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Journal articles on the topic 'Extracellular matrix'

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Published: 4 June 2021
Last updated: 29 July 2024

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1

TANZER, M. L. "Extracellular Matrix: Extracellular Matrix Biochemty." Science 227, no. 4684 (January 18, 1985): 289–90. http://dx.doi.org/10.1126/science.227.4684.289-a.

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2

B, Saberi. "Glioma and Extracellular Matrix, A Review on the Integrins as the Receptors of the Extracellular Matrix." Bioequivalence & Bioavailability International Journal 7, no. 1 (January 4, 2023): 1–2. http://dx.doi.org/10.23880/beba-16000190.

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The brain extracellular matrix is a complex structure. The invading tumors like gliomas would interact with the extracellular matrix. There are receptors in the extracellular matrix including Integrins. This brief review tries to point to some important notes about the extracellular matrix and Integrins as a group of receptors in the extracellular matrix which can play the important role in the pathogenesis of gliomas in the brain tissue
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3

Labat-Robert, J., M. Bihari-Varga, and L. Robert. "Extracellular matrix." FEBS Letters 268, no. 2 (August 1, 1990): 386–93. http://dx.doi.org/10.1016/0014-5793(90)81291-u.

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4

Bernfield, M. "Extracellular matrix." Current Opinion in Cell Biology 1, no. 5 (October 1989): 953–55. http://dx.doi.org/10.1016/0955-0674(89)90064-1.

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5

McDonald, John A. "Extracellular Matrix Assembly." Annual Review of Cell Biology 4, no. 1 (November 1988): 183–207. http://dx.doi.org/10.1146/annurev.cb.04.110188.001151.

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6

Fessler, J. H., and L. I. Fessler. "Drosophila Extracellular Matrix." Annual Review of Cell Biology 5, no. 1 (November 1989): 309–39. http://dx.doi.org/10.1146/annurev.cb.05.110189.001521.

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7

Ruoslahti, Erkki. "Brain extracellular matrix." Glycobiology 6, no. 5 (1996): 489–92. http://dx.doi.org/10.1093/glycob/6.5.489.

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8

Rienks, Marieke, Anna-Pia Papageorgiou, Nikolaos G. Frangogiannis, and Stephane Heymans. "Myocardial Extracellular Matrix." Circulation Research 114, no. 5 (February 28, 2014): 872–88. http://dx.doi.org/10.1161/circresaha.114.302533.

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9

Mueller, Andrea R., Klaus-Peter Platz, Cordula Heckert, Michaela H??usler, Olaf Guckelberger, Detlef Schuppan, Hartmut Lobeck, and Peter Neuhaus. "THE EXTRACELLULAR MATRIX." Transplantation 65, no. 6 (March 1998): 770–76. http://dx.doi.org/10.1097/00007890-199803270-00002.

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10

Aplin, J. D., L. J. Foden, and A. K. Charlton. "Decidual extracellular matrix." Placenta 7, no. 5 (September 1986): 458. http://dx.doi.org/10.1016/s0143-4004(86)80062-5.

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11

Tayebjee, Muzahir H., Robert J. MacFadyen, and Gregory YH Lip. "Extracellular matrix biology." Journal of Hypertension 21, no. 12 (December 2003): 2211–18. http://dx.doi.org/10.1097/00004872-200312000-00002.

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12

Rennard, Stephen I. "5. Extracellular Matrix." American Journal of Respiratory and Critical Care Medicine 153, no. 6_pt_2 (June 1996): S14—S15. http://dx.doi.org/10.1164/ajrccm/153.6_pt_2.s14.

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13

Davis, George E., and Donald R. Senger. "Endothelial Extracellular Matrix." Circulation Research 97, no. 11 (November 25, 2005): 1093–107. http://dx.doi.org/10.1161/01.res.0000191547.64391.e3.

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14

Lyaruu, Don. "Enamel extracellular matrix." European Journal of Oral Sciences 119 (December 2011): 307. http://dx.doi.org/10.1111/j.1600-0722.2011.00932.x.

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15

Theocharis, Achilleas D., Spyros S. Skandalis, Chrysostomi Gialeli, and Nikos K. Karamanos. "Extracellular matrix structure." Advanced Drug Delivery Reviews 97 (February 2016): 4–27. http://dx.doi.org/10.1016/j.addr.2015.11.001.

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16

Har‐El, Ronit, and Marvin L. Tanzer. "Extracellular Matrix 3: Evolution of the extracellular matrix in invertebrates." FASEB Journal 7, no. 12 (September 1993): 1115–23. http://dx.doi.org/10.1096/fasebj.7.12.8375610.

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17

Werb, Zena, Patrice Tremble, Zena Werb, Caroline H. Damsky, Patrice Tremble, and Caroline H. Damsky. "Regulation of extracellular matrix degradation by cell—extracellular matrix interactions." Cell Differentiation and Development 32, no. 3 (December 1990): 299–306. http://dx.doi.org/10.1016/0922-3371(90)90043-v.

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18

Mathivanan, Suresh. "Extracellular Matrix and the Extracellular Environment." PROTEOMICS 17, no. 23-24 (December 2017): 7700185. http://dx.doi.org/10.1002/pmic.2017700185.

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19

Vizovišek, Matej, Marko Fonović, and Boris Turk. "Cysteine cathepsins in extracellular matrix remodeling: Extracellular matrix degradation and beyond." Matrix Biology 75-76 (January 2019): 141–59. http://dx.doi.org/10.1016/j.matbio.2018.01.024.

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20

WANG, Ke-Yong, Akihide TANIMOTO, and Yasuyuki SASAGURI. "Extracellular Matrix and Atherosclerosis." Journal of UOEH 32, no. 2 (2010): 195–203. http://dx.doi.org/10.7888/juoeh.32.195.

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21

Kirmse, Robert, Hannes Otto, and Thomas Ludwig. "The extracellular matrix remodeled." Communicative & Integrative Biology 5, no. 1 (January 2012): 71–73. http://dx.doi.org/10.4161/cib.17342.

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22

Katsuda, Shogo, and Toshiyuki Kaji. "Atherosclerosis and Extracellular Matrix." Journal of Atherosclerosis and Thrombosis 10, no. 5 (2003): 267–74. http://dx.doi.org/10.5551/jat.10.267.

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23

Doyle, Andrew D., Shayan S. Nazari, and Kenneth M. Yamada. "Cell–extracellular matrix dynamics." Physical Biology 19, no. 2 (January 12, 2022): 021002. http://dx.doi.org/10.1088/1478-3975/ac4390.

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Abstract The sites of interaction between a cell and its surrounding microenvironment serve as dynamic signaling hubs that regulate cellular adaptations during developmental processes, immune functions, wound healing, cell migration, cancer invasion and metastasis, as well as in many other disease states. For most cell types, these interactions are established by integrin receptors binding directly to extracellular matrix proteins, such as the numerous collagens or fibronectin. For the cell, these points of contact provide vital cues by sampling environmental conditions, both chemical and physical. The overall regulation of this dynamic interaction involves both extracellular and intracellular components and can be highly variable. In this review, we highlight recent advances and hypotheses about the mechanisms and regulation of cell–ECM interactions, from the molecular to the tissue level, with a particular focus on cell migration. We then explore how cancer cell invasion and metastasis are deeply rooted in altered regulation of this vital interaction.
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24

UTANI, ATSUSHI. "The extracellular matrix (1)." Nishi Nihon Hifuka 61, no. 1 (1999): 79–83. http://dx.doi.org/10.2336/nishinihonhifu.61.79.

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25

Andrade, Zilton A. "Extracellular matrix and schistosomiasis." Memórias do Instituto Oswaldo Cruz 86, suppl 3 (1991): 61–73. http://dx.doi.org/10.1590/s0074-02761991000700010.

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26

Shin, Kwanwoo. "Understanding the extracellular matrix." Journal of Periodontal & Implant Science 43, no. 3 (2013): 109. http://dx.doi.org/10.5051/jpis.2013.43.3.109.

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27

Okazaki, Ken, and Linda J. Sandell. "Extracellular Matrix Gene Regulation." Clinical Orthopaedics and Related Research 427 (October 2004): S123—S128. http://dx.doi.org/10.1097/01.blo.0000144478.51284.f3.

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28

Shaub, Amy. "Unravelling the extracellular matrix." Nature Cell Biology 1, no. 7 (November 1999): E173—E174. http://dx.doi.org/10.1038/15608.

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29

Spinale, Francis G. "The extracellular matrix: Summation." Journal of Cardiac Failure 8, no. 6 (December 2002): S349—S350. http://dx.doi.org/10.1054/jcaf.2002.129257.

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30

Offiah, Ifeoma, Athanasios Didangelos, Barry A. OʼReilly, and Stephen B. McMahon. "Manipulating the extracellular matrix." PAIN 158, no. 1 (January 2017): 161–70. http://dx.doi.org/10.1097/j.pain.0000000000000749.

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31

Connolly, Jon H., and Graeme Berlyn. "The plant extracellular matrix." Canadian Journal of Botany 74, no. 10 (October 1, 1996): 1545–46. http://dx.doi.org/10.1139/b96-186.

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32

Kadler, Karl E. "Extracellular matrix (ECM) research." Methods 45, no. 1 (May 2008): 1. http://dx.doi.org/10.1016/j.ymeth.2008.04.001.

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33

F.G. "The dynamic extracellular matrix." Human Pathology 19, no. 7 (July 1988): 751–52. http://dx.doi.org/10.1016/s0046-8177(88)80256-9.

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34

Arias, J. L., and M. S. Fernández. "Extracellular Matrix and Biomineralization." Microscopy and Microanalysis 9, S02 (August 2003): 1516–17. http://dx.doi.org/10.1017/s1431927603447582.

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35

McCann, MC, B. Penning, A. Olek, and NC Carpita. "The Plant Extracellular Matrix." Microscopy and Microanalysis 14, S2 (August 2008): 1488–89. http://dx.doi.org/10.1017/s1431927608088843.

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36

Mosher, Deane F., Jane Sottile, Chuanyue Wu, and John A. McDonald. "Assembly of extracellular matrix." Current Biology 2, no. 12 (December 1992): 672. http://dx.doi.org/10.1016/0960-9822(92)90138-z.

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37

Roberts, K. "The plant extracellular matrix." Current Opinion in Cell Biology 1, no. 5 (October 1989): 1020–27. http://dx.doi.org/10.1016/0955-0674(89)90074-4.

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38

Mosher, Deane F., Jane Sottile, Chuanyue Wu, and John A. McDonald. "Assembly of extracellular matrix." Current Opinion in Cell Biology 4, no. 5 (October 1992): 810–18. http://dx.doi.org/10.1016/0955-0674(92)90104-k.

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39

Gullberg, Donald. "The extracellular matrix catalogued." Trends in Cell Biology 6, no. 11 (November 1996): 449–50. http://dx.doi.org/10.1016/0962-8924(96)88897-0.

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40

Birk, D. E. "Corneal extracellular matrix assembly." Experimental Eye Research 55 (September 1992): 34. http://dx.doi.org/10.1016/0014-4835(92)90325-m.

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41

Flinn, Barry S. "Plant extracellular matrix metalloproteinases." Functional Plant Biology 35, no. 12 (2008): 1183. http://dx.doi.org/10.1071/fp08182.

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The plant extracellular matrix (ECM) includes a variety of proteins with critical roles in the regulation of plant growth, development, and responses to pests and pathogens. Several studies have shown that various ECM proteins undergo proteolytic modification. In mammals, the extracellular matrix metalloproteinases (MMPs) are known modifiers of the ECM, implicated in tissue architecture changes and the release of biologically active and/or signalling molecules. Although plant MMPs have been identified, little is known about their activity and function. Plant MMPs show structural similarity to mammalian MMPs, including the presence of an auto-regulatory cysteine switch domain and a zinc-binding catalytic domain. Plant MMPs are differentially expressed in cells and tissues during plant growth and development, as well as in response to several biotic and abiotic stresses. The few gene expression and mutant analyses to date indicate their involvement in plant growth, morphogenesis, senescence and adaptation and response to stress. In order to gain a further understanding of their function, an analysis and characterisation of MMP proteins, their activity and their substrates during plant growth and development are still required. This review describes plant MMP work to date, as well as the variety of genomic and proteomic methodologies available to characterise plant MMP activity, function and potential substrates.
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42

OFOSU-APPIAH, W., R. J. WARRINGTON, K. MORGAN, and J. A. WILKINS. "Lymphocyte Extracellular Matrix Interactions." Scandinavian Journal of Immunology 29, no. 5 (May 1989): 517–25. http://dx.doi.org/10.1111/j.1365-3083.1989.tb01154.x.

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43

da Silva Sergio, Luiz Philippe, Adenilson de Souza da Fonseca, Andre Luiz Mencalha, and Flavia de Paoli. "Photobiomodulation on extracellular matrix." Laser Physics 33, no. 3 (February 9, 2023): 033001. http://dx.doi.org/10.1088/1555-6611/acb70c.

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Abstract The extracellular matrix (ECM) is a three-dimensional multicomponent, and a structural meshwork constituted of many specialized macromolecules. Such macromolecules provide an essential scaffold to tissue cells and chemical signals involved in cell proliferation, survival, migration, and differentiation, which are crucial to tissue morphogenesis, homeostasis, and functions. Photobiomodulation (PBM) is based on non-ionizing radiations in the visible and infrared spectrum, emitted from low-power lasers, light-emitting diodes, and broadband light sources. PBM has been used for improving tissue repair, and successful results have been reported from experimental studies. In this review, studies were accessed by PubMed, and their findings on PBM-induced effects on the ECM were summarized. The results showed that low-power violet-red lights and near-infrared radiation modulate gene expression, cell proliferation, adhesion and differentiation, factors and enzymes, and structural constituents in the ECM. These results showed a dependence on radiation wavelength, fluence, irradiance, exposure time, emission mode, and cellular and tissue conditions. Such results suggest that the irradiation parameters, biological tissue type, and conditions should be considered for an effective therapeutic protocol aiming at tissue repair based on PBM-induced extracellular matrix remodeling.
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44

Mecham, Robert P. "Overview of Extracellular Matrix." Current Protocols in Cell Biology 00, no. 1 (October 1998): 10.1.1–10.1.14. http://dx.doi.org/10.1002/0471143030.cb1001s00.

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45

Screen, Hazel R. C., David E. Berk, Karl E. Kadler, Francesco Ramirez, and Marian F. Young. "Tendon Functional Extracellular Matrix." Journal of Orthopaedic Research 33, no. 6 (April 29, 2015): 793–99. http://dx.doi.org/10.1002/jor.22818.

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46

Martinez-Hernandez, Antonio, and Peter S. Amenta. "The hepatic extracellular matrix." Virchows Archiv A Pathological Anatomy and Histopathology 423, no. 1 (January 1993): 1–11. http://dx.doi.org/10.1007/bf01606425.

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47

Martinez-Hernandez, Antonio, and Peter S. Amenta. "The hepatic extracellular matrix." Virchows Archiv A Pathological Anatomy and Histopathology 423, no. 2 (March 1993): 77–84. http://dx.doi.org/10.1007/bf01606580.

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48

Dolmatov, Igor Yu, and Vladimir A. Nizhnichenko. "Extracellular Matrix of Echinoderms." Marine Drugs 21, no. 7 (July 22, 2023): 417. http://dx.doi.org/10.3390/md21070417.

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This review considers available data on the composition of the extracellular matrix (ECM) in echinoderms. The connective tissue in these animals has a rather complex organization. It includes a wide range of structural ECM proteins, as well as various proteases and their inhibitors. Members of almost all major groups of collagens, various glycoproteins, and proteoglycans have been found in echinoderms. There are enzymes for the synthesis of structural proteins and their modification by polysaccharides. However, the ECM of echinoderms substantially differs from that of vertebrates by the lack of elastin, fibronectins, tenascins, and some other glycoproteins and proteoglycans. Echinoderms have a wide variety of proteinases, with serine, cysteine, aspartic, and metal peptidases identified among them. Their active centers have a typical structure and can break down various ECM molecules. Echinoderms are also distinguished by a wide range of proteinase inhibitors. The complex ECM structure and the variety of intermolecular interactions evidently explain the complexity of the mechanisms responsible for variations in the mechanical properties of connective tissue in echinoderms. These mechanisms probably depend not only on the number of cross-links between the molecules, but also on the composition of ECM and the properties of its proteins.
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49

Patel, Neil J., Anisa Ashraf, and Eun Ji Chung. "Extracellular Vesicles as Regulators of the Extracellular Matrix." Bioengineering 10, no. 2 (January 19, 2023): 136. http://dx.doi.org/10.3390/bioengineering10020136.

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Extracellular vesicles (EVs) are small membrane-bound vesicles secreted into the extracellular space by all cell types. EVs transfer their cargo which includes nucleic acids, proteins, and lipids to facilitate cell-to-cell communication. As EVs are released and move from parent to recipient cell, EVs interact with the extracellular matrix (ECM) which acts as a physical scaffold for the organization and function of cells. Recent work has shown that EVs can modulate and act as regulators of the ECM. This review will first discuss EV biogenesis and the mechanism by which EVs are transported through the ECM. Additionally, we discuss how EVs contribute as structural components of the matrix and as components that aid in the degradation of the ECM. Lastly, the role of EVs in influencing recipient cells to remodel the ECM in both pathological and therapeutic contexts is examined.
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50

Mebarek, Saida, Rene Buchet, Slawomir Pikula, Agnieszka Strzelecka-Kiliszek, Leyre Brizuela, Giada Corti, Federica Collacchi, et al. "Do Media Extracellular Vesicles and Extracellular Vesicles Bound to the Extracellular Matrix Represent Distinct Types of Vesicles?" Biomolecules 14, no. 1 (December 28, 2023): 42. http://dx.doi.org/10.3390/biom14010042.

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Mineralization-competent cells, including hypertrophic chondrocytes, mature osteoblasts, and osteogenic-differentiated smooth muscle cells secrete media extracellular vesicles (media vesicles) and extracellular vesicles bound to the extracellular matrix (matrix vesicles). Media vesicles are purified directly from the extracellular medium. On the other hand, matrix vesicles are purified after discarding the extracellular medium and subjecting the cells embedded in the extracellular matrix or bone or cartilage tissues to an enzymatic treatment. Several pieces of experimental evidence indicated that matrix vesicles and media vesicles isolated from the same types of mineralizing cells have distinct lipid and protein composition as well as functions. These findings support the view that matrix vesicles and media vesicles released by mineralizing cells have different functions in mineralized tissues due to their location, which is anchored to the extracellular matrix versus free-floating.
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