Zobrazeno 21 - 29
of 29
pro vyhledávání: '"Anni Kauko"'
Autor:
Gunnar von Heijne, Arne Elofsson, Anni Kauko, Estelle Thebaud, Linnea E. Hedin, Susana Cristobal
Publikováno v:
Journal of Molecular Biology. 397:190-201
We have determined the optimal placement of individual transmembrane helices in the Pyrococcus horikoshii Glt(Ph) glutamate transporter homolog in the membrane. The results are in close agreement with theoretical predictions based on hydrophobicity,
Autor:
Anni Kauko, Heli Havukainen, Anastassios C. Papageorgiou, Sauli Haataja, Annika Salminen, Jukka Finne, Arto T. Pulliainen, Teemu Haikarainen
Publikováno v:
Protein Science. 17:1513-1521
Streptococcus suis Dpr is an iron-binding protein involved in oxidative stress resistance. It belongs to the bacterial Dps protein family whose members form dodecameric assemblies. Previous studies have shown that zinc and terbium inhibit iron incorp
Publikováno v:
Journal of Molecular Biology. 380:170-180
With the increasing number of available α-helical transmembrane (TM) protein structures, the traditional picture of membrane proteins has been challenged. For example, reentrant regions, which enter and exit the membrane at the same side, and interf
The folding of most integral membrane proteins follows a two-step process: Initially, individual transmembrane helices are inserted into the membrane by the Sec translocon. Thereafter, these helices fold to shape the final conformation of the protein
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2ee1cc422e30bc4177a4b5bbf96d1be9
Autor:
Anni Kauko, Anastassios C. Papageorgiou, Sauli Haataja, Arto T. Pulliainen, Jukka Finne, Wolfram Meyer-Klaucke
Publikováno v:
Journal of Molecular Biology. 364:97-109
The Dps-like peroxide resistance protein (Dpr) is a dodecameric protein that protects the human and swine pathogen Streptococcus suis from hydrogen peroxide by removing free Fe2+ from the cytosol. Subsequent oxidation of iron by Dpr results in the de
Publikováno v:
Molecular Microbiology. 57:1086-1100
The Dps family members constitute a distinct group of multimeric and ferritin-like iron binding proteins (up to 500 iron atoms/12-mer) that are widespread in eubacteria and archaea and implicated in oxidative stress resistance and virulence. Despite
Autor:
Aron Hennerdal, Anni Kauko, IngMarie Nilsson, Susana Cristobal, Karl Enquist, Mirjam Lerch-Bader, Gunnar von Heijne, Andreas Bernsel, Kristoffer Illergård, Karin Öjemalm, Linnea E. Hedin, Arne Elofsson
Publikováno v:
Journal of Molecular Biology; Vol 396
In mammalian cells, most integral membrane proteins are initially inserted into the endoplasmic reticulum membrane by the so-called Sec61 translocon. However, recent predictions suggest that many transmembrane helices (TMHs) in multispanning membrane
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::97ccd5ace88bb829a487f08e25540436
http://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-33926
http://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-33926
Publikováno v:
Molecular microbiology. 57(4)
The Dps family members constitute a distinct group of multimeric and ferritin-like iron binding proteins (up to 500 iron atoms/12-mer) that are widespread in eubacteria and archaea and implicated in oxidative stress resistance and virulence. Despite
Publikováno v:
Journal of molecular biology. 338(3)
The Dps-like peroxide resistance protein (Dpr) is an aerotolerance and hydrogen peroxide resistance agent found in the meningitis-associated pathogen Streptococcus suis. Dpr is believed to act by binding free intracellular iron to prevent Fenton chem
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