP-2) and insulin-like growth factor-1 receptor (IGF-1R), and was shown to interact with Rabenosyn-5, SNAP29, EHBP1 (EH domain binding protein 1) and syndapin I and II. In this study, we show that EHD1, like the other human EHDs, undergoes serine-phosphorylation. Our results also indicate that EHD1 is a serum-inducible serine-phosphoprotein and that PKC (protein kinase C) is one of its kinases. In addition, we show that inhibitors of clathrin-mediated endocytosis decrease EHD1 phosphorylation, while inhibitors of caveolinmediated endocytosis do not affect EHD1 phosphorylation. The results of experiments in which inhibitors of endocytosis were employed strongly suggest that EHD1 phosphorylation occurs between early endosomes and the endocytic recycling compartment.

17

Regulation of RNA polymerase III transcription by Maf1 protein

75%

Ciesla M., Boguta M.

Acta Biochimica Polonica

|

2008

|

tom 55

|

nr 2

215-225

Maf1 was the first protein discovered to regulate polymerase III RNA in yeast and because it is evolutionarily conserved, a Maf1 ortholog also serves to restrain transcription in mouse and human cells. Understanding the mechanism of the regulation has been made possible by recent studies showing that Maf1 is a nuclear/cytoplasmic protein whose subcellular distribution and hence negative regulation of Pol III transcription is mediated by the nutrient-sensing signaling pathways, TOR and RAS. Under stress conditions and during growth in a nonfermentable carbon source Maf1 is dephosphorylated and imported to the nucleus. In its non-phosphorylated form, Maf1 interacts with the polymerase III transcription machinery. Phosphorylation serves to locate Maf1 to the cytoplasm under favorable growth conditions, thereby preventing it from non-negatively regulating polymerase III when high levels of tRNA transcription are required. Relocation of Maf1 to the cytoplasm is dependent on Msn5, a carrier responsible for export of several other phosphoproteins out of the nucleus. The absence of Maf1-mediated control of tRNA synthesis impairs yeast viability in nonfermentable carbon sources. Moreover, in cells grown in a nonfer mentable carbon source, Maf1 regulates the levels of different tRNAs to various extents. This differential regulation may contribute to the physiological role of Maf1.

18

IL-39 increases ROS production and promotes the phosphorylation of p38 MAPK in the apoptotic cardiomyocytes

75%

Xiong W., Chen H., Lu J., Ren J., Nie C., Liang R., Liu F., Huang B., Luo Y.

Folia Histochemica et Cytobiologica

|

2021

|

tom 59

|

nr 3

19

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A new approach to phosphorylation of nucleosides using oxyonium phosphobetaines as intermediates

75%

Materna M., Stawinski J., Sobkowski M.

BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology

|

2023

|

tom 104

|

nr 1

20

Protein phosphatase 2A: Variety of forms and diversity of functions

75%

Lechward K., Awotunde O. S., Swiatek W., Muszynska G.

Acta Biochimica Polonica

|

2001

|

tom 48

|

nr 4

Protein phosphatase 2A (PP2A) comprises a diverse family of phosphoserine- and phosphothreonine-specific phosphatases present in all eukaryotic cells. All forms of PP2A contain a catalytic subunit (PP2Ac) which forms a stable complex with thestructural subunit PR65/A. The heterodimer PP2Ac-PR65/A associates with regulatory proteins, termed variable subunits, in order to form trimeric holoenzymes attributed with distinct substrate specificity and targeted to different subcellular compartments. PP2Ac activity can be modulated by reversible phosphorylation on Tyr307 and methylation on C-terminal Leu309. Studies on PP2A have shown that this enzyme may be implicated in the regulation of metabolism, transcription, RNA splicing, translation, differentiation, cell cycle, oncogenic transformation and signal transduction.

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