Zobrazeno 1 - 10
of 24
pro vyhledávání: '"Sarah M. Auclair"'
Publikováno v:
Langmuir. 32:3015-3023
Here we introduce ApoE-based Nanolipoprotein particles (NLP) – soluble, discoidal bilayer mimetic of ~23 nm in diameter, as fusion partners to study the dynamics of fusion pores induced by SNARE proteins. Using in vitro lipid mixing and content rel
Autor:
Alexandre Parrin, Amel Bahloul, Sylvie Nouaille, Christine Petit, Sarah M. Auclair, Martin Sachse, Nicolas Michalski, Juan D Goutman, Marc Guillon, Didier Dulon, Margot Tertrais, Saaid Safieddine, Danica Ciric, Paul Avan, Roger Bryan Sutton, Jacques Boutet de Monvel, Jean-Pierre Hardelin, Shyam S. Krishnakumar, James E. Rothman, Alice Emptoz
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::25fd65427218bb68931c2a144190050f
https://doi.org/10.7554/elife.31013.024
https://doi.org/10.7554/elife.31013.024
Autor:
Sarah M. Auclair, Ben O'Shaughnessy, Wensi Vennekate, Oscar D. Bello, Zhenyong Wu, Erdem Karatekin, Shyam S. Krishnakumar, Sathish Thiyagarajan
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5d59ef9b84d4d8c2ce77fb61283e68e7
https://doi.org/10.7554/elife.22964.025
https://doi.org/10.7554/elife.22964.025
Autor:
Shyam S. Krishnakumar, Ben O'Shaughnessy, Sarah M. Auclair, Sathish Thiyagarajan, Wensi Vennekate, Oscar D. Bello, Zhenyong Wu, Erdem Karatekin
Publikováno v:
eLife, Vol 6 (2017)
eLife
eLife
Hormones and neurotransmitters are released through fluctuating exocytotic fusion pores that can flicker open and shut multiple times. Cargo release and vesicle recycling depend on the fate of the pore, which may reseal or dilate irreversibly. Pore n
Autor:
Jing Wang, Oscar Bello, Sarah M. Auclair, Jeff Coleman, Frederic Pincet, Shyam S. Krishnakumar, Charles V. Sindelar, James E. Rothman
Publikováno v:
Proceedings of the National Academy of Sciences. 111:13966-13971
The synaptic vesicle protein synaptotagmin-1 (SYT) is required to couple calcium influx to the membrane fusion machinery. However, the structural mechanism underlying this process is unclear. Here we report an unexpected circular arrangement (ring) o
Autor:
Jun Zhang, Michael L. Gross, Andy J. Wowor, Eric R. May, Dongmei Yu, Debra A. Kendall, Yuetian Yan, James L. Cole, Sarah M. Auclair
Publikováno v:
Biochemistry
The Sec pathway mediates translocation of protein across the inner membrane of bacteria. SecA is a motor protein that drives translocation of preprotein through the SecYEG channel. SecA reversibly dimerizes under physiological conditions, but differe
Autor:
Oscar D. Bello, Zhenyong Wu, Wensi Vennekate, Shyam S. Krishnakumar, Erdem Karatekin, Sarah M. Auclair, Natasha Dudzinski
Publikováno v:
Scientific Reports
The initial, nanometer-sized connection between the plasma membrane and a hormone- or neurotransmitter-filled vesicle –the fusion pore– can flicker open and closed repeatedly before dilating or resealing irreversibly. Pore dynamics determine rele
Autor:
Erdem Karatekin, Natasha Dudzinski, Shyam S. Krishnakumar, Wensi Vennekate, Oscar D. Bello, Zhenyong Wu, Sarah M. Auclair
Publikováno v:
Biophysical Journal. 110(3)
A key step during neurotransmitter or hormone release (exocytosis) is the formation of a nanometer-sized fusion pore that connects the plasma membrane to the synaptic or secretory vesicle. The pore can flicker open and closed repeatedly before dilati
Publikováno v:
Protein Science. 21:13-25
Signal peptidase I (SPase I) is critical for the release of translocated preproteins from the membrane as they are transported from a cytoplasmic site of synthesis to extracytoplasmic locations. These proteins are synthesized with an amino-terminal e
Autor:
Ishita Mukerji, Sarah M. Auclair, Debra A. Kendall, Donald Oliver, Monika Musial-Siwek, Julia P. Moses
Publikováno v:
Biochemistry. 49:782-792
Identification of the signal peptide-binding domain within SecA ATPase is an important goal for understanding the molecular basis of SecA preprotein recognition as well as elucidating the chemo-mechanical cycle of this nanomotor during protein transl