Thematische Bibliographien / Vesicular transport proteins

Inhaltsverzeichnis

  1. Zeitschriftenartikel
  2. Dissertationen
  3. Bücher
  4. Buchteile

Auswahl der wissenschaftlichen Literatur zum Thema „Vesicular transport proteins“

Autor: Grafiati
Veröffentlicht am 4. Juni 2021
Zuletzt aktualisiert am 13. Februar 2022

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Zeitschriftenartikel zum Thema "Vesicular transport proteins"

1

NAKANO, AKIHIKO. "Vesicular Transport of Proteins in Yeast." RADIOISOTOPES 44, no. 3 (1995): 221–22. http://dx.doi.org/10.3769/radioisotopes.44.221.

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2

Balch, William E. "Small GTP-binding proteins in vesicular transport." Trends in Biochemical Sciences 15, no. 12 (1990): 473–77. http://dx.doi.org/10.1016/0968-0004(90)90301-q.

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Kurzchalia, T. V., P. Dupree, R. G. Parton, et al. "VIP21, a 21-kD membrane protein is an integral component of trans-Golgi-network-derived transport vesicles." Journal of Cell Biology 118, no. 5 (1992): 1003–14. http://dx.doi.org/10.1083/jcb.118.5.1003.

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In simple epithelial cells, apical and basolateral proteins are sorted into separate vesicular carriers before delivery to the appropriate plasma membrane domains. To dissect the putative sorting machinery, we have solubilized Golgi-derived transport vesicles with the detergent CHAPS and shown that an apical marker, influenza haemagglutinin (HA), formed a large complex together with several integral membrane proteins. Remarkably, a similar set of CHAPS-insoluble proteins was found after solubilization of a total cellular membrane fraction. This allowed the cloning of a cDNA encoding one protei
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Stow, Jennifer L. "Regulation of vesicular transport by GTP-binding proteins." Current Opinion in Nephrology and Hypertension 4, no. 5 (1995): 421–25. http://dx.doi.org/10.1097/00041552-199509000-00009.

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Waters, M. Gerard, Irene C. Griff, and James E. Rothman. "Proteins involved in vesicular transport and membrane fusion." Current Opinion in Cell Biology 3, no. 4 (1991): 615–20. http://dx.doi.org/10.1016/0955-0674(91)90031-s.

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Advani, Raj J., Bin Yang, Rytis Prekeris, Kelly C. Lee, Judith Klumperman, and Richard H. Scheller. "Vamp-7 Mediates Vesicular Transport from Endosomes to Lysosomes." Journal of Cell Biology 146, no. 4 (1999): 765–76. http://dx.doi.org/10.1083/jcb.146.4.765.

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A more complete picture of the molecules that are critical for the organization of membrane compartments is beginning to emerge through the characterization of proteins in the vesicle-associated membrane protein (also called synaptobrevin) family of membrane trafficking proteins. To better understand the mechanisms of membrane trafficking within the endocytic pathway, we generated a series of monoclonal and polyclonal antibodies against the cytoplasmic domain of vesicle-associated membrane protein 7 (VAMP-7). The antibodies recognize a 25-kD membrane-associated protein in multiple tissues and
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Martínez-Menárguez, José A., Rytis Prekeris, Viola M. J. Oorschot, et al. "Peri-Golgi vesicles contain retrograde but not anterograde proteins consistent with the cisternal progression model of intra-Golgi transport." Journal of Cell Biology 155, no. 7 (2001): 1213–24. http://dx.doi.org/10.1083/jcb.200108029.

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A cisternal progression mode of intra-Golgi transport requires that Golgi resident proteins recycle by peri-Golgi vesicles, whereas the alternative model of vesicular transport predicts anterograde cargo proteins to be present in such vesicles. We have used quantitative immuno-EM on NRK cells to distinguish peri-Golgi vesicles from other vesicles in the Golgi region. We found significant levels of the Golgi resident enzyme mannosidase II and the transport machinery proteins giantin, KDEL-receptor, and rBet1 in coatomer protein I–coated cisternal rims and peri-Golgi vesicles. By contrast, when
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Predescu, Dan, Stephen M. Vogel, and Asrar B. Malik. "Functional and morphological studies of protein transcytosis in continuous endothelia." American Journal of Physiology-Lung Cellular and Molecular Physiology 287, no. 5 (2004): L895—L901. http://dx.doi.org/10.1152/ajplung.00075.2004.

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Continuous microvascular endothelium constitutively transfers protein from vessel lumen to interstitial space. Compelling recent biochemical, ultrastructural, and physiological evidence reviewed herein demonstrates that protein transport is not the result of barrier “leakiness” but, rather, is an active process occurring primarily in a transendothelial vesicular pathway. Protein accesses the vesicular pathway by means of caveolae open to the vessel lumen. Vascular tracer proteins appear in free cytoplasmic vesicles within minutes; contents of transport vesicles are rapidly deposited into the s
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Chaudhari, Rahul, Vishakha Dey, Aishwarya Narayan, Shobhona Sharma, and Swati Patankar. "Membrane and luminal proteins reach the apicoplast by different trafficking pathways in the malaria parasitePlasmodium falciparum." PeerJ 5 (April 27, 2017): e3128. http://dx.doi.org/10.7717/peerj.3128.

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The secretory pathway inPlasmodium falciparumhas evolved to transport proteins to the host cell membrane and to an endosymbiotic organelle, the apicoplast. The latter can occur via the ER or the ER-Golgi route. Here, we study these three routes using proteins Erythrocyte Membrane Protein-1 (PfEMP1), Acyl Carrier Protein (ACP) and glutathione peroxidase-like thioredoxin peroxidase (PfTPxGl) and inhibitors of vesicular transport. As expected, the G protein-dependent vesicular fusion inhibitor AlF4−and microtubule destabilizing drug vinblastine block the trafficking of PfEMP-1, a protein secreted
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FAIRN, Gregory D., and Christopher R. McMASTER. "Identification and assessment of the role of a nominal phospholipid binding region of ORP1S (oxysterol-binding-protein-related protein 1 short) in the regulation of vesicular transport." Biochemical Journal 387, no. 3 (2005): 889–96. http://dx.doi.org/10.1042/bj20041915.

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The ORPs (oxysterol-binding-protein-related proteins) constitute an enigmatic family of intracellular lipid receptors that are related through a shared lipid binding domain. Emerging evidence suggests that ORPs relate lipid metabolism to membrane transport. Current data imply that the yeast ORP Kes1p is a negative regulator of Golgi-derived vesicular transport mediated by the essential phosphatidylinositol/phosphatidylcholine transfer protein Sec14p. Inactivation of Kes1p function allows restoration of growth and vesicular transport in cells lacking Sec14p function, and Kes1p function in this
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Dissertationen zum Thema "Vesicular transport proteins"

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Barmark, Gunilla. "Functional studies of vesicular transport in yeast /." Uppsala : Dept. of Plant Biology and Forest Genetics, Swedish University of Agricultural Sciences, 2005. http://epsilon.slu.se/2005110.pdf.

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Hansson, Stefan R. "The serotonin transporter and vesicular monoamine transporters during development." Lund : Lund University, 1998. http://catalog.hathitrust.org/api/volumes/oclc/68945023.html.

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Merithew, Eric Lee. "Structural Basis for Rab5 Activation and Effector Specificity in Endosome Tethering: A Dissertation." eScholarship@UMMS, 2004. https://escholarship.umassmed.edu/gsbs_diss/278.

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As critical regulators of vesicular trafficking, Rab proteins comprise the largest GTPase family, with thirty-eight functionally distinct members and another twenty isoforms in the human genome. Activated Rab GTPases interact with effector proteins involved in vesicle formation, transport, tethering, docking and fusion. The specificity of Rab interactions with effectors and regulatory factors plays a central role with respect to the fidelity of membrane trafficking. Rab recognition determinants and the mechanisms underlying interactions with structurally diverse regulatory factors and effector
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Zhuo, Yue. "Solution studies of protein complexes of the endocytic machinery : a dissertation /." San Antonio : UTHSC, 2007. http://proquest.umi.com/pqdweb?did=1310415421&sid=2&Fmt=2&clientId=70986&RQT=309&VName=PQD.

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Dubuke, Michelle L. "The Exocyst Subunit Sec6 Interacts with Assembled Exocytic Snare Complexes: A Dissertation." eScholarship@UMMS, 2015. https://escholarship.umassmed.edu/gsbs_diss/868.

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In eukaryotic cells, membrane-bound vesicles carry cargo between intracellular compartments, to and from the cell surface, and to the extracellular environment. Many conserved families of proteins are required for properly localized vesicle fusion, including the multi-subunit tethering complexes and the SNARE complexes. These protein complexes work together to promote proper vesicle fusion in other trafficking pathways. Contrary to these other pathways, our lab previously suggested that the exocyst subunit Sec6, a component of the exocytosis-specific tethering complex, inhibited Sec9:Sso1 SNAR
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Dubuke, Michelle L. "The Exocyst Subunit Sec6 Interacts with Assembled Exocytic Snare Complexes: A Dissertation." eScholarship@UMMS, 2012. http://escholarship.umassmed.edu/gsbs_diss/868.

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In eukaryotic cells, membrane-bound vesicles carry cargo between intracellular compartments, to and from the cell surface, and to the extracellular environment. Many conserved families of proteins are required for properly localized vesicle fusion, including the multi-subunit tethering complexes and the SNARE complexes. These protein complexes work together to promote proper vesicle fusion in other trafficking pathways. Contrary to these other pathways, our lab previously suggested that the exocyst subunit Sec6, a component of the exocytosis-specific tethering complex, inhibited Sec9:Sso1 SNAR
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Custer, Kenneth Leybourne. "The roles of SV2 and SVOP proteins in regulating neurotransmission /." Thesis, Connect to this title online; UW restricted, 2006. http://hdl.handle.net/1773/10643.

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Brewer, Daniel Niron. "Elucidation of the Role of the Exocyst Subunit Sec6p in Exocytosis: A Dissertation." eScholarship@UMMS, 2009. https://escholarship.umassmed.edu/gsbs_diss/446.

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Trafficking of protein and lipid cargo through the secretory pathway in eukaryotic cells is mediated by membrane-bound vesicles. Secretory vesicles are targeted to sites of exocytosis on the plasma membrane in part by a conserved multi-subunit protein complex termed the exocyst. In addition to tethering vesicles to the plasma membrane, the exocyst complex and components therein may also add a layer of regulation by directly controlling assembly of the SNARE complex, which is required for membrane fusion, as well as other regulatory factors such as Sec1p. In the past, we have shown that Sec6p i
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Georgiev, Alexander. "Membrane Stress and the Role of GYF Domain Proteins." Doctoral thesis, Stockholm : Department of Biochemistry and Biophysics, Stockholm university, 2008. http://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-7764.

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Furgason, Melonnie Lynn Marie. "VPS45p as a Model System for Elucidation of SEC1/MUNC18 Protein Function: A Dissertation." eScholarship@UMMS, 2008. https://escholarship.umassmed.edu/gsbs_diss/425.

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Vesicular trafficking, the movement of vesicles between organelles and the plasma membrane for secretion, consists of multiple highly regulated processes. Many protein families function as specificity and regulatory determinants to ensure correct vesicle targeting and timing of trafficking events. The SNARE proteins dock and fuse vesicles to their target membranes. Sec1/Munc18 (SM) proteins regulate membrane fusion through interactions with the SNAREs—SM proteins have been shown to act as both inhibitors and stimulators of SNARE assembly and membrane fusion. However, the details of these SM pr
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Bücher zum Thema "Vesicular transport proteins"

1

Miao-Kun, Sun, ed. Cognitive sciences research progress. Nova Science Publishers, 2009.

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Buchteile zum Thema "Vesicular transport proteins"

1

Harter, C. L., and F. T. Wieland. "Non-clathrin coat proteins in biosynthetic vesicular protein transport." In Biochemistry of Cell Membranes. Birkhäuser Basel, 1995. http://dx.doi.org/10.1007/978-3-0348-9057-1_7.

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Adolf, Frank, and Felix T. Wieland. "Small G Proteins: Arf Family GTPases in Vesicular Transport." In Ras Superfamily Small G Proteins: Biology and Mechanisms 2. Springer International Publishing, 2014. http://dx.doi.org/10.1007/978-3-319-07761-1_9.

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3

Iaea, David B., Shu Mao, and Frederick R. Maxfield. "Steroidogenic Acute Regulatory Protein-related Lipid Transfer (START) Proteins in Non-vesicular Cholesterol Transport." In Cholesterol Transporters of the START Domain Protein Family in Health and Disease. Springer New York, 2014. http://dx.doi.org/10.1007/978-1-4939-1112-7_8.

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Buxbaum, Engelbert. "Vesicular Transport in Eukaryotic Cells." In Fundamentals of Protein Structure and Function. Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-19920-7_17.

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Balch, W. E., H. Plutner, R. Schwaninger, et al. "G Protein Regulation of Vesicular Transport Through the Exocytic Pathway." In Molecular Mechanisms of Membrane Traffic. Springer Berlin Heidelberg, 1993. http://dx.doi.org/10.1007/978-3-662-02928-2_3.

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Novick, Peter, Patrick Brennwald, Michelle D. Garrett, Mary Moya, Denise Roberts, and Robert Bowser. "The Nucleotide Cycle of SEC4 is Important for its Function in Vesicular Transport." In Protein Synthesis and Targeting in Yeast. Springer Berlin Heidelberg, 1993. http://dx.doi.org/10.1007/978-3-642-84921-3_30.

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Duden, R., B. Storrie, R. Pepperkok, et al. "β-COP, a Coat Protein of Nonclathrin-Coated Vesicles of the Golgi Complex, is Involved in Transport of Vesicular Stomatitis Virus Glycoprotein." In Molecular Mechanisms of Membrane Traffic. Springer Berlin Heidelberg, 1993. http://dx.doi.org/10.1007/978-3-662-02928-2_26.

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Cevher-Keskin, Birsen. "Endomembrane Trafficking in Plants." In Electrodialysis. IntechOpen, 2020. http://dx.doi.org/10.5772/intechopen.91642.

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The functional organization of eukaryotic cells requires the exchange of proteins, lipids, and polysaccharides between membrane compartments through transport intermediates. Small GTPases largely control membrane traffic, which is essential for the survival of all eukaryotes. Transport from one compartment of this pathway to another is mediated by vesicular carriers, which are formed by the controlled assembly of coat protein complexes (COPs) on donor organelles. The activation of small GTPases is essential for vesicle formation from a donor membrane. In eukaryotic cells, small GTP-binding proteins comprise the largest family of signaling proteins. The ADP-ribosylation factor 1 (ARF1) and secretion-associated RAS superfamily 1 (SAR1) GTP-binding proteins are involved in the formation and budding of vesicles throughout plant endomembrane systems. ARF1 has been shown to play a critical role in coat protein complex I (COPI)-mediated retrograde trafficking in eukaryotic systems, whereas SAR1 GTPases are involved in intracellular coat protein complex II (COPII)-mediated protein trafficking from the endoplasmic reticulum (ER) to the Golgi apparatus. The dysfunction of the endomembrane system can affect signal transduction, plant development, and defense. This chapter offers a summary of membrane trafficking system with an emphasis on the role of GTPases especially ARF1, SAR1, and RAB, their regulatory proteins, and interaction with endomembrane compartments. The vacuolar and endocytic trafficking are presented to enhance our understanding of plant development and immunity in plants.
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Walters, Julian R. F. "EFFECTS OF Ca-BINDING PROTEINS ON VESICULAR Ca TRANSPORT BY RAT INTESTINAL BASOLATERAL MEMBRANES." In Calcium-Binding Proteins in Health and Disease. Elsevier, 1987. http://dx.doi.org/10.1016/b978-0-12-521040-9.50026-7.

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Benarroch, Eduardo E. "Vesicular Trafficking." In Neuroscience for Clinicians, edited by Eduardo E. Benarroch. Oxford University Press, 2021. http://dx.doi.org/10.1093/med/9780190948894.003.0007.

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Normal cell function depends on the appropriate synthesis, maturation, sorting, and delivery of fully processed proteins and other macromolecules to specific intracellular compartments; uptake of material from the cell exterior; and regulated intracellular processing and degradation of proteins, lipids, complex carbohydrates, abnormal aggregates, and senescent organelles. These fundamental functions involve secretory, endocytic, and autophagic pathways. The secretory pathway is responsible for protein maturation, sorting, and delivery of transmembrane and secreted proteins from their site of synthesis to their final destinations. Synaptic vesicle exocytosis is a special form of secretion that allows rapid communication between neurons. The endocytic pathway starts with the internalization of material via endosomes. Endosomal content can be transported back to the cell body, recycled to cell compartments, or delivered for degradation by the lysosome. Abnormal protein aggregates or damaged organelles undergo autophagy, which involves formation of an autophagosome and degradation by the lysosome. Impaired vesicular trafficking is a fundamental mechanism in a large number of neurodegenerative disorders, including hereditary spastic paraplegia, lower motor neuron syndromes, and Parkinson disease.
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