Structured Review

Syntaxin syntaxin sx
Schematic view of the SNARE complex. The four parallel helices of synaptobrevin (Sb), <t>syntaxin</t> (Sx), and SNAP25 form the core bundle of the complex. One arginine and three glutamine residues constitute the ionic layer, which divides the C-terminal domain
Syntaxin Sx, supplied by Syntaxin, used in various techniques. Bioz Stars score: 88/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/syntaxin sx/product/Syntaxin
Average 88 stars, based on 1 article reviews
Price from $9.99 to $1999.99
syntaxin sx - by Bioz Stars, 2020-09
88/100 stars

Images

1) Product Images from "Simulations Reveal Multiple Intermediates in the Unzipping Mechanism of Neuronal SNARE Complex"

Article Title: Simulations Reveal Multiple Intermediates in the Unzipping Mechanism of Neuronal SNARE Complex

Journal: Biophysical Journal

doi: 10.1016/j.bpj.2018.08.043

Schematic view of the SNARE complex. The four parallel helices of synaptobrevin (Sb), syntaxin (Sx), and SNAP25 form the core bundle of the complex. One arginine and three glutamine residues constitute the ionic layer, which divides the C-terminal domain
Figure Legend Snippet: Schematic view of the SNARE complex. The four parallel helices of synaptobrevin (Sb), syntaxin (Sx), and SNAP25 form the core bundle of the complex. One arginine and three glutamine residues constitute the ionic layer, which divides the C-terminal domain

Techniques Used:

2) Product Images from "Single Molecule Probing of Exocytotic Protein Interactions Using Force Spectroscopy"

Article Title: Single Molecule Probing of Exocytotic Protein Interactions Using Force Spectroscopy

Journal: Croatica chemica acta. Arhiv za kemiju

doi:

Exocytotic release of transmitter utilizes SNARE proteins. (a) The ternary SNARE complex consists of synaptobrevin 2 (red), also known as vesicle-associated membrane protein 2 (VAMP 2), located on the vesicular membrane; syntaxin (green) and synaptosome-associated
Figure Legend Snippet: Exocytotic release of transmitter utilizes SNARE proteins. (a) The ternary SNARE complex consists of synaptobrevin 2 (red), also known as vesicle-associated membrane protein 2 (VAMP 2), located on the vesicular membrane; syntaxin (green) and synaptosome-associated

Techniques Used:

3) Product Images from "Simulations Reveal Multiple Intermediates in the Unzipping Mechanism of Neuronal SNARE Complex"

Article Title: Simulations Reveal Multiple Intermediates in the Unzipping Mechanism of Neuronal SNARE Complex

Journal: Biophysical Journal

doi: 10.1016/j.bpj.2018.08.043

Schematic view of the SNARE complex. The four parallel helices of synaptobrevin (Sb), syntaxin (Sx), and SNAP25 form the core bundle of the complex. One arginine and three glutamine residues constitute the ionic layer, which divides the C-terminal domain
Figure Legend Snippet: Schematic view of the SNARE complex. The four parallel helices of synaptobrevin (Sb), syntaxin (Sx), and SNAP25 form the core bundle of the complex. One arginine and three glutamine residues constitute the ionic layer, which divides the C-terminal domain

Techniques Used:

4) Product Images from "Reconciling the regulatory role of Munc18 proteins in SNARE-complex assembly"

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

Journal: IUCrJ

doi: 10.1107/S2052252514020727

SNARE proteins involved in membrane fusion. ( a ) Domain arrangements of the SNARE proteins: syntaxin, SNAP23/25 and VAMP2 (TMD, transmembrane domain); ( b ) trans -SNARE-complex formation through interaction of SNARE motifs on t-SNARE proteins (syntaxin and SNAP on the target membrane) with the SNARE motif of the v-SNARE protein (VAMP2) on the vesicle membrane; ( c ) cis -SNARE complex with the TMD of syntaxin and VAMP2 on the same membrane. The blue circle labeled ‘N’ is the N-peptide. Palmitoylation anchors for SNAP23/25 are not shown in panels ( b ) and ( c ).
Figure Legend Snippet: SNARE proteins involved in membrane fusion. ( a ) Domain arrangements of the SNARE proteins: syntaxin, SNAP23/25 and VAMP2 (TMD, transmembrane domain); ( b ) trans -SNARE-complex formation through interaction of SNARE motifs on t-SNARE proteins (syntaxin and SNAP on the target membrane) with the SNARE motif of the v-SNARE protein (VAMP2) on the vesicle membrane; ( c ) cis -SNARE complex with the TMD of syntaxin and VAMP2 on the same membrane. The blue circle labeled ‘N’ is the N-peptide. Palmitoylation anchors for SNAP23/25 are not shown in panels ( b ) and ( c ).

Techniques Used: Labeling

Related Articles

other:

Article Title: Energetics of (Dis)Assembly of the Ternary SNARE ComplexA commentary on Is assembly of the SNARE complex enough to fuel membrane fusion?
Article Snippet: In the majority of neurons, this complex is composed of the vesicular protein synaptobrevin 2 (Sb2), and two proteins located at the plasma membrane, syntaxin (Sx) and synaptosome-associated protein of 25 kDa (SNAP25).

Article Title: Neuronal SNAREs Do Not Trigger Fusion between Synthetic Membranes but Do Promote PEG-Mediated Membrane Fusion
Article Snippet: The three soluble N -ethyl maleimide sensitive factor attachment protein receptor (SNARE) proteins synaptobrevin (SB), located in the synaptic vesicle membrane, and syntaxin (SX) and SNAP-25 (SN25), both located in the presynaptic membrane, play an important role in this highly regulated process ( ).

Article Title: Interactions between Neuronal Fusion Proteins Explored by Molecular Dynamics
Article Snippet: The structure of the assembled neuronal SNARE complex consists of a parallel four-helical bundle forming a ternary assembly of the synaptobrevin (Sb), syntaxin (Sx), and SNAP-25 (Sn) proteins (see ).

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    Syntaxin syntaxin sx
    Schematic view of the SNARE complex. The four parallel helices of synaptobrevin (Sb), <t>syntaxin</t> (Sx), and SNAP25 form the core bundle of the complex. One arginine and three glutamine residues constitute the ionic layer, which divides the C-terminal domain
    Syntaxin Sx, supplied by Syntaxin, used in various techniques. Bioz Stars score: 88/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/syntaxin sx/product/Syntaxin
    Average 88 stars, based on 2 article reviews
    Price from $9.99 to $1999.99
    syntaxin sx - by Bioz Stars, 2020-09
    88/100 stars
      Buy from Supplier

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    Schematic view of the SNARE complex. The four parallel helices of synaptobrevin (Sb), syntaxin (Sx), and SNAP25 form the core bundle of the complex. One arginine and three glutamine residues constitute the ionic layer, which divides the C-terminal domain

    Journal: Biophysical Journal

    Article Title: Simulations Reveal Multiple Intermediates in the Unzipping Mechanism of Neuronal SNARE Complex

    doi: 10.1016/j.bpj.2018.08.043

    Figure Lengend Snippet: Schematic view of the SNARE complex. The four parallel helices of synaptobrevin (Sb), syntaxin (Sx), and SNAP25 form the core bundle of the complex. One arginine and three glutamine residues constitute the ionic layer, which divides the C-terminal domain

    Article Snippet: Synaptobrevin (Sb) and syntaxin (Sx) both contribute to this complex with one α -helix, whereas SNAP25 consists of two α -helical motifs connected by an unstructured linker loop.

    Techniques:

    Specificity of Munc18:Syntaxin interactions. Munc18a (cyan) binds Sx1 (magenta) via two tight binding modes (left hand side). One binding mode occurs in the presence of the Sx1 N-peptide, the other in its absence. “Non-cognate” Munc18c (gray) also binds tightly to Sx1, though its interaction with Sx1 lacking the N-peptide is very weak (indicated by dotted line). Munc18c binds more tightly than Munc18a to Sx4 (orange) but neither Munc18 recognises Sx4 lacking its N-peptide. These findings indicate that Munc18a and Munc18c bind Sxs differently. Specifically Munc18a has two tight binding modes/sites for Sx1 one of which does not require the N-peptide binding interaction. Munc18c has one tight binding mode/site for Sx4 or Sx1 that requires the Sx N-peptide.

    Journal: PLoS ONE

    Article Title: Revisiting interaction specificity reveals neuronal and adipocyte Munc18 membrane fusion regulatory proteins differ in their binding interactions with partner SNARE Syntaxins

    doi: 10.1371/journal.pone.0187302

    Figure Lengend Snippet: Specificity of Munc18:Syntaxin interactions. Munc18a (cyan) binds Sx1 (magenta) via two tight binding modes (left hand side). One binding mode occurs in the presence of the Sx1 N-peptide, the other in its absence. “Non-cognate” Munc18c (gray) also binds tightly to Sx1, though its interaction with Sx1 lacking the N-peptide is very weak (indicated by dotted line). Munc18c binds more tightly than Munc18a to Sx4 (orange) but neither Munc18 recognises Sx4 lacking its N-peptide. These findings indicate that Munc18a and Munc18c bind Sxs differently. Specifically Munc18a has two tight binding modes/sites for Sx1 one of which does not require the N-peptide binding interaction. Munc18c has one tight binding mode/site for Sx4 or Sx1 that requires the Sx N-peptide.

    Article Snippet: SM proteins are SNARE binding proteins that play a crucial role in the late stages of vesicle docking and fusion, as well as stabilisation of the target Syntaxin (Sx) proteins.

    Techniques: Binding Assay

    Exocytotic release of transmitter utilizes SNARE proteins. (a) The ternary SNARE complex consists of synaptobrevin 2 (red), also known as vesicle-associated membrane protein 2 (VAMP 2), located on the vesicular membrane; syntaxin (green) and synaptosome-associated

    Journal: Croatica chemica acta. Arhiv za kemiju

    Article Title: Single Molecule Probing of Exocytotic Protein Interactions Using Force Spectroscopy

    doi:

    Figure Lengend Snippet: Exocytotic release of transmitter utilizes SNARE proteins. (a) The ternary SNARE complex consists of synaptobrevin 2 (red), also known as vesicle-associated membrane protein 2 (VAMP 2), located on the vesicular membrane; syntaxin (green) and synaptosome-associated

    Article Snippet: The core SNARE complex is comprised of synaptobrevin 2 (Sb2), also known as vesicle-associated membrane protein 2 (VAMP 2), located on the vesicular membrane; syntaxin (Sx) and synaptosome-associated protein of 25 kDa (SNAP25), both located on the plasma membrane.

    Techniques: