FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2099539214> ?p ?o ?g. }

• W2099539214 abstract "This work centered on the SNARE proteins syntaxin 1, SNAP-25, and synaptobrevin 2, which drive the discharge of neurotransmitters from synaptic vesicles. A relatively simple scenario for the role of SNAREs in neurotransmitter release is given by the zipper model, which assumes that the SNARE assembly proceeds from N → C terminus and the energy released during the assembly is probably sufficient to overcome the energy barrier for fusion. However, the evidence for the zipper model is largely circumstantial.Physiologically, neurotransmitter release takes place in milliseconds, but when neuronal SNAREs are reconstituted into liposomes, fusion occurs very slowly (> several minutes). The initial part of this work addressed this long-standing controversy in the SNARE field. Biochemical analysis demonstrates the sequential assembly of neuronal SNAREs. The assembly initiates with the formation of transient dimer of syntaxin and SNAP-25, which constitutes the appropriate binding site for synaptobrevin. However this binding site is also readily occupied by a second syntaxin molecule, resulting in an `off-pathway´ 2:1 syntaxin-SNAP-25 complex. In the beginning of the work we hypothesized that the liposome fusion is probably slow because of this `off-pathway´ reaction. In this study a ternary SNARE complex containing syntaxin, SNAP-25 and C-terminal portion of synaptobrevin prevented this `off-pathway´ reaction. This ΔN complex was also a structural mimic of syntaxin-SNAP-25 dimer. When this complex was reconstituted into liposomes the fusion was greatly enhanced. Therefore by providing an appropriate binding site and by preventing the `off-pathway´ reaction, SNAREs can rapidly fuse membranes. My data also demonstrates that the synaptobrevin binding site is restricted to the N-terminal portion of the Q-SNAREs. Thus, my study supports the zipper model.The other part of the work focused on the soluble SNARE regulatory proteins tomosyn and Amisyn. The initial detailed characterization of the SNARE motif of tomosyn led to the elucidation of the crystal structure of the core tomosyn SNARE complex, which is a four-helix bundle similar to that of the SNARE complex containing synaptobrevin. The tomosyn in the SNARE complex cannot be replaced by synaptobrevin and my work supports the view that tomosyn acts as a negative regulator of exocytosis. The full-length and the SNARE motif of amisyn, like tomosyn, formed a stable ternary complex with syntaxin and SNAP-25. Preliminary experiments suggested that amisyn also acts as a negative regulator of exocytosis.>" @default.
• W2099539214 created "2016-06-24" @default.
• W2099539214 creator A5033859458 @default.
• W2099539214 date "2022-02-20" @default.
• W2099539214 modified "2023-10-03" @default.
• W2099539214 title "Characterization of neuronal SNAREs and interacting proteins" @default.
• W2099539214 cites W1540559701 @default.
• W2099539214 cites W1544228065 @default.
• W2099539214 cites W1555714096 @default.
• W2099539214 cites W1607993356 @default.
• W2099539214 cites W1700565657 @default.
• W2099539214 cites W1822252127 @default.
• W2099539214 cites W1875944393 @default.
• W2099539214 cites W1927485791 @default.
• W2099539214 cites W1944127002 @default.
• W2099539214 cites W1966364658 @default.
• W2099539214 cites W1970930136 @default.
• W2099539214 cites W1972816955 @default.
• W2099539214 cites W1973361899 @default.
• W2099539214 cites W1975085160 @default.
• W2099539214 cites W1976479871 @default.
• W2099539214 cites W1994342014 @default.
• W2099539214 cites W1996598000 @default.
• W2099539214 cites W2003813143 @default.
• W2099539214 cites W2005852124 @default.
• W2099539214 cites W2006158152 @default.
• W2099539214 cites W2009073915 @default.
• W2099539214 cites W2013617213 @default.
• W2099539214 cites W2014045979 @default.
• W2099539214 cites W2014229034 @default.
• W2099539214 cites W2016266703 @default.
• W2099539214 cites W2018757497 @default.
• W2099539214 cites W2020222865 @default.
• W2099539214 cites W2022772974 @default.
• W2099539214 cites W2027775552 @default.
• W2099539214 cites W2033500343 @default.
• W2099539214 cites W2034468530 @default.
• W2099539214 cites W2038728575 @default.
• W2099539214 cites W2040368827 @default.
• W2099539214 cites W2042212641 @default.
• W2099539214 cites W2047808133 @default.
• W2099539214 cites W2049199355 @default.
• W2099539214 cites W2050325660 @default.
• W2099539214 cites W2063959590 @default.
• W2099539214 cites W2085370553 @default.
• W2099539214 cites W2086442201 @default.
• W2099539214 cites W2093465143 @default.
• W2099539214 cites W2100837269 @default.
• W2099539214 cites W2103376970 @default.
• W2099539214 cites W2104801664 @default.
• W2099539214 cites W2107335219 @default.
• W2099539214 cites W2118140199 @default.
• W2099539214 cites W2125384218 @default.
• W2099539214 cites W2128635872 @default.
• W2099539214 cites W2135839939 @default.
• W2099539214 cites W2136178051 @default.
• W2099539214 cites W2155219479 @default.
• W2099539214 cites W2161485116 @default.
• W2099539214 cites W2165068760 @default.
• W2099539214 cites W2168833657 @default.
• W2099539214 cites W2170349574 @default.
• W2099539214 cites W3202912068 @default.
• W2099539214 doi "https://doi.org/10.53846/goediss-3234" @default.
• W2099539214 hasPublicationYear "2022" @default.
• W2099539214 type Work @default.
• W2099539214 sameAs 2099539214 @default.
• W2099539214 citedByCount "0" @default.
• W2099539214 crossrefType "dissertation" @default.
• W2099539214 hasAuthorship W2099539214A5033859458 @default.
• W2099539214 hasBestOaLocation W20995392141 @default.
• W2099539214 hasConcept C103038307 @default.
• W2099539214 hasConcept C12554922 @default.
• W2099539214 hasConcept C130316041 @default.
• W2099539214 hasConcept C148785051 @default.
• W2099539214 hasConcept C185592680 @default.
• W2099539214 hasConcept C196330066 @default.
• W2099539214 hasConcept C2777029164 @default.
• W2099539214 hasConcept C2778256703 @default.
• W2099539214 hasConcept C2908790754 @default.
• W2099539214 hasConcept C41625074 @default.
• W2099539214 hasConcept C55493867 @default.
• W2099539214 hasConcept C86803240 @default.
• W2099539214 hasConcept C95444343 @default.
• W2099539214 hasConceptScore W2099539214C103038307 @default.
• W2099539214 hasConceptScore W2099539214C12554922 @default.
• W2099539214 hasConceptScore W2099539214C130316041 @default.
• W2099539214 hasConceptScore W2099539214C148785051 @default.
• W2099539214 hasConceptScore W2099539214C185592680 @default.
• W2099539214 hasConceptScore W2099539214C196330066 @default.
• W2099539214 hasConceptScore W2099539214C2777029164 @default.
• W2099539214 hasConceptScore W2099539214C2778256703 @default.
• W2099539214 hasConceptScore W2099539214C2908790754 @default.
• W2099539214 hasConceptScore W2099539214C41625074 @default.
• W2099539214 hasConceptScore W2099539214C55493867 @default.
• W2099539214 hasConceptScore W2099539214C86803240 @default.
• W2099539214 hasConceptScore W2099539214C95444343 @default.
• W2099539214 hasLocation W20995392141 @default.
• W2099539214 hasOpenAccess W2099539214 @default.
• W2099539214 hasPrimaryLocation W20995392141 @default.
• W2099539214 hasRelatedWork W13294641 @default.

• next