Relevant bibliographies by topics / Desmosomal cadherins

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Academic literature on the topic 'Desmosomal cadherins'

Author: Grafiati
Published: 4 June 2021
Last updated: 9 February 2022

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Journal articles on the topic "Desmosomal cadherins"

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Wahl, J. K., P. A. Sacco, T. M. McGranahan-Sadler, L. M. Sauppe, M. J. Wheelock, and K. R. Johnson. "Plakoglobin domains that define its association with the desmosomal cadherins and the classical cadherins: identification of unique and shared domains." Journal of Cell Science 109, no. 5 (1996): 1143–54. http://dx.doi.org/10.1242/jcs.109.5.1143.

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Two cell-cell junctions, the adherens junction and the desmosome, are prominent in epithelial cells. These junctions are composed of transmembrane cadherins which interact with cytoplasmic proteins that serve to link the cadherin to the cytoskeleton. One component of both adherens junctions and desmosomes is plakoglobin. In the adherens junction plakoglobin interacts with both the classical cadherin and with alpha-catenin. Alpha-catenin in turn interacts with microfilaments. The role plakoglobin plays in the desmosome is not well understood. Plakoglobin interacts with the desmosomal cadherins,
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Kowalczyk, Andrew P., Elayne A. Bornslaeger, Jeffrey E. Borgwardt, et al. "The Amino-terminal Domain of Desmoplakin Binds to Plakoglobin and Clusters Desmosomal Cadherin–Plakoglobin Complexes." Journal of Cell Biology 139, no. 3 (1997): 773–84. http://dx.doi.org/10.1083/jcb.139.3.773.

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The desmosome is a highly organized plasma membrane domain that couples intermediate filaments to the plasma membrane at regions of cell–cell adhesion. Desmosomes contain two classes of cadherins, desmogleins, and desmocollins, that bind to the cytoplasmic protein plakoglobin. Desmoplakin is a desmosomal component that plays a critical role in linking intermediate filament networks to the desmosomal plaque, and the amino-terminal domain of desmoplakin targets desmoplakin to the desmosome. However, the desmosomal protein(s) that bind the amino-terminal domain of desmoplakin have not been identi
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Marcozzi, C., I. D. Burdett, R. S. Buxton, and A. I. Magee. "Coexpression of both types of desmosomal cadherin and plakoglobin confers strong intercellular adhesion." Journal of Cell Science 111, no. 4 (1998): 495–509. http://dx.doi.org/10.1242/jcs.111.4.495.

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Desmosomes are unique intercellular junctions in that they invariably contain two types of transmembrane cadherin molecule, desmocollins and desmogleins. In addition they possess a distinct cytoplasmic plaque structure containing a few major proteins including desmoplakins and the armadillo family member plakoglobin. Desmosomal cadherins are putative cell-cell adhesion molecules and we have tested their adhesive capacity using a transfection approach in mouse L cells. We find that L cells expressing either one or both of the desmosomal cadherins desmocollin 2a or desmoglein 1 display weak cell
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Owen, Gethin R., and David L. Stokes. "Exploring the Nature of Desmosomal Cadherin Associations in 3D." Dermatology Research and Practice 2010 (2010): 1–12. http://dx.doi.org/10.1155/2010/930401.

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Desmosomes are a complex assembly of protein molecules that mediate adhesion between adjacent cells. Desmosome composition is well established and spatial relationships between components have been identified. Intercellular cell-cell adhesion is created by the interaction of extracellular domains of desmosomal cadherins, namely, desmocollins and desmogleins. High-resolution methods have provided insight into the structural interactions between cadherins. However, there is a lack of understanding about the architecture of the intact desmosomes and the physical principles behind their adhesive s
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Sikora, Mateusz, Utz H. Ermel, Anna Seybold, et al. "Desmosome architecture derived from molecular dynamics simulations and cryo-electron tomography." Proceedings of the National Academy of Sciences 117, no. 44 (2020): 27132–40. http://dx.doi.org/10.1073/pnas.2004563117.

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Desmosomes are cell–cell junctions that link tissue cells experiencing intense mechanical stress. Although the structure of the desmosomal cadherins is known, the desmosome architecture—which is essential for mediating numerous functions—remains elusive. Here, we recorded cryo-electron tomograms (cryo-ET) in which individual cadherins can be discerned; they appear variable in shape, spacing, and tilt with respect to the membrane. The resulting sub-tomogram average reaches a resolution of ∼26 Å, limited by the inherent flexibility of desmosomes. To address this challenge typical of dynamic biol
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Tariq, Humera, Jordi Bella, Thomas A. Jowitt, et al. "Cadherin flexibility provides a key difference between desmosomes and adherens junctions." Proceedings of the National Academy of Sciences 112, no. 17 (2015): 5395–400. http://dx.doi.org/10.1073/pnas.1420508112.

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Desmosomes and adherens junctions are intercellular adhesive structures essential for the development and integrity of vertebrate tissue, including the epidermis and heart. Their cell adhesion molecules are cadherins: type 1 cadherins in adherens junctions and desmosomal cadherins in desmosomes. A fundamental difference is that desmosomes have a highly ordered structure in their extracellular region and exhibit calcium-independent hyperadhesion, whereas adherens junctions appear to lack such ordered arrays, and their adhesion is always calcium-dependent. We present here the structure of the en
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Lewis, Jani E., James K. Wahl, Kristin M. Sass, Pamela J. Jensen, Keith R. Johnson, and Margaret J. Wheelock. "Cross-Talk between Adherens Junctions and Desmosomes Depends on Plakoglobin." Journal of Cell Biology 136, no. 4 (1997): 919–34. http://dx.doi.org/10.1083/jcb.136.4.919.

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Squamous epithelial cells have both adherens junctions and desmosomes. The ability of these cells to organize the desmosomal proteins into a functional structure depends upon their ability first to organize an adherens junction. Since the adherens junction and the desmosome are separate structures with different molecular make up, it is not immediately obvious why formation of an adherens junction is a prerequisite for the formation of a desmosome. The adherens junction is composed of a transmembrane classical cadherin (E-cadherin and/or P-cadherin in squamous epithelial cells) linked to eithe
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Nekrasova, Oxana E., Evangeline V. Amargo, William O. Smith, Jing Chen, Geri E. Kreitzer, and Kathleen J. Green. "Desmosomal cadherins utilize distinct kinesins for assembly into desmosomes." Journal of Cell Biology 195, no. 7 (2011): 1185–203. http://dx.doi.org/10.1083/jcb.201106057.

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The desmosomal cadherins, desmogleins (Dsgs) and desmocollins (Dscs), comprise the adhesive core of intercellular junctions known as desmosomes. Although these adhesion molecules are known to be critical for tissue integrity, mechanisms that coordinate their trafficking into intercellular junctions to regulate their proper ratio and distribution are unknown. We demonstrate that Dsg2 and Dsc2 both exhibit microtubule-dependent transport in epithelial cells but use distinct motors to traffic to the plasma membrane. Functional interference with kinesin-1 blocked Dsg2 transport, resulting in the a
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Chitaev, N. A., R. E. Leube, R. B. Troyanovsky, L. G. Eshkind, W. W. Franke, and S. M. Troyanovsky. "The binding of plakoglobin to desmosomal cadherins: patterns of binding sites and topogenic potential." Journal of Cell Biology 133, no. 2 (1996): 359–69. http://dx.doi.org/10.1083/jcb.133.2.359.

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Plakoglobin is the only protein that occurs in the cytoplasmic plaques of all known adhering junctions and has been shown to be crucially involved in the formation and maintenance of desmosomes anchoring intermediate-sized filaments (IFs) by its interaction with the desmosomal cadherins, desmoglein (Dsg), and desmocollin (Dsc). This topogenic importance of plakoglobin is now directly shown in living cells as well as in binding assays in vitro. We show that, in transfected human A-431 carcinoma cells, a chimeric protein combining the vesicle-forming transmembrane glycoprotein synaptophysin, wit
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Garrod, David R., Anita J. Merritt, and Zhuxiang Nie. "Desmosomal cadherins." Current Opinion in Cell Biology 14, no. 5 (2002): 537–45. http://dx.doi.org/10.1016/s0955-0674(02)00366-6.

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Dissertations / Theses on the topic "Desmosomal cadherins"

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McEvoy, Katherina Yasmin. "The role of desmosomal cadherins in colorectal tumourigenesis." Thesis, University of Birmingham, 2012. http://etheses.bham.ac.uk//id/eprint/3466/.

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In cancer, loss of intercellular contact contributes to tumour progression and invasion. Desmosomal cadherins are essential constituents of desmosomes – intercellular junctions that confer significant adhesive strength to epithelial tissues and cardiac muscle. Although changes in desmosomal components have been noted in a variety of cancers previously, this investigation has shown for the first time altered desmocollin expression in colorectal cancer. Real-time PCR and western blotting were used to assess desmocollin expression in a series of colorectal cancer and matched normal tissue samples
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Rimpler, Ute. "Funktionelle Charakterisierung von Desmocollin 2 während der Embryonalentwicklung und im adulten Herzen in der Maus." Doctoral thesis, Humboldt-Universität zu Berlin, Mathematisch-Naturwissenschaftliche Fakultät I, 2014. http://dx.doi.org/10.18452/16878.

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Desmosomen sind hochorganisierte Zell-Zell-Verbindungen. Aufgrund ihrer hohen Adhäsivität sind sie für die mechanische Kopplung und strukturelle Stabilität stark beanspruchter Gewebe von essentieller Bedeutung. Die adhäsive interzelluläre Kernstruktur der Desmosomen wird durch die transmembranen Cadherine des Desmocollin und Desmoglein-Typs gebildet. Deren extrazelluläre Domänen stellen den Kontakt zwischen zwei benachbarten Zellen her. Dsc2 ist neben Dsg2 die prädominante Isoform und wird in allen Desmosomen-bildenden Geweben wie auch dem Herzen exprimiert. Ziel der Arbeit war es, die Rolle
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Cowley, Catherine Mary. "Genetic analysis of the human desmosomal cadherin locus." Thesis, University College London (University of London), 1997. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.264340.

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Scothern, Anthea. "Localization of the cytoplasmic sub-domains of the desmosomal cadherin desmoglein 2." Thesis, University of Manchester, 2008. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.491334.

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Desmosomes are intercellular junctions found in epithelia and some other tissues. Their primary function is strong cell-cell adhesion. They also link the keratin intermediate filament (IF) cytoskeleton between cells and have roles in cell signalling, tissue morphogenesis and wound repair. Desmosomes are disc-like plaques arranged symmetrically on either side of the plasma membranes of adjacent cells. Each plaque consists of an outer dense plaque (ODP), an electron lucent zone and an inner dense plaque (IDP), the site of intermediate filament attachment. The plaques are joined to each other by
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Sahota, Virender Kumar. "Molecular genetic studies of human and mouse cell adhesion genes : the desmosomal cadherin locus on chromosome 18." Thesis, University College London (University of London), 2001. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.246773.

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Silva, Melina Coelho da. "Evolution of desmosomal genes in teleost fish and expression analysis of desmosomal cadherins in the gilthead sea bream (Sparus aurata)." Master's thesis, 2016. http://hdl.handle.net/10400.1/10029.

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Dissertação de mestrado, Biotecnologia, Faculdade de Ciências e Tecnologia, Universidade do Algarve, 2017<br>Fish aquaculture is a viable and profitable industry worldwide and monitoring fish larvae health and growth is a key step. The gilthead sea bream (Sparus aurata) is an economically important species reared mainly under mesocosm and intensive aquaculture systems. However, heterogeneous larvae growth and anatomic deformations are observed using these systems and few molecular markers to monitor fish growth are currently in use. Desmosomes are a type of cell-cell junction formed by a prot
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Heupel, Wolfgang-Moritz Felix. "Role and modulation of cadherins in pathologic processes." Doctoral thesis, 2010. https://nbn-resolving.org/urn:nbn:de:bvb:20-opus-52716.

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Ca2+ dependent cell adhesion molecules (cadherins) are central for a variety of cell and tissue functions such as morphogenesis, epithelial and endothelial barrier formation, synaptic function and cellular signaling. Of paramount importance for cadherin function is their specific extracellular adhesive trans-interaction. Cadherins are embedded in a cellular environment of intracellular and extracellular regulators that modify cadherin binding in response to various physiological and pathological stimuli. Most experimental approaches used for studying cadherin interaction however lack a physiol
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Endlich, Alexander Dominic. "Die Rolle der Dsg3-Depletion in der Pathogenese des Pemphigus vulgaris." Doctoral thesis, 2021. https://doi.org/10.25972/OPUS-22557.

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Pemphigus vulgaris (PV) ist eine blasenbildende Autoimmunerkrankung, die durch Autoantikörper gegen Dsg1 und Dsg3 gekennzeichnet ist. Der genaue Pathomechanismus, der zu einem PV-IgG vermittelten Verlust der interzellulären Adhäsion führt, ist noch unklar. Die Dsg3-Depletion und die Modulation von Signalkaskaden stellen hierbei kennzeichnende Merkmale der Erkrankung dar. Mit den Ergebnissen der vorliegenden Arbeit ist eine bessere Einordnung der Dsg3-Depletion in den pathogenetischen Kontext von Pemphigus vulgaris möglich. Die Experimente zeigen, dass die Dsg3-Depletion von Differenzierungspro
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Books on the topic "Desmosomal cadherins"

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Legan, Paul Kevin. The Desmocollin family of adhesion molecules: Desmosomal cadherins showing tissue and differentiation specific patterns of expression. University of Manchester, 1993.

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Book chapters on the topic "Desmosomal cadherins"

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Chidgey, Martyn, and David Garrod. "Desmosomal Cadherins." In The Cadherin Superfamily. Springer Japan, 2016. http://dx.doi.org/10.1007/978-4-431-56033-3_7.

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"Desmosomal Cadherins." In Encyclopedia of Cancer. Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/978-3-642-16483-5_1585.

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Collins, Jane E. "Classical and desmosomal cadherins." In Advances in Structural Biology. Elsevier, 1996. http://dx.doi.org/10.1016/s1064-6000(96)80006-8.

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Gornowicz-Porowska, Justyna, Monika Bowszyc-Dmochowska, and Marian Dmochowski. "Desmosomal Cadherins in Basal Cell Carcinomas." In Skin Cancer Overview. InTech, 2011. http://dx.doi.org/10.5772/27540.

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Cowin, Pamela, and Sailaja Puttagunta. "Desmosomal Cadherins and Their Interactions with Plakoglobin." In Advances in Molecular and Cell Biology. Elsevier, 1996. http://dx.doi.org/10.1016/s1569-2558(08)60064-8.

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Conference papers on the topic "Desmosomal cadherins"

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Thiess, L., N. Mwewa, P. Schirmacher, and K. Breuhahn. "The desmosomal cadherin desmoglein-2 regulates the Hippo pathway effector yes-associated protein (YAP) in liver cancer." In 36. Jahrestagung der Deutschen Arbeitsgemeinschaft zum Studium der Leber. Georg Thieme Verlag KG, 2020. http://dx.doi.org/10.1055/s-0039-3402211.

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chen, jing, Bhushan V. Desai, Evangeline V. Amargo, Jodi L. Klessner, Dipal M. Patel, and Kathleen J. Green. "Abstract LB-32: The unique region of a desmosomal cadherin, desmoglein 2, regulates internalization via tail-tail interactions." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-lb-32.

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You might also be interested in the extended bibliographies on the topic 'Desmosomal cadherins' for particular source types:
Journal articles
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