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10 Acta Biochimica Polonica

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The phosphorylation sites of ribosomal P proteins from Saccharomyces cerevisiae cells by endogenous CK-2, PK60S and RAP protein kinases

100%

Boguszewska A. , Szyszka R. , Grankowski N.

Acta Biochimica Polonica

1997

tom 44

nr 2

191-200

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

100%

Krokowski D. , Tchórzewski M. , Grankowski N.

Acta Biochimica Polonica

2002

tom 49

nr 1

11-18

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.

On the role of cyclic AMP-independent protein kinases in the modification of yeast ribosomal proteins in vivo

100%

Kudlicki W. , Szyszka R. , Grankowski N. , Gąsior E.

Acta Biochimica Polonica

1981

tom 28

nr 1

51-59

Extraribosomal function of the acidic ribosomal P1-protein YP1α from Saccharomyces cerevisiae

100%

Tchórzewski M. , Boldyreff B. , Grankowski N.

Acta Biochimica Polonica

1999

tom 46

nr 4

901-910

The yeast acidic ribosomal P-proteins YP1α, YP1β, YP2a and YP2b were studied for a possible transactivation potential beside their ribosomal function. The fusions of P-proteins with the GAL4 DNA-binding domain were assayed toward their transcriptional activity with the aid of reporter genes in yeast. Two of the P-proteins, YP1α and YP1β, exhibited transactivation potential, however, only YP1α can be regarded as a potent transactivator. This protein was able to transactivate a reporter gene associated with two distinct promoter systems, GAL1 or CYC1. Additionally, truncated proteins of YP1α and YP1β were analyzed. The N-terminal part of YP1α fused to GAL4-BD showed transactivation potential but the C-terminal part did not. Our results suggest a putative extraribosomal function for these ribosomal proteins which consequently may be classified as "moonlighting" proteins.

Differential phosphorylation of ribosomal acidic proteins from yeast cell by two endogenous protein kinases: casein kinase-2 and 60S kinase

100%

Szyszka R. , Boguszewska A. , Grankowski N. , Ballesta J. P. G.

Acta Biochimica Polonica

1995

tom 42

nr 3

357-362

Halogenated benzimidazole inhibitors of phosphorylation, in vitro and in vivo, of the surface acidic proteins of the yeast ribosomal 60S subunit by endogenous protein kinases CK-II and PK60S

100%

Szyszka R. , Boguszewska A. , Shugar D. , Grankowski N.

Acta Biochimica Polonica

1996

tom 43

nr 2

389-396

Further studies on the quaternary structure of yeast casein kinase II

88%

Szyszka R. , Łopaczyński W. , Gałasiński W. , Grankowski N. , Gąsior E.

Acta Biochimica Polonica

1986

tom 33

nr 1

39-46

Immunological properties and peptide mapping of two type casein kinases from yeast

88%

Grankowski N. , Szyszka R. , Pilecki M.

Acta Biochimica Polonica

1987

tom 34

nr 1

45-49

Endogenous inhibitor of a cyclic AMP-independent (A type) protein kinase

87%

Grankowski N.

Acta Biochimica Polonica

1982

tom 29

nr 3-4

235-243

Phosphoprotein phosphatase from yeast and its ribosomal substrate

75%

Paleń E. , Grankowski N. , Gąsior E.

Acta Biochimica Polonica

1983

tom 30

nr 2

165-173