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pro vyhledávání: '"Mats-Jerry Eriksson"'
Autor:
Adrian K. Clarke, Mats-Jerry Eriksson
Publikováno v:
Journal of Bacteriology. 182:7092-7096
ClpB is a highly conserved heat shock protein that is essential for thermotolerance in bacteria and eukaryotes. One distinctive feature of all bacterial clpB genes is the dual translation of a truncated 79-kDa form (ClpB-79) in addition to the full-l
Autor:
Mats-Jerry Eriksson, Adrian K. Clarke
Publikováno v:
Journal of Bacteriology. 178:4839-4846
The heat shock protein CIpB (HSP100) is a member of the diverse group of Clp polypeptides that function as molecular chaperones and/or regulators of energy-dependent proteolysis. A single-copy gene coding for a ClpB homolog was cloned and sequenced f
Autor:
Åsa Strand, Anasuya Mohapatra, Peter Kindgren, Thomas Kieselbach, Simon P. Gough, Catherine Benedict, Mats Hansson, Mats-Jerry Eriksson
Publikováno v:
Physiologia plantarum. 141(4)
The presence of genes encoding organellar proteins in different cellular compartments necessitates a tight coordination of expression by the different genomes of the eukaryotic cell. This coordination of gene expression is achieved by organelle-to-nu
Current ambient UV-B levels can significantly depress productivity in aquatic habitats, largely because UV-B inhibits several steps of photosynthesis, including the photooxidation of water catalyzed by photosystem II. We show that upon UV-B exposure
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c3d2e793d2bc426b96b528e7e244bacb
https://europepmc.org/articles/PMC18225/
https://europepmc.org/articles/PMC18225/
Autor:
Adrian K. Clarke, Mats-Jerry Eriksson
Publikováno v:
Plant molecular biology. 31(4)
The Clp family consists of large, ubiquitous proteins that function as molecular chaperones and/or regulators of ATP-dependent proteolysis. A single copy gene coding for one of these proteins, ClpC, was cloned from the unicellular cyanobacterium Syne
Autor:
Adrian K. Clarke, Mats-Jerry Eriksson
Publikováno v:
Cell Stress & Chaperones. 5:255
In both prokaryotes and eukaryotes, the heat shock protein ClpB functions as a molecular chaperone and plays a key role in resisting high temperature stress. ClpB is important for the development of thermotolerance in yeast and cyanobacteria but appa
Publikováno v:
Plant Molecular Biology; Jul1998, Vol. 37 Issue 5, p791-801, 11p
Autor:
Clarke, Adrian, Eriksson, Mats-Jerry
Publikováno v:
Plant Molecular Biology; Jul1996, Vol. 31 Issue 4, p721-730, 10p
Autor:
Mary-Jane Gething
The precise shape of a protein is a crucial factor in its function. How do proteins become folded into the right conformation? Molecular chaperones and protein folding catalysts bind to developing polypeptides in the cytoplasm and ensure correct fold