Wyniki wyszukiwania - Biblioteka Nauki

1

Plant peroxidases and nitrogen metabolism: interactions with nitrates and nitrites

100%

Minibayeva F. , Galeeva E. , Gurjanov O. , Viktorova L.

BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology

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2013

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tom 94

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nr 2

2

Plastoquinones incorporated in sodium cholate micelles are effectively reduced by ferredoxin: NADPplus oxidoreductase

100%

Bojko M. , Kruk J. , Wieckowski S.

Polish Journal of Natural Sciences. Supplement

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2003

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tom 01

3

Application of enzymes for bioremediation. Part 1. Oxidoreductases

100%

Piotrowska A.

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nr 6

4

Why chloroplastic ferredoxin: NADPplus oxidoreductase binds to lipids – model membranes study?

84%

Grzyb J.

BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology

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2013

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tom 94

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nr 3

5

AAN82231 protein from uropathogenic E. coli CFT073 is a close paralog of DsbB enzymes and does not belong to the DsbI family

84%

Pawlowski M. , Lasica A. M. , Jagusztyn-Krynicka E. K. , Bujnicki J. M.

Polish Journal of Microbiology

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2009

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tom 58

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nr 2

181-184

EN

Dsb proteins control the formation and rearrangement of disulfide bonds during the folding of membrane and exported proteins. DsbA is an oxidant that catalyzes formation of disulfide bonds in newly synthesized, and yet unfolded proteins. In order to act catalytically again, it has to be reoxidized by a transmembrane protein DsbB characterized by two pairs of disulfides. DsbB is related to another protein family Dsbl, characterized by the presence of only one disulfide, and an additional C-terminal beta-propeller domain. The protein AAN82231 from E. coli strain CFT073 has been recently described as a new member of the Dsbl family (Grimshaw et al., 2008). It was found that AAN82231 forms a functional redox pair with DsbL - a newly described DsbA-like protein. Here, we report that AAN82231 shares no characteristic features with the Dsbl proteins. Instead, according to phylogenetic analyses AAN82231 clearly belongs to another, previously described subfamily of DsbB paralogs. To facilitate classification of DsbB and Dsbl homologs, we propose a new nomenclature system and present an updated phylogenetic analysis of the DsbB superfamily, which comprises the following families: "orthodox" DsbB, its paralogs now named DsbB2 (including AAN82231), Dsbl and two groups of so far uncharacterized DsbB paralogs termed DsbB3 and DsbB4. We have also developed a web server dedicated to phylogenetic assignment of DsbB/Dsbl candidate proteins that will be identified in the future.

6

RNA-seq reveals differentially expressed genes in cucumber MSC lines possessing mitochondrial DNA rearrangements

84%

Mroz T. , Pryszcz L. , Skarzynska A. , Kielkowska A. , Havey M. , Bartoszewski G.

BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology

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2013

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tom 94

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nr 2

7

Localization of oxido-reductases and hydrolases during adventitious root primordium initiation and emergence in hypocotyl cuttings of Phaseolus vulgaris L.

84%

Kakkar R. K. , Rai V. K.

Acta Physiologiae Plantarum

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1994

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tom 16

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nr 4

8

Aeration properties and enzyme activity on the example of Arenic Chernozem [Tisice]

84%

Wlodarczyk T. , Glinski J. , Stepniewski W. , Stepniewska Z. , Brzezinska M. , Kuraz V.

International Agrophysics

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2001

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tom 15

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nr 2

9

Produkcja lakkazy i jej immobilizacja na wybranych nosnikach

67%

Rekuc A. , Kruczkiewicz P. , Kielczynski R. , Jastrzembska B. , Bryjak J.

Acta Scientiarum Polonorum. Biotechnologia

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2006

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tom 05

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nr 1-2

3-15

10

Novo wykorzystuje enzymy

67%

W K.

Biuletyn Informacyjny Ośrodka Badawczo-Rozwojowego Przemysłu Płyt Drewnopochodnych w Czarnej Wodzie

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1997

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tom 38

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nr 3

156-157

11

Campylobacter protein oxidation influences epithelial cell invasion or intracellular survival as well as intestinal tract colonization in chickens

67%

Lasica A. M. , Wyszynska A. , Szymanek K. , Majewski P. , Jagusztyn-Krynicka E. K.

Journal of Applied Genetics

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2010

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tom 51

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nr 3

EN

The Dsb family of redox proteins catalyzes disulfide bond formation and isomerization. Since mutations in dsb genes change the conformation and stability of many extracytoplasmic proteins, and since many virulence factors of pathogenic bacteria are extracytoplasmic, inactivation of dsb genes often results in pathogen attenuation. This study investigated the role of 2 membrane-bound oxidoreductases, DsbB and Dsbl, in the Campylobacter jejuni oxidative Dsb pathway. Campylobacter mutants, lacking DsbB or Dsbl or both, were constructed by allelic replacement and used in the human intestinal epithelial T84 cell line for the gentamicin protection assay (invasion assay) and chicken colonization experiments. In C. coli strain 23/1, the inactivation of the dsbB or dsbl gene separately did not significantly affect the colonization process. However, simultaneous disruption of both membrane-bound oxidoreductase genes significantly decreased the strain's ability to colonize chicken intestines. Moreover, C. jejuni strain 81-176 with mutated dsbB or dsbI genes showed reduced invasion/intracellular survival abilities. No cells of the double mutants (dsbB⁻ dsbI⁻) of C. jejuni 81-176 were recovered from human cells after 3 h of invasion.

12

Enzymy wewnątrzkomórkowych przemian redoks (oksydoreduktazy)

67%

Brzezinska M. , Wlodarczyk T.

Acta Agrophysica. Rozprawy i Monografie

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2005

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nr 3[120]

13

The influence of Cd, Pb, Cu and Ni on NO3 uptake by cucumber seedlings. II. In vitro and in vivo effects of Cd, Cu, Pb and Ni on the plasmalemma ATPase and oxidoreductase from cucumber seedlings roots

59%

Burzynski M. , Buczek J.

Acta Physiologiae Plantarum

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1994

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tom 16

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nr 4