Zobrazeno 1 - 10
of 16
pro vyhledávání: '"Torsten H, Walther"'
Autor:
Eva R. Stockwald, Lena M.E. Steger, Stefanie Vollmer, Christina Gottselig, Stephan L. Grage, Jochen Bürck, Sergii Afonin, Julia Fröbel, Anne-Sophie Blümmel, Julia Setzler, Wolfgang Wenzel, Torsten H. Walther, Anne S. Ulrich
Publikováno v:
Biophysical journal.
The twin arginine translocase (Tat) exports folded proteins across bacterial membranes. The putative pore-forming or membrane-weakening component (TatA
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8370f3f0231c75c4afc0e8b493e8a0af
https://pubmed.ncbi.nlm.nih.gov/36523158
https://pubmed.ncbi.nlm.nih.gov/36523158
Autor:
Stephan L. Grage, Lena M. E. Steger, Johannes Reichert, Anne Görner, Marin Kempfer, Sergii Afonin, Torsten H. Walther, Julia Koch, Erik Strandberg, Anne S. Ulrich, Jochen Bürck, Parvesh Wadhwani, Annika Kohlmeyer
Publikováno v:
Proceedings of the National Academy of Sciences. 117:29637-29646
Pinholin S2168 triggers the lytic cycle of bacteriophage φ21 in infected Escherichia coli. Activated transmembrane dimers oligomerize into small holes and uncouple the proton gradient. Transmembrane domain 1 (TMD1) regulates this activity, while TMD
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1e9f9b7fe222936d77883425cbd97a7d
https://doi.org/10.1073/pnas.2007979117
https://doi.org/10.1073/pnas.2007979117
Autor:
Lena M E, Steger, Annika, Kohlmeyer, Parvesh, Wadhwani, Jochen, Bürck, Erik, Strandberg, Johannes, Reichert, Stephan L, Grage, Sergii, Afonin, Marin, Kempfer, Anne C, Görner, Julia, Koch, Torsten H, Walther, Anne S, Ulrich
Publikováno v:
Proc Natl Acad Sci U S A
Pinholin S(21)68 triggers the lytic cycle of bacteriophage φ21 in infected Escherichia coli. Activated transmembrane dimers oligomerize into small holes and uncouple the proton gradient. Transmembrane domain 1 (TMD1) regulates this activity, while T
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::954af8121805df9af0c3e938e4517d94
https://pubmed.ncbi.nlm.nih.gov/33154156
https://pubmed.ncbi.nlm.nih.gov/33154156
Autor:
Fereidoun Mahboudi, Torsten H. Walther, Christine Blattner, Maryam Tabasinezhad, Eskandar Omidinia, Wolfgang Wenzel, Hamzeh Rahimi
Publikováno v:
International Journal of Drug Development and Research, 11 (2), 38-44
Rapid growth in the therapeutic antibody market leads to a drastic development of antibody engineering to optimize biophysical properties. One of the main focuses of biopharmaceutical researches was the expansion of different approaches for affinity
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8c4b2624dd9cc923bc017114f6498849
https://doi.org/10.36648/0975-9344.11.2.135
https://doi.org/10.36648/0975-9344.11.2.135
Autor:
Wolfgang Wenzel, Maryam Tabasinezhad, Eskandar Omidinia, Hamzeh Rahimi, Christine Blattner, Torsten H. Walther, Fereidoun Mahboudi
Publikováno v:
Protein expression and purification. 155
Recombinant antibodies have emerged over the last few decades as the fastest growing class of therapeutic proteins for autoimmune diseases. Post-translation modifications of antibodies produced by human cell lines are highly consistent with those exi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::da0fecdcf03f369f32a7629f13a18e9a
https://pubmed.ncbi.nlm.nih.gov/30468855
https://pubmed.ncbi.nlm.nih.gov/30468855
Autor:
Moritz Wolf, Marco J. Klein, Wolfgang Wenzel, Stefanie Vollmer, Mareike Hartmann, Attilio Vittorio Vargiu, Anne S. Ulrich, Christina Gottselig, Olga V. Nolandt, Stephan L. Grage, Sebastian Prock, Sergiy Afonin, Eva Stockwald, Paolo Ruggerone, Hartmut Heinzmann, Torsten H. Walther
Publikováno v:
Cell (Online) 152 (2013): 316–326. doi:10.1016/j.cell.2012.12.017
info:cnr-pdr/source/autori:Torsten H Walther, Christina Gottselig, Stephan L Grage, Moritz Wolf, Attilio V Vargiu, Marco J Klein, Stefanie Vollmer, Sebastian Prock, Mareike Hartmann, Sergiy Afonin, Eva Stockwald, Hartmut Heinzmann, Olga V Nolandt, Wolfgang Wenzel, Paolo Ruggerone, and Anne S Ulrich/titolo:Folding and Self-Assembly of the TatA Translocation Pore Based on a Charge Zipper Mechanism./doi:10.1016%2Fj.cell.2012.12.017/rivista:Cell (Online)/anno:2013/pagina_da:316/pagina_a:326/intervallo_pagine:316–326/volume:152
info:cnr-pdr/source/autori:Torsten H Walther, Christina Gottselig, Stephan L Grage, Moritz Wolf, Attilio V Vargiu, Marco J Klein, Stefanie Vollmer, Sebastian Prock, Mareike Hartmann, Sergiy Afonin, Eva Stockwald, Hartmut Heinzmann, Olga V Nolandt, Wolfgang Wenzel, Paolo Ruggerone, and Anne S Ulrich/titolo:Folding and Self-Assembly of the TatA Translocation Pore Based on a Charge Zipper Mechanism./doi:10.1016%2Fj.cell.2012.12.017/rivista:Cell (Online)/anno:2013/pagina_da:316/pagina_a:326/intervallo_pagine:316–326/volume:152
We propose a concept for the folding and self- assembly of the pore-forming TatA complex from the Twin-arginine translocase and of other mem- brane proteins based on electrostatic ''charge zippers.'' Each subunit of TatA consists of a trans- membrane
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d1a185798f3ce5208495df4035264c1a
https://doi.org/10.1016/j.cell.2012.12.017
https://doi.org/10.1016/j.cell.2012.12.017
Autor:
Katharina Becker, Anne S. Ulrich, Torsten H. Walther, Ariadna Grau Campistany, Stephan L. Grage, Sergiy Afonin, Jochen Bürck, Erik Strandberg, Benjamin Zimpfer, Lena M. E. Steger, Dirk Windisch, Parvesh Wadhwani, Johannes Reichert
Publikováno v:
Biophysical Journal. 114:34a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::18fb10d4effac08142bbe9b17e79ead6
https://doi.org/10.1016/j.bpj.2017.11.233
https://doi.org/10.1016/j.bpj.2017.11.233
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. 1788(10):2238-2244
The twin arginine translocation (Tat) system can transport fully folded proteins, including their cofactors, across bacterial and thylakoid membranes. The Tat system of Bacillus subtilis that serves to export the phosphodiesterase (PhoD) consists of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2fecd2f787b13c9e4d542dd302dbf1df
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. 1768(10):2627-2634
The twin-arginine-translocase (Tat) can transport proteins in their folded state across bacterial or thylakoid membranes. In Bacillus subtilis the Tat-machinery consists of only two integral (inner) membrane proteins, TatA and TatC. Multiple copies o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5191f01fa36650680e41dc7b0281f25d
Autor:
Anne S. Ulrich, Torsten H. Walther
Publikováno v:
Current opinion in structural biology. 27
Transmembrane helix–helix interactions mediate the folding and assembly of membrane proteins. Recognition motifs range from GxxxG and leucine zippers to polar side chains and salt bridges. Some canonical membrane proteins contain local charge clust
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::df77ef1229927febbe12f11911fdc414
https://pubmed.ncbi.nlm.nih.gov/24907460
https://pubmed.ncbi.nlm.nih.gov/24907460