Wyniki wyszukiwania - Biblioteka Nauki

1

Cloning and characterization of the gene encoding ribosomal P0 phosphoprotein from Neurospora crassa.

100%

Krokowski D. , Tchórzewski M. , Grankowski N.

Acta Biochimica Polonica

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2002

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tom 49

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nr 1

11-18

EN

A gene for ribosomal protein P0 that belongs to the family of ribosomal P proteins was isolated from a Neurospora crassa cDNA library, using polyclonal antibodies against recombinant P0 protein from Saccharomyces cerevisiae. This is the first gene for ribosomal P0 protein to be cloned from filamentous fungi. The derived P0 protein sequence has a strong homology to other eukaryotic P0 proteins; yet, there is a notable alteration in the conservative C-terminal region, placing this protein among the unique sequences from protozoan parasites.

2

New Aspects Connected with the Synthesis of H-Phosphinate Anhydrides

100%

Nycz J. E.

Polish Journal of Chemistry

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2009

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tom Vol. 83, nr 4

589-594

EN

A novel reaction between sodium salt of phenylphosphinic acid PhP(O)(OH)H (1) and various phosphorus electrophiles, R2P(O)Cl (2; R = alkyl, aryl, alkoxy or aryloxy) has been described. The presented reaction showed a high selectivity (yield up to 96 per cent) in the products of the symmetric phosphorus an hydrides, R2P(O)-O-(O)PR2 (4), which preferentially come from the starting phosphorus electrophiles (2). The results demonstrate that the phosphorus-phosphorus mixed an hydrides, RPH(O)-O-(O)PR2 (3) are unstable under basic condition and possibly decomposed with expulsion of a phosphinylidene (Ph-P=O) fragment (6).

3

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

4

In vitro phosphorylation of alfa-preprotachykinin by protein kinase C

100%

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

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nr 2

5

Protein phosphorylation and signal transduction

100%

Krebs E. G.

Cellular and Molecular Biology Letters

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1998

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tom 03

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nr 3

6

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

100%

Kazanietz M. G.

Cellular and Molecular Biology Letters

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2005

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tom 10

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nr Suppl.2

7

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

100%

Cytrynska M. , Jakubowicz T. , Gasior E.

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nr 2

8

Regulation of synaptic functions by modification of postsynaptic density proteins

88%

Sheng M.

Acta Neurobiologiae Experimentalis

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2009

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tom 69

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nr 3

EN

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.

9

High sequence homology between protein tyrosine acid phosphatase from boar seminal vesicles and human prostatic acid phosphatase

88%

Wysocki P. , Płucienniczak G. , Strzeżek J.

Acta Biochimica Polonica

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2009

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tom 56

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nr 3

481-486

EN

Boar seminal vesicle protein tyrosine acid phosphatase (PTAP) and human prostatic acid phosphatase (PAP) show high affinity for protein phosphotyrosine residues. The physico-chemical and kinetic properties of the boar and human enzymes are different. The main objective of this study was to establish the nucleotide sequence of cDNA encoding boar PTAP and compare it with that of human PAP cDNA. Also, the amino-acid sequence of boar PTAP was compared with the sequence of human PAP. PTAP was isolated from boar seminal vesicle fluid and sequenced. cDNA to boar seminal vesicle RNA was synthesized, amplified by PCR, cloned in E. coli and sequenced. The obtained N-terminal amino-acid sequence of boar PTAP showed 92% identity with the N-terminal amino-acid sequence of human PAP. The determined sequence of a 354 bp nucleotide fragment (GenBank accession number: GQ184596) showed 90% identity with the corresponding sequence of human PAP. On the basis of this sequence a 118 amino acid fragment of boar PTAP was predicted. This fragment showed 89% identity with the corresponding fragment of human PAP and had a similar hydropathy profile. The compared sequences differ in terms of their isoelectric points and amino-acid composition. This may explain the differences in substrate specificity and inhibitor resistance of boar PTAP and human PAP.

10

Protein kinases CKI and CKII are implicated in modification of ribosomal proteins of the yeast Trichosporon cutaneum

88%

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

Acta Biochimica Polonica

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2002

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tom 49

|

nr 4

947-957

EN

Phosphorylation of acidic ribosomal proteins P1/P2-P0 is a common phenomenon in eukaryotic organisms. It was found previously that in Trichosporon cutaneum, unlike in other yeast species, in addition to the two acidic ribosomal proteins, two other proteins of 15 kDa and 19 kDa of the small ribosomal subunit were phosphorylated. Here we describe two protein kinases: CKI and CKII, which are engaged in the modification of T. cutaneum ribosomal proteins. The acidic ribosomal proteins and the protein of 19 kDa were modified by CKII associated with ribosomes, while the protein of 15 kDa was modified by CKI. Protein kinase CKI was purified from cell-free extract (CKIC) and from ribosomal fraction (CKIR). The molecular mass of CKIC was established at 33 kDa while that of CKIR at 35-37 kDa. A protein of 40 kDa copurified with CKIR but not CKIC. Heparin significantly increased 40 kDa protein phosphorylation level by CKIR. Microsequencing analysis revealed the presence of CKI recognition motifs in the N-terminal fragment of the 40 kDa protein.

11

A New Strategy for the Synthesis of Pyridine Amides, Phosphorylated Quinoline Amides and Their Thio-Analogues

88%

Nycz J. E.

Polish Journal of Chemistry

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2009

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tom Vol. 83, nr 9

1637-1642

EN

A new strategy for the synthesis of pyridine amides, phosphorylated quinoline amides and their thio-analogues has been developed. The direct reaction between in situ generated mixed phosphoric-carboxylic anhydrides with primary amines al lowed a simultaneous phosphorylation (thiophosphorylation) and amidation of hydroxyquinoline acids. In the absence of hydroxyl group, quinoline and pyridine acids were smoothly converted into amides.

12

Rabbit muscle fructose-1,6-bisphosphatase is phosphorylated in vivo.

88%

Rakus D. , Zarzycki M. , Dzugaj A.

Acta Biochimica Polonica

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2003

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tom 50

|

nr 1

115-121

EN

Phosphorylated fructose-1,6-bisphosphatase (FBPase) was isolated from rabbit muscle in an SDS/PAGE homogeneous form. Its dephosphorylation with alkaline phosphatase revealed 2.8 moles of inorganic phosphate per mole of FBPase. The phosphorylated FBPase (P-FBPase) differs from the dephosphorylated enzyme in terms of its kinetic properties like Km and kcat, which are two times higher for the phosphorylated FBPase, and in the affinity for aldolase, which is three times lower for the dephosphorylated enzyme. ephosphorylated FBPase can be a substrate for protein kinase A and the amount of phosphate incorporated per FBPase monomer can reach 2-3 molecules. Since interaction of muscle aldolase with muscle FBPase results in desensitisation of the latter toward AMP inhibition (Rakus & Dzugaj, 2000, Biochem. Biophys. Res. Commun. 275, 611-616), phosphorylation may be considered as a way of muscle FBPase activity regulation.

13

C-Phosphorylated Azoles

88%

Pinchuk A. , Yurchenko A. A. , Oshovsky G. V. , Zarudnitskii E. V. , Pushechnikov A. O. , Tolmachev A. A.

Polish Journal of Chemistry

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2001

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tom Vol. 75, nr 8

1137-1146

EN

A method of phosphorylation of heterocycles incorporating 1,3-azole moiety with phosphorus( III) halides is elaborated. As a result, previously unknown azolyldihalogenphosphines are prepared. Influence of heteroatom and quantity of nitrogen atoms in a cycle on the activity of azoles is studied. Reaction of 5-aminopyrazole derivatives with phosphorus(III) halides affords novel phosphorus-containing bi- and tricyclic fused systems

14

Bacterial serine and tyrosine protein kinases containing a walker motif

88%

Deutscher J.

Cellular and Molecular Biology Letters

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2003

|

tom 08

|

nr 2A

15

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

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1997

|

tom 02

|

nr 2

16

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

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1999

|

tom 04

|

nr 3

17

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

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1998

|

tom 03

|

nr 3

18

Manipulation of alternative splicing by specific inhibitors of SR protein kinases

88%

Hagiwara M.

Cellular and Molecular Biology Letters

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2005

|

tom 10

|

nr Suppl.2

19

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

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1998

|

tom 03

|

nr 3

20

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

75%

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

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nr 4

632-648

EN

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.