Results 61 to 70 of about 150,506 (397)

An expanded role of the SNARE-containing regulon as it relates to the defense process that Glycine max has to Heterodera glycines

open access: yesJournal of Plant Interactions, 2019
The defense regulon has been defined genetically in Arabidopsis thaliana to involve the syntaxin PENETRATION1 (PEN1), the secreted glucosidase (PEN2) and an ATP-binding cassette (ABC) transporter (PEN3).
Hannah W. Austin   +5 more
doaj   +1 more source

Munc18-1-regulated stage-wise SNARE assembly underlying synaptic exocytosis

open access: yeseLife, 2015
Synaptic-soluble N-ethylmaleimide-sensitive factor attachment receptor (SNARE) proteins couple their stage-wise folding/assembly to rapid exocytosis of neurotransmitters in a Munc18-1-dependent manner.
Lu Ma   +6 more
doaj   +1 more source

The rab3A-22A chimera prevents sperm exocytosis by stabilizing open fusion pores [PDF]

open access: yes, 2016
At the final stage of exocytotis, a fusion pore opens between the plasma and a secretory vesicle membranes; typically, when the pore dilates the vesicle releases its cargo.
Bustos, Matias Alberto   +5 more
core   +1 more source

By dawn or dusk—how circadian timing rewrites bacterial infection outcomes

open access: yesFEBS Letters, EarlyView.
The circadian clock shapes immune function, yet its influence on infection outcomes is only beginning to be understood. This review highlights how circadian timing alters host responses to the bacterial pathogens Salmonella enterica, Listeria monocytogenes, and Streptococcus pneumoniae revealing that the effectiveness of immune defense depends not only
Devons Mo   +2 more
wiley   +1 more source

The Sec1/Munc18 protein Vps45 holds the Qa-SNARE Tlg2 in an open conformation

open access: yeseLife, 2020
Fusion of intracellular trafficking vesicles is mediated by the assembly of SNARE proteins into membrane-bridging complexes. SNARE-mediated membrane fusion requires Sec1/Munc18-family (SM) proteins, SNARE chaperones that can function as templates to ...
Travis J Eisemann   +5 more
doaj   +1 more source

SNARE protein mimicry by an intracellular bacterium. [PDF]

open access: yesPLoS Pathogens, 2008
Many intracellular pathogens rely on host cell membrane compartments for their survival. The strategies they have developed to subvert intracellular trafficking are often unknown, and SNARE proteins, which are essential for membrane fusion, are possible ...
Cédric Delevoye   +6 more
doaj   +1 more source

Loss of AP-3 function affects spontaneous and evoked release at hippocampal mossy fiber synapses [PDF]

open access: yes, 2006
Synaptic vesicle (SV) exocytosis mediating neurotransmitter release occurs spontaneously at low intraterminal calcium concentrations and is stimulated by a rise in intracellular calcium.
A. Scheuber   +32 more
core   +6 more sources

Structural insights into lacto‐N‐biose I recognition by a family 32 carbohydrate‐binding module from Bifidobacterium bifidum

open access: yesFEBS Letters, EarlyView.
Bifidobacterium bifidum establishes symbiosis with infants by metabolizing lacto‐N‐biose I (LNB) from human milk oligosaccharides (HMOs). The extracellular multidomain enzyme LnbB drives this process, releasing LNB via its catalytic glycoside hydrolase family 20 (GH20) lacto‐N‐biosidase domain.
Xinzhe Zhang   +5 more
wiley   +1 more source

The Caenorhabditis elegans DPF‐3 and human DPP4 have tripeptidyl peptidase activity

open access: yesFEBS Letters, EarlyView.
The dipeptidyl peptidase IV (DPPIV) family comprises serine proteases classically defined by their ability to remove dipeptides from the N‐termini of substrates, a feature that gave the family its name. Here, we report the discovery of a previously unrecognized tripeptidyl peptidase activity in DPPIV family members from two different species.
Aditya Trivedi, Rajani Kanth Gudipati
wiley   +1 more source

Multiple factors maintain assembled trans-SNARE complexes in the presence of NSF and αSNAP

open access: yeseLife, 2019
Neurotransmitter release requires formation of trans-SNARE complexes between the synaptic vesicle and plasma membranes, which likely underlies synaptic vesicle priming to a release-ready state.
Eric A. Prinslow   +4 more
semanticscholar   +1 more source

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