Výsledky vyhledávání - "V. N. Subramaniam"

N-Ethylmaleimide-sensitive Factor (NSF) and α-Soluble NSF Attachment Proteins (SNAP) Mediate Dissociation of GS28-Syntaxin 5 Golgi SNAP Receptors (SNARE) Complex

Autor: V. N. Subramaniam, Eva Loh, Wanjin Hong

Publikováno v: Journal of Biological Chemistry. 272:25441-25444

Golgi soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) GS28 and syntaxin 5 can be reciprocally coimmunoprecipitated from Golgi extracts, suggesting that they exist in a protein complex. When Golgi extract is preincubate

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::77cbd3bad86893396383c0a6bd091257
https://doi.org/10.1074/jbc.272.41.25441

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cDNA characterization and chromosomal mapping of human golgi SNARE GS27 and GS28 to chromosome 17

Autor: Elaine R. Levy, T. D. Bui, S. L. Lowe, Wanjin Hong, V. N. Subramaniam

Publikováno v: Genomics. 57(2)

Transport of proteins along the exocytotic pathway is primarily achieved by vesicular intermediates. Two proteins, Golgi SNAREs of 27 kDa, GS27, and of 28 kDa, GS28 (HGMW-approved nomenclature GOSR2 and GOSR1, respectively), are important trafficking

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::654bd3276d01eab9bdb378d6ce56196d
https://pubmed.ncbi.nlm.nih.gov/10198168

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Alpha-SNAP but not gamma-SNAP is required for ER-Golgi transport after vesicle budding and the Rab1-requiring step but before the EGTA-sensitive step

Autor: Bor Luen Tang, Wanjin Hong, Siew Heng Wong, V. N. Subramaniam, F. Peter

Publikováno v: Journal of cell science. 111

N-ethylmaleimide-sensitive factor (NSF) and soluble NSF attachment proteins (SNAPs) have been implicated in diverse vesicular transport events; yet their exact role and site of action remain to be established. Using an established in vitro system, we

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::df8a6394db052b3725de769775667dc2
https://pubmed.ncbi.nlm.nih.gov/9701561

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GS15, a 15-kilodalton Golgi soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) homologous to rbet1

Autor: Wanjin Hong, Siew Heng Wong, Yue Xu, V. N. Subramaniam, Tong Zhang

Publikováno v: The Journal of biological chemistry. 272(32)

Bet1p plays an essential role in vesicular transport from the endoplasmic reticulum (ER) to the Golgi in yeast, and it functions as a vesicle soluble N-ethylmaleimide-sensitive factor protein receptor (v-SNARE). A mammalian protein related to Bet1p h

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e8e8562e1f5d9ebcaeccbcc2f4b53408
https://pubmed.ncbi.nlm.nih.gov/9242691

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Cytosolic factors block antibody binding to the C-terminal cytoplasmic tail of the KDEL receptor

Autor: B L, Tang, S H, Wong, S H, Low, V N, Subramaniam, W, Hong

Publikováno v: European journal of cell biology. 65(2)

The mammalian KDEL receptor is an extremely hydrophobic membrane protein. One of the longest stretches of hydrophilic sequence resides at the C-terminus. Various antibodies against a synthetic peptide corresponding to this region confirmed that the C

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::5dfa5bd2a60f68f5234522ca251fbc8c
https://pubmed.ncbi.nlm.nih.gov/7720725

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Golgi-localized beta-galactoside alpha 2,6-sialyltransferase in transfected CHO cells is redistributed into the endoplasmic reticulum by brefeldin A

Autor: B L, Tang, S H, Wong, X, Qi, V N, Subramaniam, W, Hong

Publikováno v: European journal of cell biology. 59(1)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::516e56a71e83c57fad4c2e15c90e761c
https://pubmed.ncbi.nlm.nih.gov/1468444

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Biochemical fractionation and characterization of proteins from Golgi-enriched membranes

Autor: V N, Subramaniam, A R, bin Mohd Yusoff, S H, Wong, G B, Lim, M, Chew, W, Hong

Publikováno v: The Journal of biological chemistry. 267(17)

Fractions enriched in Golgi membranes were prepared from rat liver by sucrose gradient ultracentrifugation. These enriched membranes were further subfractionated on the basis of their solubilities in EGTA, 150 mM sodium carbonate, pH 11.5, sodium deo

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::daa241d7f103120a87fe200629505575
https://pubmed.ncbi.nlm.nih.gov/1601872

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Inhibition by brefeldin A of protein secretion from the apical cell surface of Madin-Darby canine kidney cells

Autor: S H, Low, S H, Wong, B L, Tang, P, Tan, V N, Subramaniam, W, Hong

Publikováno v: The Journal of biological chemistry. 266(27)

The effect of brefeldin A (BFA) on total and polarized protein secretion was examined in MDCK cells. Increasing concentrations of BFA have increasingly inhibitory effects on total protein secretion. The total protein secretion was essentially unaffec

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::d46e57e53adc852c5e7e32660e04d7ea
https://pubmed.ncbi.nlm.nih.gov/1917917

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Apical cell surface expression of rat dipeptidyl peptidase IV in transfected Madin-Darby canine kidney cells

Autor: S H, Low, S H, Wong, B L, Tang, V N, Subramaniam, W J, Hong

Publikováno v: The Journal of biological chemistry. 266(20)

Dipeptidyl peptidase IV (DPPIV) is a type II membrane glycoprotein that is predominantly localized to the apical plasma membrane in various epithelial cells. In order to understand in more detail the biogenesis and sorting of DPPIV, the cDNA for rat

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::822961d45365d829c9c2a2863dc77c00
https://pubmed.ncbi.nlm.nih.gov/1677006

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