نتایج جستجو برای: triple loops snare

تعداد نتایج: 85633  

Journal: :Physiological reviews 2012
Haruo Kasai Noriko Takahashi Hiroshi Tokumaru

The dynamics of exocytosis are diverse and have been optimized for the functions of synapses and a wide variety of cell types. For example, the kinetics of exocytosis varies by more than five orders of magnitude between ultrafast exocytosis in synaptic vesicles and slow exocytosis in large dense-core vesicles. However, in all cases, exocytosis is mediated by the same fundamental mechanism, i.e....

Journal: :Journal of cell science 2000
M M Tsui D K Banfield

The transport of proteins between various compartments of the secretory pathway occurs by the budding of vesicles from one membrane and their fusion with another. A key event in this process is the selective recognition of the target membrane by the vesicle and the current view is that SNARE protein interactions likely play a central role in vesicle-target recognition and or membrane fusion. In...

Journal: :Molecular biology of the cell 2008
Elena Fdez Thomas A Jowitt Ming-Chuan Wang Manisha Rajebhosale Keith Foster Jordi Bella Clair Baldock Philip G Woodman Sabine Hilfiker

The interactions underlying the cooperativity of soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complexes during neurotransmission are not known. Here, we provide a molecular characterization of a dimer formed between the cytoplasmic portions of neuronal SNARE complexes. Dimerization generates a two-winged structure in which the C termini of cytosolic SNARE comple...

Journal: :Developmental cell 2018
Misoon Park Cornelia Krause Matthias Karnahl Ilka Reichardt Farid El Kasmi Ulrike Mayer York-Dieter Stierhof Ulrike Hiller Georg Strompen Martin Bayer Marika Kientz Masa H Sato Marc T Nishimura Jeffery L Dangl Anton A Sanderfoot Gerd Jürgens

Membrane vesicles delivered to the cell-division plane fuse with one another to form the partitioning membrane during plant cytokinesis, starting in the cell center. In Arabidopsis, this requires SNARE complexes involving the cytokinesis-specific Qa-SNARE KNOLLE. However, cytokinesis still occurs in knolle mutant embryos, suggesting contributions from KNOLLE-independent SNARE complexes. Here we...

2008
Elena Fdez Thomas A. Jowitt Ming-Chuan Wang Manisha Rajebhosale Keith Foster Jordi Bella Clair Baldock Philip G. Woodman Sabine Hilfiker

The interactions underlying the cooperativity of soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complexes during neurotransmission are not known. Here, we provide a molecular characterization of a dimer formed between the cytoplasmic portions of neuronal SNARE complexes. Dimerization generates a two-winged structure in which the C-termini of cytosolic SNARE comple...

Journal: :IACR Cryptology ePrint Archive 2008
Temitope Gbolahan Jaiyeola John Olushola Adeniran

This study digs out some new algebraic properties of an Osborn loop that will help in the future to unveil the mystery behind the middle inner mappings T(x) of an Osborn loop. These new algebraic properties, will open our eyes more to the study of Osborn loops like CC-loops which has received a tremendious attention in this 21st and VD-loops whose study is yet to be explored. In this study, som...

2009
B. Baumeister G. Stroth

We classify " nice " loop envelopes to Bruck loops of 2-power exponent under the assumption that every nonabelian simple section of G is either passive or isomorphic to PSL2(q), q − 1 ≥ 4 a 2-power. The hypothesis is verified in a separate paper. This paper is a continuation of the work by Aschbacher, Kinyon and Phillips on finite Bruck loops [AKP]. In [BS3] we will apply these results and get ...

Journal: :The Journal of biological chemistry 2015
Niket Shah Karen N Colbert Michael D Enos Daniel Herschlag William I Weis

The fusion of intracellular membranes is driven by the formation of a highly stable four-helix bundle of SNARE proteins embedded in the vesicle and target membranes. N-Ethylmaleimide sensitive factor recycles SNAREs after fusion by binding to the SNARE complex through an adaptor protein, αSNAP, and using the energy of ATP hydrolysis to disassemble the complex. Although only a single molecule of...

Journal: :The Journal of biological chemistry 2003
Jan Rohde Lars Dietrich Dieter Langosch Christian Ungermann

It is presently not clear how the function of SNARE proteins is affected by their transmembrane domains. Here, we analyzed the role of the transmembrane domain of the vacuolar SNARE Vam3 by replacing it by a lipid anchor. Vacuoles with mutant Vam3 fuse poorly and have increased amounts of cis-SNARE complexes, indicating that they are more stable. As a consequence efficient cis-SNARE complex dis...

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