Výsledky vyhledávání - "B W Wattenberg"

The regulated degradation of a 3-hydroxy-3-methylglutaryl-coenzyme A reductase reporter construct occurs in the endoplasmic reticulum

Autor: L W, Lecureux, B W, Wattenberg

Publikováno v: Journal of Cell Science. 107:2635-2642

The rate-limiting enzyme in cholesterol biosynthesis, 3-hydroxy-3-methylglutaryl-coenzyme A (HMG CoA) reductase, is regulated at a number of levels. One important mechanism is regulation of the half-life of the protein by a controlled proteolytic sys

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ee10a7eef8358737ebc682707df261a4
https://doi.org/10.1242/jcs.107.9.2635

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Expression of a catalytically inactive sphingosine kinase mutant blocks agonist-induced sphingosine kinase activation. A dominant-negative sphingosine kinase

Autor: S M, Pitson, P A, Moretti, J R, Zebol, P, Xia, J R, Gamble, M A, Vadas, R J, D'Andrea, B W, Wattenberg

Publikováno v: The Journal of biological chemistry. 275(43)

Sphingosine kinase (SK) catalyzes the formation of sphingosine 1-phosphate (S1P), a lipid messenger that plays an important role in a variety of mammalian cell processes, including inhibition of apoptosis and stimulation of cell proliferation. Basal

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::5066501f3cb3602b7b04245c1b801437
https://pubmed.ncbi.nlm.nih.gov/10944534

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Targeting and insertion of C-terminally anchored proteins to the mitochondrial outer membrane is specific and saturable but does not strictly require ATP or molecular chaperones

Autor: L, Lan, S, Isenmann, B W, Wattenberg

Publikováno v: The Biochemical journal. 349(Pt 2)

A distinct class of proteins contain a C-terminal membrane anchor and a cytoplasmic functional domain. A subset of these proteins is targeted to the mitochondrial outer membrane. Here, to probe for the involvement of a saturable targeting mechanism f

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::40f412eeb5877c4d952aa5eca966acb8
https://pubmed.ncbi.nlm.nih.gov/10880361

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Fusion Rapidly Follows Vesicle Transport to the Target Membrane in Protein Transport through the Golgi Apparatus in Vitro. A Re-evaluation of Transport Kinetics Based on the Finding that the Glycosylation Used to Mark Transport, and Not Transport Itself, is Rate Limiting in the Assay

Autor: B. W. Wattenberg, R. R. Hiebsch

Publikováno v: Molecular Mechanisms of Membrane Traffic ISBN: 9783662029305

A well characterized assay measuring protein transport between compartments of the Golgi apparatus (W.E. Balch et al, 1984, Cell 39:405416) utilizes glycosylation of a membrane protein to mark transit. Previously, kinetic analysis of the assay relied

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::e3f826df3796e1adb5f009e60196fd33
https://doi.org/10.1007/978-3-662-02928-2_4

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Primaquine blocks transport by inhibiting the formation of functional transport vesicles. Studies in a cell-free assay of protein transport through the Golgi apparatus

Autor: R R, Hiebsch, T J, Raub, B W, Wattenberg

Publikováno v: The Journal of biological chemistry. 266(30)

The lysosomotropic amine primaquine has previously been shown to inhibit both secretory and recycling processes of cells in culture. We have used a cell-free assay that reconstitutes glycoprotein transport through the Golgi apparatus to investigate t

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::81ebd773e8c98f4ac46cbf51e7ce53e8
https://pubmed.ncbi.nlm.nih.gov/1657920

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The molecular control of transport vesicle fusion

Autor: B W, Wattenberg

Publikováno v: The New biologist. 2(6)

The fusion of transport vesicles with the appropriate target membrane in constitutive transport is a complex and well-controlled process. Many of the molecular details of the reactions that result in this control are being revealed through the use of

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::ef48f5fc0d341b96bead09337f698788
https://pubmed.ncbi.nlm.nih.gov/2128471

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Sterol partitioning among intracellular membranes. Testing a model for cellular sterol distribution

Autor: B W Wattenberg, D F Silbert

Publikováno v: Journal of Biological Chemistry. 258:2284-2289

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::9ea55a43cbb8d9b3b51259e7bf1088ac
https://doi.org/10.1016/s0021-9258(18)32920-x

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Sterol depletion of LM cells using chemical inhibitors and genetic defects. A comparison of secondary phospholipid alterations

Autor: B W Wattenberg, C. E. Freter, D. F. Silbert

Publikováno v: Journal of Biological Chemistry. 254:12295-12298

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::618570c416f46b43dda5937a0a6a1ce9
https://doi.org/10.1016/s0021-9258(19)86312-3

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Multiple cytosolic components promote intra-Golgi protein transport. Resolution of a protein acting at a late stage, prior to membrane fusion

Autor: B W, Wattenberg, J E, Rothman

Publikováno v: The Journal of biological chemistry. 261(5)

Cytosolic components are required to produce the "primed donor" and to consume the "dilution-resistant" intermediates of the intercompartmental protein transport pathway as elucidated in a cell-free system (Balch, W. E., Glick, B. S., and Rothman, J.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::4f9772ad9fa86cb459293ad10ecf4707
https://pubmed.ncbi.nlm.nih.gov/3003102

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