Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Jeanine de Keyzer"'
Publikováno v:
Journal of Bacteriology, 197, 1444-1450. AMER SOC MICROBIOLOGY
Membrane proteins need to be properly inserted and folded in the membrane in order to perform a range of activities that are essential for the survival of bacteria. The Sec translocon and the YidC insertase are responsible for the insertion of the ma
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ad442c3ee8b736d42d33e897449a1b66
https://doi.org/10.1128/jb.02556-14
https://doi.org/10.1128/jb.02556-14
Publikováno v:
The Journal of Biological Chemistry
The Journal of Biological Chemistry, 285(28), 21600-21606. AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
The Journal of Biological Chemistry, 285(28), 21600-21606. AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Kar2p, an essential Hsp70 chaperone in the endoplasmic reticulum of Saccharomyces cerevisiae, facilitates the transport and folding of nascent polypeptides within the endoplasmic reticulum lumen. The chaperone activity of Kar2p is regulated by its in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f9b0f0b36d2bdf2a1f6376575a0290c9
http://europepmc.org/articles/PMC2898433
http://europepmc.org/articles/PMC2898433
Publikováno v:
FEBS Letters, 581(9), 1859-1864. Wiley
The Escherichia coli SecYEG complex forms a transmembrane channel for both protein export and membrane protein insertion. Secretory proteins and large periplasmic domains of membrane proteins require for translocation in addition the SecA ATPase. The
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::86ed38c4efbd0d3a8c1256b8cfaf9188
https://doi.org/10.1016/j.febslet.2007.03.081
https://doi.org/10.1016/j.febslet.2007.03.081
Autor:
Chris van der Does, Eli O. van der Sluis, Robert Tampé, Jeanine de Keyzer, Joachim Koch, Nico Nouwen, Arnold J. M. Driessen
Publikováno v:
Journal of Molecular Biology, 361(5), 839-849. Academic Press
The motor protein SecA drives the translocation of (pre-)proteins across the SecYEG channel in the bacterial cytoplasmic membrane by nucleotide-dependent cycles of conformational changes often referred to as membrane insertion/de-insertion. Despite s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::91dfe9d975462ad17a89a2dc01284374
https://research.rug.nl/en/publications/b88ba089-6fdc-468c-9824-86d74ef085ba
https://research.rug.nl/en/publications/b88ba089-6fdc-468c-9824-86d74ef085ba
Publikováno v:
The Journal of Biological Chemistry, 277(48), 46059-46065. AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Protein secretion in Escherichia coliis mediated by translocase, a multi-subunit membrane protein complex with SecA as ATP-driven motor protein and the SecYEG complex as translocation pore. A fluorescent assay was developed to facilitate kinetic stud
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::50492f9de989b329faa1523108189621
https://doi.org/10.1074/jbc.m208449200
https://doi.org/10.1074/jbc.m208449200
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 1033
The interaction between membrane proteins and their (protein) ligands is conventionally investigated by nonequilibrium methods such as co-sedimentation or pull-down assays. Surface Plasmon Resonance can be used to monitor such binding events in real-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::f076063a091e09ca6702f89d69a10325
https://pubmed.ncbi.nlm.nih.gov/23996177
https://pubmed.ncbi.nlm.nih.gov/23996177
Publikováno v:
Journal of Cell Biology, 199(2), 303-315. ROCKEFELLER UNIV PRESS
The Journal of Cell Biology
The Journal of Cell Biology
The Sec and Tat pathways are both required to insert the three hydrophobic domains of the Rieske protein into the membrane.
Membrane protein assembly is a fundamental process in all cells. The membrane-bound Rieske iron-sulfur protein is an esse
Membrane protein assembly is a fundamental process in all cells. The membrane-bound Rieske iron-sulfur protein is an esse
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3620f3fe47bbef7057b786ef4d177835
https://research.rug.nl/en/publications/5d3a6d7a-1bea-44ab-807c-d3bda4af2740
https://research.rug.nl/en/publications/5d3a6d7a-1bea-44ab-807c-d3bda4af2740
Publikováno v:
The Journal of Biological Chemistry, 287(11), 7885-7895. AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
During co-translational membrane insertion of membrane proteins with large periplasmic domains, the bacterial SecYEG complex needs to interact both with the ribosome and the SecA ATPase. Although the binding sites for SecA and the ribosome overlap, i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::89e8455b9bf564ce25790349a0ae6c69
https://research.rug.nl/en/publications/e1d46aa5-ed07-4b30-a8d6-0e017221aaaf
https://research.rug.nl/en/publications/e1d46aa5-ed07-4b30-a8d6-0e017221aaaf
Publikováno v:
The Journal of Biological Chemistry
Protein translocation and folding in the endoplasmic reticulum of Saccharomyces cerevisiae involves two distinct Hsp70 chaperones, Lhs1p and Kar2p. Both proteins have the characteristic domain structure of the Hsp70 family consisting of a conserved N
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::456715e8fb6d67303aeb8704701cfec5
https://pubmed.ncbi.nlm.nih.gov/19759005
https://pubmed.ncbi.nlm.nih.gov/19759005