Results 21 to 30 of about 25,530 (255)

A KNN Model Based on Manhattan Distance to Identify the SNARE Proteins

open access: yesIEEE Access, 2020
SNARE proteins, known as membrane fusion proteins, play a primary role to mediate vesicle fusion. Loss of function of the SNARE protein can lead to a variety of diseases. A method to accurately identify the SNARE protein is important and necessary.
Xing Gao, Guilin Li
doaj   +1 more source

Mechanisms of SNARE proteins in membrane fusion. [PDF]

open access: yesNat Rev Mol Cell Biol, 2023
Soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) are a family of small conserved eukaryotic proteins that mediate membrane fusion between organelles and with the plasma membrane. SNAREs are directly or indirectly anchored to membranes.
Jahn R, Cafiso DC, Tamm LK.
europepmc   +5 more sources

A Pearson Based Feature Compressing Model for SNARE Protein Classification

open access: yesIEEE Access, 2020
SNARE proteins are a group of proteins that drive the biological fusion of two membranes. It is important to identify them accurately, because malfunction of the SNARE proteins can lead to a lot of diseases.
Guilin Li
doaj   +1 more source

SNARE zippering requires activation by SNARE-like peptides in Sec1/Munc18 proteins [PDF]

open access: yesProceedings of the National Academy of Sciences, 2018
Significance Soluble N -ethylmaleimide-sensitive factor attachment protein receptor(SNARE) proteins drive membrane fusion by zippering into coiled-coil bundles between membrane bilayers. In this work, we showed that certain layers in the SNARE bundle are dispensable for SNARE-mediated membrane fusion ...
Haijia Yu   +6 more
openaire   +2 more sources

Reconciling the regulatory role of Munc18 proteins in SNARE-complex assembly

open access: yesIUCrJ, 2014
Membrane fusion is essential for human health, playing a vital role in processes as diverse as neurotransmission and blood glucose control. Two protein families are key: (1) the Sec1p/Munc18 (SM) and (2) the soluble N-ethylmaleimide-sensitive attachment ...
Asma Rehman   +5 more
doaj   +1 more source

Molecular Dynamics Simulations of the Proteins Regulating Synaptic Vesicle Fusion

open access: yesMembranes, 2023
Neuronal transmitters are packaged in synaptic vesicles (SVs) and released by the fusion of SVs with the presynaptic membrane (PM). An inflow of Ca2+ into the nerve terminal triggers fusion, and the SV-associated protein Synaptotagmin 1 (Syt1) serves as ...
Maria Bykhovskaia
doaj   +1 more source

ER assembly of SNARE complexes mediating formation of partitioning membrane in Arabidopsis cytokinesis

open access: yeseLife, 2017
Intracellular membrane fusion mediates diverse processes including cell growth, division and communication. Fusion involves complex formation between SNARE proteins anchored to adjacent membranes.
Matthias Karnahl   +4 more
doaj   +1 more source

Role of SNAREs in Neurodegenerative Diseases

open access: yesCells, 2021
Neurodegenerative diseases are pathologies of the central and peripheral nervous systems characterized by loss of brain functions and problems in movement which occur due to the slow and progressive degeneration of cellular elements.
Azzurra Margiotta
doaj   +1 more source

A comparative analysis of trypanosomatid SNARE proteins. [PDF]

open access: yesParasitol Int, 2014
The Kinetoplastida are flagellated protozoa evolutionary distant and divergent from yeast and humans. Kinetoplastida include trypanosomatids, and a number of important pathogens. Trypanosoma brucei, Trypanosoma cruzi and Leishmania spp. inflict significant morbidity and mortality on humans and livestock as the etiological agents of human African ...
Murungi E   +6 more
europepmc   +3 more sources

Structural and Functional Analysis of the CAPS SNARE-Binding Domain Required for SNARE Complex Formation and Exocytosis

open access: yesCell Reports, 2019
Summary: Exocytosis of synaptic vesicles and dense-core vesicles requires both the Munc13 and CAPS (Ca2+-dependent activator proteins for secretion) proteins.
Hao Zhou   +5 more
doaj   +1 more source

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