Relevant bibliographies by topics / Golgi Apparatu

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
  6. Reports

Academic literature on the topic 'Golgi Apparatu'

Author: Grafiati
Published: 10 March 2023
Last updated: 31 July 2025

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Journal articles on the topic "Golgi Apparatu"

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Bucurica, Sandica, Laura Gaman, Mariana Jinga, Andrei Adrian Popa, and Florentina Ionita-Radu. "Golgi Apparatus Target Proteins in Gastroenterological Cancers: A Comprehensive Review of GOLPH3 and GOLGA Proteins." Cells 12, no. 14 (2023): 1823. http://dx.doi.org/10.3390/cells12141823.

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The Golgi apparatus plays a central role in protein sorting, modification and trafficking within cells; its dysregulation has been implicated in various cancers including those affecting the GI tract. This review highlights two Golgi target proteins, namely GOLPH3 and GOLGA proteins, from this apparatus as they relate to gastroenterological cancers. GOLPH3—a highly conserved protein of the trans-Golgi network—has become a key player in cancer biology. Abnormal expression of GOLPH3 has been detected in various gastrointestinal cancers including gastric, colorectal and pancreatic cancers. GOLPH3
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Diao, Aipo, Dinah Rahman, Darryl J. C. Pappin, John Lucocq, and Martin Lowe. "The coiled-coil membrane protein golgin-84 is a novel rab effector required for Golgi ribbon formation." Journal of Cell Biology 160, no. 2 (2003): 201–12. http://dx.doi.org/10.1083/jcb.200207045.

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Fragmentation of the mammalian Golgi apparatus during mitosis requires the phosphorylation of a specific subset of Golgi-associated proteins. We have used a biochemical approach to characterize these proteins and report here the identification of golgin-84 as a novel mitotic target. Using cryoelectron microscopy we could localize golgin-84 to the cis-Golgi network and found that it is enriched on tubules emanating from the lateral edges of, and often connecting, Golgi stacks. Golgin-84 binds to active rab1 but not cis-Golgi matrix proteins. Overexpression or depletion of golgin-84 results in f
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Short, Benjamin, Christian Preisinger, Roman Körner, Robert Kopajtich, Olwyn Byron, and Francis A. Barr. "A GRASP55-rab2 effector complex linking Golgi structure to membrane traffic." Journal of Cell Biology 155, no. 6 (2001): 877–84. http://dx.doi.org/10.1083/jcb.200108079.

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Membrane traffic between the endoplasmic reticulum (ER) and Golgi apparatus and through the Golgi apparatus is a highly regulated process controlled by members of the rab GTPase family. The GTP form of rab1 regulates ER to Golgi transport by interaction with the vesicle tethering factor p115 and the cis-Golgi matrix protein GM130, also part of a complex with GRASP65 important for the organization of cis-Golgi cisternae. Here, we find that a novel coiled-coil protein golgin-45 interacts with the medial-Golgi matrix protein GRASP55 and the GTP form of rab2 but not other Golgi rab proteins. Deple
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Añel, Alberto Marcelo Diaz, та Vivek Malhotra. "Correction: PKCη is required for β1γ2/β3γ2- and PKD-mediated transport to the cell surface and the organization of the Golgi apparatu". Journal of Cell Biology 169, № 3 (2005): 539–40. http://dx.doi.org/10.1083/jcb.200412089042805c.

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Jiang, Shu, Sung W. Rhee, Paul A. Gleeson, and Brian Storrie. "Capacity of the Golgi Apparatus for Cargo Transport Prior to Complete Assembly." Molecular Biology of the Cell 17, no. 9 (2006): 4105–17. http://dx.doi.org/10.1091/mbc.e05-12-1112.

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In yeast, particular emphasis has been given to endoplasmic reticulum (ER)-derived, cisternal maturation models of Golgi assembly while in mammalian cells more emphasis has been given to golgins as a potentially stable assembly framework. In the case of de novo Golgi formation from the ER after brefeldin A/H89 washout in HeLa cells, we found that scattered, golgin-enriched, structures formed early and contained golgins including giantin, ranging across the entire cis to trans spectrum of the Golgi apparatus. These structures were incompetent in VSV-G cargo transport. Second, we compared Golgi
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Yadav, Smita, Sapna Puri, and Adam D. Linstedt. "A Primary Role for Golgi Positioning in Directed Secretion, Cell Polarity, and Wound Healing." Molecular Biology of the Cell 20, no. 6 (2009): 1728–36. http://dx.doi.org/10.1091/mbc.e08-10-1077.

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Peri-centrosomal positioning of the mammalian Golgi apparatus is known to involve microtubule-based motility, but its importance for cellular physiology is a major unanswered question. Here, we identify golgin-160 and GMAP210 as proteins required for centripetal motility of Golgi membranes. In the absence of either golgin, peri-centrosomal positioning of the Golgi apparatus was disrupted while the cytoskeleton remained intact. Although secretion persisted with normal kinetics, it was evenly distributed in response to wounding rather than directed to the wound edge. Strikingly, these cells also
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Sato, Keisuke, Peristera Roboti, Alexander A. Mironov, and Martin Lowe. "Coupling of vesicle tethering and Rab binding is required for in vivo functionality of the golgin GMAP-210." Molecular Biology of the Cell 26, no. 3 (2015): 537–53. http://dx.doi.org/10.1091/mbc.e14-10-1450.

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Golgins are extended coiled-coil proteins believed to participate in membrane-tethering events at the Golgi apparatus. However, the importance of golgin-mediated tethering remains poorly defined, and alternative functions for golgins have been proposed. Moreover, although golgins bind to Rab GTPases, the functional significance of Rab binding has yet to be determined. In this study, we show that depletion of the golgin GMAP-210 causes a loss of Golgi cisternae and accumulation of numerous vesicles. GMAP-210 function in vivo is dependent upon its ability to tether membranes, which is mediated e
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Lu, Lei, Guihua Tai, and Wanjin Hong. "Autoantigen Golgin-97, an Effector of Arl1 GTPase, Participates in Traffic from the Endosome to the Trans-Golgi Network." Molecular Biology of the Cell 15, no. 10 (2004): 4426–43. http://dx.doi.org/10.1091/mbc.e03-12-0872.

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The precise cellular function of Arl1 and its effectors, the GRIP domain Golgins, is not resolved, despite our recent understanding that Arl1 regulates the membrane recruitment of these Golgins. In this report, we describe our functional study of Golgin-97. Using a Shiga toxin B fragment (STxB)-based in vitro transport assay, we demonstrated that Golgin-97 plays a role in transport from the endosome to the trans-Golgi network (TGN). The recombinant GRIP domain of Golgin-97 as well as antibodies against Golgin-97 inhibited the transport of STxB in vitro. Membrane-associated Golgin-97, but not i
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Liu, Chunyi, Mei Mei, Qiuling Li, et al. "Loss of the golgin GM130 causes Golgi disruption, Purkinje neuron loss, and ataxia in mice." Proceedings of the National Academy of Sciences 114, no. 2 (2016): 346–51. http://dx.doi.org/10.1073/pnas.1608576114.

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The Golgi apparatus lies at the heart of the secretory pathway where it is required for secretory trafficking and cargo modification. Disruption of Golgi architecture and function has been widely observed in neurodegenerative disease, but whether Golgi dysfunction is causal with regard to the neurodegenerative process, or is simply a manifestation of neuronal death, remains unclear. Here we report that targeted loss of the golgin GM130 leads to a profound neurological phenotype in mice. Global KO of mouse GM130 results in developmental delay, severe ataxia, and postnatal death. We further show
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Munro, S. "The Golgin Coiled-Coil Proteins of the Golgi Apparatus." Cold Spring Harbor Perspectives in Biology 3, no. 6 (2011): a005256. http://dx.doi.org/10.1101/cshperspect.a005256.

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Dissertations / Theses on the topic "Golgi Apparatu"

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D, Nolfi. "Studio morfologico e funzionale dell’apparato di Golgi in relazione ad una struttura LTL-positiva nelle cellule di carcinoma prostatico DU145." Doctoral thesis, Università di Siena, 2020. http://hdl.handle.net/11365/1095701.

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The Golgi apparatus is a complex structure present in all eukaryotic cells. This organelle, which was first observed in 1989, still represents a fascinating enigma for much of its structural and functional peculiarity. Generally, the Golgi apparatus is known as the heart of the secretory pathway and glycosylation, which is one of the major post-traductional modifications. Most of the reactions of the glycosylation pathway occur in the Golgi apparatus, where glycosyltransferases and glycosidases modify glucidic chains by adding or removing monosaccharides. All the steps follow a precise seque
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Wong, Mei Wai Mie. "Functions of the golgin coiled-coil proteins of the Golgi apparatus." Thesis, University of Cambridge, 2014. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.708308.

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Au, Catherine. "Organellar proteomics of the Golgi apparatus and Golgi derived COPI vesicles." Thesis, McGill University, 2008. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=18742.

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Studying an organelle with traditional biochemistry, histology, or microscopy techniques allows the determination of the presence of up to three proteins simultaneously. Mass spectrometry based proteomics has changed the study of organelles; for the first time it is possible to investigate the whole protein complement of a subcellular compartment. In this work I demonstrate our ability to use redundant peptide counting as a quantitative technique to compare the relative abundance of different proteins in a complex sample, specifically, enriched organellar preparations. I present the pipelin
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Dworkin, Joel. "Cell-free reconstitution of the Golgi apparatus." Thesis, McGill University, 1989. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=59884.

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The Golgi apparatus is organized into a characteristic differentiated stack in all eukaryotic cells. During mitosis, the Golgi apparatus disassembles into smaller clustered vesicles lacking recognizable cisternae whereupon they recombine to form typical stacks in each of the daughter cells (Lucocq et al., 1987). Paiment et al. (1989) have demonstrated that dispersed (unstacked) Golgi fragments will reconstitute into a functional stacked Golgi apparatus when microinjected into Xenopus laevis oocytes. Disrupted hepatic Golgi fractions (Gi) were isolated on discontinuous sucrose gradients and inc
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Hui, Hu. "Targeting and retention in the Golgi apparatus." Thesis, University College London (University of London), 1997. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.263648.

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Radau, Boris. "Die Regulation der Vesikelbildung am trans-Golgi-Netzwerk durch Proteinkinase C." [S.l.] : [s.n.], 2001. http://www.diss.fu-berlin.de/2001/89/index.html.

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Li, Xue-Yi. "Characterization of a novel GPI-anchored protein, a component of sphingomyelin enriched microdomains at the Golgi complex." [S.l. : s.n.], 2003. http://deposit.ddb.de/cgi-bin/dokserv?idn=967973775.

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Rivinoja, A. (Antti). "Golgi pH and glycosylation." Doctoral thesis, University of Oulu, 2009. http://urn.fi/urn:isbn:9789514292699.

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Abstract Glycans, as a part of glycoproteins, glycolipids and other glycoconjugates, are involved in many vital intra- and inter-cellular tasks, such as protein folding and sorting, protein quality control, vesicular trafficking, cell signalling, immunological defence, cell motility and adhesion. Therefore, their correct construction is crucial for the normal functioning of eukaryotic cells and organisms they form. Most cellular glycans are constructed in the Golgi, and abnormalities in their structure may derive, for instance, from alkalinization of the Golgi lumen. In this work we show th
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Gilchrist, Annalyn. "Proteomics analysis of the endoplasmic reticulum and Golgi apparatus." Thesis, McGill University, 2008. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=18715.

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Isolated rough and smooth microsomes of the endoplasmic reticulum and isolated Golgi apparatus from rat liver were analyzed by proteomics using mass spectrometry, identifying 1064 proteins among the three fractions. An additional 598 proteins were identified by biochemically subfractionating the rough and smooth microsomes by treatment with a high salt wash and the detergent Triton-X 114. Proteins were quantified by redundant peptide counts which enabled an assessment of the extent of cross-contamination between the endoplasmic reticulum and Golgi fractions and other organellar contaminatio
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Rocchetti, Alessandra. "Interactions between the plant Golgi apparatus and the cytoskeleton." Thesis, Oxford Brookes University, 2016. https://radar.brookes.ac.uk/radar/items/e035b419-1acc-4031-aadd-2cfc1f9ed3c8/1/.

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In animal cells, the relationship between the Golgi apparatus and cytoskeleton has been well characterised but not much is known in plants. The functions of the Golgi apparatus are conserved amongst eukaryotes. It is one of the main stations in the secretory pathway and is involved in protein processing and sorting to different destinations. In plants, it is also involved in trafficking and positioning of cell wall components. In tobacco epidermal cells, fluorescent labelling with Golgi marker proteins has shown that the Golgi apparatus is made of hundreds of individual units scattered in the
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Books on the topic "Golgi Apparatu"

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Mironov, Alexander A., and Margit Pavelka, eds. The Golgi Apparatus. Springer Vienna, 2008. http://dx.doi.org/10.1007/978-3-211-76310-0.

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Berger, E. G., and J. Roth, eds. The Golgi Apparatus. Birkhäuser Basel, 1997. http://dx.doi.org/10.1007/978-3-0348-8876-9.

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Morré, D. James, and Hilton H. Mollenhauer, eds. The Golgi Apparatus. Springer New York, 2009. http://dx.doi.org/10.1007/978-0-387-74347-9.

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G, Berger Eric, and Roth, J. (Jürgen), Prof. Dr. Dr., eds. The Golgi apparatus. Birkhäuser Verlag, 1997.

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Kloc, Malgorzata, ed. The Golgi Apparatus and Centriole. Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-030-23173-6.

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Pavelka, Margit. Functional Morphology of the Golgi Apparatus. Springer Berlin Heidelberg, 1987. http://dx.doi.org/10.1007/978-3-642-72826-6.

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Hawkins, Christopher J. Golgi apparatus: Structure, functions and mechanisms. Nova Science Publishers, 2010.

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H, Mollenhauer Hilton, ed. The Golgi apparatus: The first 100 years. Springer, 2009.

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G, Robinson David, ed. The Golgi apparatus and the plant secretory pathway. Sheffield Academic Press, 2003.

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Valverde, Facundo. Golgi atlas of the postnatal mouse brain. Springer-Verlag, 1998.

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Book chapters on the topic "Golgi Apparatu"

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Sato, Keisuke, and Martin Lowe. "Golgi Apparatus." In Molecular Life Sciences. Springer New York, 2014. http://dx.doi.org/10.1007/978-1-4614-6436-5_189-2.

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Gooch, Jan W. "Golgi Apparatus." In Encyclopedic Dictionary of Polymers. Springer New York, 2011. http://dx.doi.org/10.1007/978-1-4419-6247-8_13851.

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Sato, Keisuke, and Martin Lowe. "Golgi Apparatus." In Molecular Life Sciences. Springer New York, 2018. http://dx.doi.org/10.1007/978-1-4614-1531-2_189.

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Berkaloff, André, Jacques Bourguet, Pierre Favard, Nina Favard, and Jean-Claude Lacroix. "Golgi-Apparat." In Die Zelle. Vieweg+Teubner Verlag, 1990. http://dx.doi.org/10.1007/978-3-663-06822-8_7.

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Bährle-Rapp, Marina. "Golgi-Apparat." In Springer Lexikon Kosmetik und Körperpflege. Springer Berlin Heidelberg, 2007. http://dx.doi.org/10.1007/978-3-540-71095-0_4463.

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Berger, E. G. "The Golgi apparatus: From discovery to contemporary studies." In The Golgi Apparatus. Birkhäuser Basel, 1997. http://dx.doi.org/10.1007/978-3-0348-8876-9_1.

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Driouich, A., and L. A. Staehelin. "The plant Golgi apparatus: Structural organization and functional properties." In The Golgi Apparatus. Birkhäuser Basel, 1997. http://dx.doi.org/10.1007/978-3-0348-8876-9_10.

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Rambourg, A., and Y. Clermont. "Three-dimensional structure of the Golgi apparatus in mammalian cells." In The Golgi Apparatus. Birkhäuser Basel, 1997. http://dx.doi.org/10.1007/978-3-0348-8876-9_2.

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Farquhar, M. G., and H. P. Hauri. "Protein sorting and vesicular traffic in the Golgi apparatus." In The Golgi Apparatus. Birkhäuser Basel, 1997. http://dx.doi.org/10.1007/978-3-0348-8876-9_3.

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Roth, J. "Topology of glycosylation in the Golgi apparatus." In The Golgi Apparatus. Birkhäuser Basel, 1997. http://dx.doi.org/10.1007/978-3-0348-8876-9_4.

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Conference papers on the topic "Golgi Apparatu"

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Bones, Eva, and Matija Marolt. "Automatic Segmentation of the Golgi Apparatus in Volumetric Data with Approximate Labels." In 2021 15th International Conference on Advanced Technologies, Systems and Services in Telecommunications (TELSIKS). IEEE, 2021. http://dx.doi.org/10.1109/telsiks52058.2021.9606279.

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Sheshukova, E. V., N. M. Ershova, A. A. Antimonova, K. A. Kamarova, and T. V. Komarova. "NICOTIANA BENTHAMIANA XYLOGLUCAN ENDOTRANSGLUCOSYLASE/HYDROLASE NBXTH19 CONTAINS ASN-LINKED GLYCAN AND PARTICIPATES IN RESPONSE TO VIRAL INFECTION." In XI МЕЖДУНАРОДНАЯ КОНФЕРЕНЦИЯ МОЛОДЫХ УЧЕНЫХ: БИОИНФОРМАТИКОВ, БИОТЕХНОЛОГОВ, БИОФИЗИКОВ, ВИРУСОЛОГОВ, МОЛЕКУЛЯРНЫХ БИОЛОГОВ И СПЕЦИАЛИСТОВ ФУНДАМЕНТАЛЬНОЙ МЕДИЦИНЫ. IPC NSU, 2024. https://doi.org/10.25205/978-5-4437-1691-6-282.

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Many cellular proteins involved in plant responses to viral infections are glycoproteins, which are secreted via the endoplasmic reticulum and Golgi apparatus where they undergo glycosylation. Additionally, the presence of N-linked glycans is crucial for their function. In this study, the NbXTH19 protein was examined, and an N-glycosylation site within it was experimentally confirmed.
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Urbanowicz, Breeanna R., Catherine Rayon, Marco A. Tine, Marcos S. Buckeridge, and Nicholas C. Carpita. "CHARACTERIZATION OF THE (1-->3),(1-->4)BETA-D-GLUCAN SYNTHASE AT THE GOLGI APPARATUS OF MAIZE." In XXIst International Carbohydrate Symposium 2002. TheScientificWorld Ltd, 2002. http://dx.doi.org/10.1100/tsw.2002.414.

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Gómez, Daniel Joseph. "Untangling the Microscopic World of Organelles, Cells, Tissues, and Organs: A Focus on the Dysfunctional Golgi Apparatus in Disease Research." In Cells 2023. MDPI, 2023. http://dx.doi.org/10.3390/blsf2023021015.

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Sinha, S., and D. D. Wagner. "INTACT MICROTUBULES ARE NECESSARY FOR COMPLETE PROCESSING, STORAGE AND REGULATED SECRETION OF VON WILLEBRAND FACTOR BY ENDOTHELIAL CELLS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642914.

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The importance of intact microtubules in the processing, storage and regulated secretion of von Willebrand factor (vWf) from Weibel-Palade bodies in endothelial cells was investigated. Human umbilical vein endothelial cells treated for one hour with colchicine (10-6M) or nocodozole (10-6M) lost their organized microtubular network. Stimulation of these cells with secretagogues (A23187, thrombin) produced only 30% release of vWf in comparison to control cells containing intact microtubules. The nocodazole treatment was reversible. One hour incubation in the absence of the drug was sufficient fo
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Reports on the topic "Golgi Apparatu"

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Nelson, Nathan, and Randy Schekman. Functional Biogenesis of V-ATPase in the Vacuolar System of Plants and Fungi. United States Department of Agriculture, 1996. http://dx.doi.org/10.32747/1996.7574342.bard.

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The vacuolar H+-ATPase (V-ATPase) is one of the most fundamental enzymes in nature. It pumps protons into the vacuolar system of eukaryotic cells and provides the energy for numerous transport systems. Through our BARD grant we discovered a novel family of membrane chaperones that modulate the amount of membrane proteins. We also elucidated the mechanism by which assembly factors guide the membrane sector of V-ATPase from the endoplasmic reticulum to the Golgi apparatus. The major goal of the research was to understand the mechanism of action and biogenesis of V-ATPase in higher plants and fun
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