Results 101 to 110 of about 3,191 (253)

Single‐molecule DNA flow‐stretch assays for high‐throughput DNA–protein interaction studies

open access: yesFEBS Open Bio, EarlyView.
We describe an optimised single‐molecule DNA flow‐stretch assay that visualises DNA–protein interactions in real time. Linear DNA fragments are tethered to a surface and stretched by buffer flow for fluorescence imaging. Using λ and φX174 DNA, this protocol enhances reproducibility and accessibility, providing a versatile approach for studying diverse ...
Ayush Kumar Ganguli   +8 more
wiley   +1 more source

Reluctance to membrane binding enables accessibility of the synaptobrevin SNARE motif for SNARE complex formation

open access: yes, 2011
SNARE proteins play a critical role in intracellular membrane fusion by forming tight complexes that bring two membranes together and involve sequences called SNARE motifs.
Wei Li   +3 more
core   +1 more source

Molecular Dynamics Simulations of SNARE Complex Unzipping [PDF]

open access: yesBiophysical Journal, 2014
The SNARE proteins facilitate biological membrane fusion. The neuronal SNARE proteins, namely VAMP-2, also called synaptobrevin 2, SNAP-25, and syntaxin-1A together form a coiled-coil complex. The formation of this SNARE complex is vital for vesicle-plasma membrane fusion resulting in neurotransmitter exocytosis.
Satyan Sharma, Manfred Lindau
openaire   +2 more sources

Matrix metalloproteinase‐9 regulates cell adhesion and membrane protrusive activity of ovarian cancer cells

open access: yesFEBS Open Bio, EarlyView.
Matrix metalloproteinase‐9 (MMP9) drives ovarian cancer progression. Using MMP9‐null cells (M9‐KO) created from ovarian cancer cells, we found MMP9 loss did not block Epidermal Growth Factor (EGF)‐driven E‐cadherin dissolution or EMT but delayed and reduced EGF‐driven membrane protrusions. Transient MMP9 re‐expression drove membrane protrusion.
Claire Strauel   +8 more
wiley   +1 more source

An activated Q-SNARE/SM protein complex as a possible intermediate in SNARE assembly.

open access: yes, 2017
Assembly of the SNARE proteins syntaxin1, SNAP25, and synaptobrevin into a SNARE complex is essential for exocytosis in neurons. For efficient assembly, SNAREs interact with additional proteins but neither the nature of the intermediates nor the sequence
Reinhard Jahn   +11 more
core   +1 more source

Mass spectrometry based identification of AMP‐O‐Tris generated by Thermococcus onnurineus Cas10

open access: yesFEBS Open Bio, EarlyView.
Isolated Thermococcus onnurineus Cas10 generates the noncanonical ATP‐derived product AMP‐O‐Tris while in Tris‐containing buffer as identified via mass spectrometry, revealing relaxed nucleophile selectivity under isolated conditions. These findings suggest that multiprotein Csm complex assembly restricts Cas10 reactivity toward canonical cyclic ...
Su‐Jin Lee   +6 more
wiley   +1 more source

Biophysical and Thermodynamical Characterization of the Neuronal SNARE Complex Formation

open access: yes, 2008
Membranfusionsereignisse werden durch eine konservierte Proteinfamilie, die so genannten SNARE-Proteine, vermittelt. SNARE-Proteine bilden einen stabilen α-helikalen Komplex zwischen zwei Membranen aus.
Wiederhold, Katrin
core   +1 more source

Time‐restricted feeding prior to Mycobacterium tuberculosis infection reduces tissue CD4+ T cells with limited impact on bacterial clearance

open access: yesFEBS Open Bio, EarlyView.
Time‐restricted feeding (TRF) in mice increased liver fatty acid oxidation and decreased fatty acid biosynthesis. These alterations persisted when TRF was discontinued and the host was infected with Mycobacterium tuberculosis. Pre‐exposure to TRF did not alter tissue (lung and spleen) mycobacterial burden but significantly reduced CD3+ T cells in lungs
Ashish Gupta   +7 more
wiley   +1 more source

N-Terminal Domain of Vacuolar SNARE Vam7p Promotes Trans-SNARE Complex Assembly

open access: yes, 2012
SNARE-dependent membrane fusion in eukaryotic cells requires that the heptad-repeat SNARE domains from R- and Q-SNAREs, anchored to apposed membranes, assemble into four-helix coiled-coil bundles.
Wickner, William T, Xu, Hao
core   +1 more source

Sec1/Munc18 protein Vps33 binds to SNARE domains and the quaternary SNARE complex

open access: yesMolecular Biology of the Cell, 2012
Soluble N-ethylmaleimide–sensitive factor attachment protein receptor (SNARE) proteins catalyze membrane fusion events in the secretory and endolysosomal systems, and all SNARE-mediated fusion processes require cofactors of the Sec1/Munc18 (SM) family. Vps33 is an SM protein and subunit of the Vps-C complexes HOPS (homotypic fusion and protein sorting)
Lobingier, Braden T., Merz, Alexey J.
openaire   +2 more sources

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