Zobrazeno 1 - 10
of 395
pro vyhledávání: '"Gunnar von Heijne"'
Autor:
Florian Wruck, Pengfei Tian, Renuka Kudva, Robert B. Best, Gunnar von Heijne, Sander J. Tans, Alexandros Katranidis
Publikováno v:
Communications Biology, Vol 4, Iss 1, Pp 1-8 (2021)
Wruck et al. investigate the folding of the small zinc-finger domain ADR1a inside and at the vestibule of the ribosomal tunnel, using optical tweezers, single-molecule FRET, and molecular dynamics simulations. They find that the ribosomal tunnel acce
Externí odkaz:
https://doaj.org/article/cbe82a426918461f8b87118d1e3aba21
Autor:
Manuel Bañó-Polo, Carlos Baeza-Delgado, Silvia Tamborero, Anthony Hazel, Brayan Grau, IngMarie Nilsson, Paul Whitley, James C. Gumbart, Gunnar von Heijne, Ismael Mingarro
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-9 (2018)
Integral membrane proteins are assembled into the ER membrane via the ribosome-translocon channel. Here authors use in vitro translation assays and MD simulations to show that folding in the ribosome is favorable for TM helices, but unfavorable for s
Externí odkaz:
https://doaj.org/article/3c5b89887b174ab79e5d3eb70d8006cc
Autor:
Felix Nicolaus, Ane Metola, Daphne Mermans, Amanda Liljenström, Ajda Krč, Salmo Mohammed Abdullahi, Matthew Zimmer, Thomas F Miller III, Gunnar von Heijne
Publikováno v:
eLife, Vol 10 (2021)
We follow the cotranslational biosynthesis of three multispanning Escherichia coli inner membrane proteins in vivo using high-resolution force profile analysis. The force profiles show that the nascent chain is subjected to rapidly varying pulling fo
Externí odkaz:
https://doaj.org/article/ca34b5603bb94c49a82623fce7c85c1b
Autor:
Vivekanandan Shanmuganathan, Nina Schiller, Anastasia Magoulopoulou, Jingdong Cheng, Katharina Braunger, Florian Cymer, Otto Berninghausen, Birgitta Beatrix, Kenji Kohno, Gunnar von Heijne, Roland Beckmann
Publikováno v:
eLife, Vol 8 (2019)
XBP1u, a central component of the unfolded protein response (UPR), is a mammalian protein containing a functionally critical translational arrest peptide (AP). Here, we present a 3 Å cryo-EM structure of the stalled human XBP1u AP. It forms a unique
Externí odkaz:
https://doaj.org/article/f441759e29854117a41889883f5b50a1
Autor:
Renuka Kudva, Pengfei Tian, Fátima Pardo-Avila, Marta Carroni, Robert B Best, Harris D Bernstein, Gunnar von Heijne
Publikováno v:
eLife, Vol 7 (2018)
The E. coli ribosome exit tunnel can accommodate small folded proteins, while larger ones fold outside. It remains unclear, however, to what extent the geometry of the tunnel influences protein folding. Here, using E. coli ribosomes with deletions in
Externí odkaz:
https://doaj.org/article/b8a00e7659374bc399c67af75ad5de29
Autor:
Ola B. Nilsson, Rickard Hedman, Jacopo Marino, Stephan Wickles, Lukas Bischoff, Magnus Johansson, Annika Müller-Lucks, Fabio Trovato, Joseph D. Puglisi, Edward P. O’Brien, Roland Beckmann, Gunnar von Heijne
Publikováno v:
Cell Reports, Vol 12, Iss 10, Pp 1533-1540 (2015)
At what point during translation do proteins fold? It is well established that proteins can fold cotranslationally outside the ribosome exit tunnel, whereas studies of folding inside the exit tunnel have so far detected only the formation of helical
Externí odkaz:
https://doaj.org/article/be6170e22afe4e52a52d732392b7ce19
Autor:
Erik Lee Snapp, Nicholas McCaul, Matthias Quandte, Zuzana Cabartova, Ilja Bontjer, Carolina Källgren, IngMarie Nilsson, Aafke Land, Gunnar von Heijne, Rogier W Sanders, Ineke Braakman
Publikováno v:
eLife, Vol 6 (2017)
Like all other secretory proteins, the HIV-1 envelope glycoprotein gp160 is targeted to the endoplasmic reticulum (ER) by its signal peptide during synthesis. Proper gp160 folding in the ER requires core glycosylation, disulfide-bond formation and pr
Externí odkaz:
https://doaj.org/article/25dc67d0945545898d855addc531adec
Autor:
Ting Su, Jingdong Cheng, Daniel Sohmen, Rickard Hedman, Otto Berninghausen, Gunnar von Heijne, Daniel N Wilson, Roland Beckmann
Publikováno v:
eLife, Vol 6 (2017)
Interaction between the nascent polypeptide chain and the ribosomal exit tunnel can modulate the rate of translation and induce translational arrest to regulate expression of downstream genes. The ribosomal tunnel also provides a protected environmen
Externí odkaz:
https://doaj.org/article/8de9745782124b58bc687fcbc7c2f96e
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 119(35)
In recent years, it has become clear that many homo- and heterodimeric cytoplasmic proteins in both prokaryotic and eukaryotic cells start to dimerize cotranslationally (i.e., while at least one of the two chains is still attached to the ribosome). W
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::e90f19d9dfb7652a3efbf7ccc500b501
https://pubmed.ncbi.nlm.nih.gov/35994672
https://pubmed.ncbi.nlm.nih.gov/35994672
Publikováno v:
FEBS lettersReferences.
Human growth hormone (hGH) is a four-helix bundle protein of considerable pharmacological interest. Recombinant hGH is produced in bacteria, yet little is known about its folding during expression in Escherichia coli. We have studied the cotranslatio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f9c87c5082babcd6241a1538fd744953
https://pubmed.ncbi.nlm.nih.gov/36520514
https://pubmed.ncbi.nlm.nih.gov/36520514