Zobrazeno 1 - 10 of 43 pro vyhledávání: '"B W Wattenberg"'
1
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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2
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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3
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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4
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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5
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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6
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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9
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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10
A novel prefusion complex formed during protein transport between Golgi cisternae in a cell-free system
Autor: B W, Wattenberg, W E, Balch, J E, Rothman
Publikováno v: The Journal of biological chemistry. 261(5)
Examination of a cell-free reconstitution of intercompartmental transport through the Golgi apparatus has enabled detection of two intermediates in the pathway (Balch, W. E., Glick, B. S., and Rothman, J. E. (1984) Cell 39, 525-536). These intermedia
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::bb6370873a0a537a65d21dc67e6b8122
https://pubmed.ncbi.nlm.nih.gov/3003101
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