Zobrazeno 1 - 10
of 93
pro vyhledávání: '"Stephan Wilkens"'
Publikováno v:
Frontiers in Molecular Biosciences, Vol 11 (2024)
Externí odkaz:
https://doaj.org/article/96a1080728764f57b9c815e9cc0a2277
Autor:
Lee S Parsons, Stephan Wilkens
Publikováno v:
PLoS ONE, Vol 7, Iss 10, p e46960 (2012)
BACKGROUND:Vacuolar (H(+))-ATPase (V-ATPase; V(1)V(o)-ATPase) is a large multisubunit enzyme complex found in the endomembrane system of all eukaryotic cells where its proton pumping action serves to acidify subcellular organelles. In the plasma memb
Externí odkaz:
https://doaj.org/article/ff9b2dedcf3347ada49649c744624853
Publikováno v:
BioEssays.
Autor:
Sijin Luozhong, Zhefan Yuan, Tara Sarmiento, Yu Chen, Wenchao Gu, Caleb McCurdy, Wenting Gao, Ruoxin Li, Stephan Wilkens, Shaoyi Jiang
Publikováno v:
Nano letters. 22(20)
Secondary lymphoid organs (SLOs) are an important target for mRNA delivery in various applications. While the current delivery method relies on the drainage of nanoparticles to lymph nodes by intramuscular (IM) or subcutaneous (SC) injections, an eff
Publikováno v:
Journal of Biological Chemistry. 294:6439-6449
The vacuolar H+-ATPase (V-ATPase; V1Vo-ATPase) is an ATP-dependent proton pump that acidifies subcellular compartments in all eukaryotic organisms. V-ATPase activity is regulated by reversible disassembly into autoinhibited V1-ATPase and Vo proton ch
Publikováno v:
The Journal of Biological Chemistry
Aggregation of the circulating protein leukocyte-cell-derived chemotaxin 2 (LECT2) causes amyloidosis of LECT2 (ALECT2), one of the most prevalent forms of systemic amyloidosis affecting the kidney and liver. The I40V mutation is thought to be necess
Publikováno v:
Encyclopedia of Biological Chemistry III ISBN: 9780128220405
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9c8bfa64c2c920d4b2b185c05edc5397
https://doi.org/10.1016/b978-0-12-819460-7.00307-8
https://doi.org/10.1016/b978-0-12-819460-7.00307-8
Autor:
Wah Chiu, Mrinal Shekhar, Abhishek Singharoy, Stephan Wilkens, Soung Hun Roh, Grigore D. Pintilie, Christophe Chipot
Publikováno v:
Science Advances. 6
Rotary vacuolar adenosine triphosphatases (V-ATPases) drive transmembrane proton transport through a Vo proton channel subcomplex. Despite recent high-resolution structures of several rotary ATPases, the dynamic mechanism of proton pumping remains el
Autor:
Soung-Hun, Roh, Mrinal, Shekhar, Grigore, Pintilie, Christophe, Chipot, Stephan, Wilkens, Abhishek, Singharoy, Wah, Chiu
Publikováno v:
Science Advances
A 2.7-Å cryo-EM structure and MD simulations explain water-mediated H+ transport and autoinhibition of yeast Vo proton channel.
Rotary vacuolar adenosine triphosphatases (V-ATPases) drive transmembrane proton transport through a Vo proton chann
Rotary vacuolar adenosine triphosphatases (V-ATPases) drive transmembrane proton transport through a Vo proton chann
Publikováno v:
Journal of Biological Chemistry. 293:10718-10730
Vacuolar H+-ATPases (V-ATPases; V1Vo-ATPases) are rotary-motor proton pumps that acidify intracellular compartments and, in some tissues, the extracellular space. V-ATPase is regulated by reversible disassembly into autoinhibited V1-ATPase and Vo pro