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Journal articles on the topic 'Extracellular matrix proteins'

Author: Grafiati
Published: 4 June 2021
Last updated: 1 August 2024

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1

Ruggiero, Florence, and Manuel Koch. "Making recombinant extracellular matrix proteins." Methods 45, no. 1 (May 2008): 75–85. http://dx.doi.org/10.1016/j.ymeth.2008.01.003.

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2

GOLDFARB, RONALD H., and LANCE A. LIOTTA. "Thrombin Cleavage of Extracellular Matrix Proteins." Annals of the New York Academy of Sciences 485, no. 1 Bioregulatory (December 1986): 288–92. http://dx.doi.org/10.1111/j.1749-6632.1986.tb34590.x.

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3

Coito, Ana J., and Jerzy W. Kupiec-Weglinski. "EXTRACELLULAR MATRIX PROTEINS IN ORGAN TRANSPLANTATION1." Transplantation 69, no. 12 (June 2000): 2465–73. http://dx.doi.org/10.1097/00007890-200006270-00001.

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4

Giomarelli, Barbara, Livia Visai, Karolin Hijazi, Simonetta Rindi, Michela Ponzio, Francesco Iannelli, Pietro Speziale, and Gianni Pozzi. "Binding ofStreptococcus gordoniito extracellular matrix proteins." FEMS Microbiology Letters 265, no. 2 (December 2006): 172–77. http://dx.doi.org/10.1111/j.1574-6968.2006.00479.x.

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5

Moran, A. P., P. Kuusela, and T. U. Kosunen. "Interaction ofHelicobacter pyloriwith extracellular matrix proteins." Journal of Applied Bacteriology 75, no. 2 (August 1993): 184–89. http://dx.doi.org/10.1111/j.1365-2672.1993.tb02765.x.

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6

Hedley, S. J., D. J. Gawkrodger, A. P. Weetman, and S. MacNeil. "Extracellular matrix proteins stimulate melanocyte tyrosinase." Melanoma Research 5 (September 1995): 38. http://dx.doi.org/10.1097/00008390-199509001-00068.

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7

Campbell, N. E., L. Kellenberger, J. Greenaway, R. A. Moorehead, N. M. Linnerth-Petrik, and J. Petrik. "Extracellular Matrix Proteins and Tumor Angiogenesis." Journal of Oncology 2010 (2010): 1–13. http://dx.doi.org/10.1155/2010/586905.

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Tumor development is a complex process that relies on interaction and communication between a number of cellular compartments. Much of the mass of a solid tumor is comprised of the stroma which is richly invested with extracellular matrix. Within this matrix are a host of matricellular proteins that regulate the expression and function of a myriad of proteins that regulate tumorigenic processes. One of the processes that is vital to tumor growth and progression is angiogenesis, or the formation of new blood vessels from preexisting vasculature. Within the extracellular matrix are structural proteins, a host of proteases, and resident pro- and antiangiogenic factors that control tumor angiogenesis in a tightly regulated fashion. This paper discusses the role that the extracellular matrix and ECM proteins play in the regulation of tumor angiogenesis.
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8

Patel, Trushar R., and Joerg Stetefeld. "Solution Conformation of Extracellular Matrix Proteins." Biophysical Journal 102, no. 3 (January 2012): 381a. http://dx.doi.org/10.1016/j.bpj.2011.11.2086.

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9

Pakianathan, Deepika R. "Extracellular matrix proteins and leukocyte function." Journal of Leukocyte Biology 57, no. 5 (May 1995): 699–702. http://dx.doi.org/10.1002/jlb.57.5.699a.

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10

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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11

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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12

Hynes, Richard O. "The evolution of metazoan extracellular matrix." Journal of Cell Biology 196, no. 6 (March 19, 2012): 671–79. http://dx.doi.org/10.1083/jcb.201109041.

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The modular domain structure of extracellular matrix (ECM) proteins and their genes has allowed extensive exon/domain shuffling during evolution to generate hundreds of ECM proteins. Many of these arose early during metazoan evolution and have been highly conserved ever since. Others have undergone duplication and divergence during evolution, and novel combinations of domains have evolved to generate new ECM proteins, particularly in the vertebrate lineage. The recent sequencing of several genomes has revealed many details of this conservation and evolution of ECM proteins to serve diverse functions in metazoa.
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13

Aasebø, Elise, Annette K. Brenner, Even Birkeland, Tor Henrik Anderson Tvedt, Frode Selheim, Frode S. Berven, and Øystein Bruserud. "The Constitutive Extracellular Protein Release by Acute Myeloid Leukemia Cells—A Proteomic Study of Patient Heterogeneity and Its Modulation by Mesenchymal Stromal Cells." Cancers 13, no. 7 (March 25, 2021): 1509. http://dx.doi.org/10.3390/cancers13071509.

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Extracellular protein release is important both for the formation of extracellular matrix and for communication between cells. We investigated the extracellular protein release by in vitro cultured normal mesenchymal stem cells (MSCs) and by primary human acute myeloid leukemia (AML) cells derived from 40 consecutive patients. We observed quantifiable levels of 3082 proteins in our study; for the MSCs, we detected 1446 proteins, whereas the number of released proteins for the AML cells showed wide variation between patients (average number 1699, range 557–2380). The proteins were derived from various cellular compartments (e.g., cell membrane, nucleus, and cytoplasms), several organelles (e.g., cytoskeleton, endoplasmatic reticulum, Golgi apparatus, and mitochondria) and had various functions (e.g., extracellular matrix and exosomal proteins, cytokines, soluble adhesion molecules, protein synthesis, post-transcriptional modulation, RNA binding, and ribonuclear proteins). Thus, AML patients were very heterogeneous both regarding the number of proteins and the nature of their extracellularly released proteins. The protein release profiles of MSCs and primary AML cells show a considerable overlap, but a minority of the proteins are released only or mainly by the MSC, including several extracellular matrix molecules. Taken together, our observations suggest that the protein profile of the extracellular bone marrow microenvironment differs between AML patients, these differences are mainly caused by the protein release by the leukemic cells but this leukemia-associated heterogeneity of the overall extracellular protein profile is modulated by the constitutive protein release by normal MSCs.
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14

Gordon-Weeks, Alex, and Arseniy Yuzhalin. "Cancer Extracellular Matrix Proteins Regulate Tumour Immunity." Cancers 12, no. 11 (November 11, 2020): 3331. http://dx.doi.org/10.3390/cancers12113331.

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The extracellular matrix (ECM) plays an increasingly recognised role in the development and progression of cancer. Whilst significant progress has been made in targeting aspects of the tumour microenvironment such as tumour immunity and angiogenesis, there are no therapies that address the cancer ECM. Importantly, immune function relies heavily on the structure, physics and composition of the ECM, indicating that cancer ECM and immunity are mechanistically inseparable. In this review we highlight mechanisms by which the ECM shapes tumour immunity, identifying potential therapeutic targets within the ECM. These data indicate that to fully realise the potential of cancer immunotherapy, the cancer ECM requires simultaneous consideration.
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15

Villa-Verde, Dea Maria S., and Wilson Savino. "Thymic "nurse" cells express extracellular matrix proteins." Memórias do Instituto Oswaldo Cruz 86, suppl 3 (1991): 109–10. http://dx.doi.org/10.1590/s0074-02761991000700018.

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16

Bergmeier, W., and R. O. Hynes. "Extracellular Matrix Proteins in Hemostasis and Thrombosis." Cold Spring Harbor Perspectives in Biology 4, no. 2 (September 21, 2011): a005132. http://dx.doi.org/10.1101/cshperspect.a005132.

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17

Xiao, Jianguo, Magnus Höök, George M. Weinstock, and Barbara E. Murray. "Conditional adherence ofEnterococcus faecalisto extracellular matrix proteins." FEMS Immunology & Medical Microbiology 21, no. 4 (August 1998): 287–95. http://dx.doi.org/10.1111/j.1574-695x.1998.tb01176.x.

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18

KORNBLIHTT, ALBERTO R., and ALEJANDRO GUTMAN. "MOLECULAR BIOLOGY OF THE EXTRACELLULAR MATRIX PROTEINS." Biological Reviews 63, no. 4 (November 1988): 465–507. http://dx.doi.org/10.1111/j.1469-185x.1988.tb00668.x.

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19

Klotz, Stephen A., and Robert L. Smith. "Glycosaminoglycans inhibitCandida albicansadherence to extracellular matrix proteins." FEMS Microbiology Letters 99, no. 2-3 (December 1992): 205–8. http://dx.doi.org/10.1111/j.1574-6968.1992.tb05567.x.

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20

LÖW, PETER, NOÉMI H. BORHEGYI, MIKLÓS SASS, LAJOS LÁSZLÓ, and STUART E. REYNOLDS. "Ubiquitinated extracellular matrix proteins in insect cuticle." Biochemical Society Transactions 25, no. 3 (August 1, 1997): 379S. http://dx.doi.org/10.1042/bst025379s.

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21

Wagener, R. "Perifibrillar proteins in the cartilage extracellular matrix." Osteoarthritis and Cartilage 20 (April 2012): S3. http://dx.doi.org/10.1016/j.joca.2012.02.614.

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22

Zare¸ba, Tomasz W., Corina Pascu, Waleria Hryniewicz, and Torkel Wadström. "Binding of Extracellular Matrix Proteins by Enterococci." Current Microbiology 34, no. 1 (January 1, 1997): 6–11. http://dx.doi.org/10.1007/s002849900135.

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23

Hook, Magnus, Martin J. McGavin, Rampyari Raja, Giuseppe Raucci, Magnus Hook, Lech M. Switalski, Per-Eric Lindgren, Martin Lindberg, and Christer Signas. "Interactions of bacteria with extracellular matrix proteins." Cell Differentiation and Development 32, no. 3 (December 1990): 433–38. http://dx.doi.org/10.1016/0922-3371(90)90060-a.

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24

Štyriak, I., B. Žatkovič, and S. Maršalková. "Binding of extracellular matrix proteins by lactobacilli." Folia Microbiologica 46, no. 1 (February 2001): 83–85. http://dx.doi.org/10.1007/bf02825894.

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25

Maillard, Elisa, Marie-Christine Sencier, A. Langlois, William Bietiger, MP Krafft, Michel Pinget, and Séverine Sigrist. "Extracellular matrix proteins involved in pseudoislets formation." Islets 1, no. 3 (November 2009): 232–41. http://dx.doi.org/10.4161/isl.1.3.9754.

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26

Schenke-Layland, Katja. "Special Issue “Extracellular Matrix Proteins and Mimics”." Acta Biomaterialia 52 (April 2017): iv. http://dx.doi.org/10.1016/j.actbio.2017.03.029.

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27

Ma, Jun, Chao Ma, Jingjing Li, Yao Sun, Fangfu Ye, Kai Liu, and Hongjie Zhang. "Extracellular Matrix Proteins Involved in Alzheimer's Disease." Chemistry – A European Journal 26, no. 53 (July 23, 2020): 12101–10. http://dx.doi.org/10.1002/chem.202000782.

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28

Boskey, Adele L. "The Role of Extracellular Matrix Components in Dentin Mineralization." Critical Reviews in Oral Biology & Medicine 2, no. 3 (July 1991): 369–87. http://dx.doi.org/10.1177/10454411910020030501.

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The extracellular matrix of dentin consists of mineral (hydroxyapatite), collagen, and several noncollagenous matrix proteins. These noncollagenous matrix proteins may be mediators of cell-matrix interactions, matrix maturation, and mineralization. This review describes the current knowledge of the chemistry of mineral crystal formation in dentin with special emphasis on the roles of the dentin matrix proteins. The functions of some of these matrix proteins in the mineralization process have been deduced based on in vitro studies. Functions for others have been postulated based on analogy with some of the bone matrix proteins. Evidence suggests that several of these matrix proteins may have multiple effects on nucleation, crystal growth, and orientation of dentin hydroxyapatite.
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29

SMITH, ANTHONY J., ROSALIND S. TOBIAS, CLIVE G. PLANT, ROGER M. BROWNE, HERVE LESOT, and JEAN-VICTOR RUCH. "Morphogenese proteins from dentine extracellular matrix and cell-Matrix interactions." Biochemical Society Transactions 19, no. 2 (April 1, 1991): 187S. http://dx.doi.org/10.1042/bst019187s.

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30

Ma, Zihan, Chenfeng Mao, Yiting Jia, Yi Fu, and Wei Kong. "Extracellular matrix dynamics in vascular remodeling." American Journal of Physiology-Cell Physiology 319, no. 3 (September 1, 2020): C481—C499. http://dx.doi.org/10.1152/ajpcell.00147.2020.

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Vascular remodeling is the adaptive response to various physiological and pathophysiological alterations that are closely related to aging and vascular diseases. Understanding the mechanistic regulation of vascular remodeling may be favorable for discovering potential therapeutic targets and strategies. The extracellular matrix (ECM), including matrix proteins and their degradative metalloproteases, serves as the main component of the microenvironment and exhibits dynamic changes during vascular remodeling. This process involves mainly the altered composition of matrix proteins, metalloprotease-mediated degradation, posttranslational modification of ECM proteins, and altered topographical features of the ECM. To date, adequate studies have demonstrated that ECM dynamics also play a critical role in vascular remodeling in various diseases. Here, we review these related studies, summarize how ECM dynamics control vascular remodeling, and further indicate potential diagnostic biomarkers and therapeutic targets in the ECM for corresponding vascular diseases.
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31

Hynes, Richard O. "The Extracellular Matrix: Not Just Pretty Fibrils." Science 326, no. 5957 (November 26, 2009): 1216–19. http://dx.doi.org/10.1126/science.1176009.

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The extracellular matrix (ECM) and ECM proteins are important in phenomena as diverse as developmental patterning, stem cell niches, cancer, and genetic diseases. The ECM has many effects beyond providing structural support. ECM proteins typically include multiple, independently folded domains whose sequences and arrangement are highly conserved. Some of these domains bind adhesion receptors such as integrins that mediate cell-matrix adhesion and also transduce signals into cells. However, ECM proteins also bind soluble growth factors and regulate their distribution, activation, and presentation to cells. As organized, solid-phase ligands, ECM proteins can integrate complex, multivalent signals to cells in a spatially patterned and regulated fashion. These properties need to be incorporated into considerations of the functions of the ECM.
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32

Aasebø, Elise, Even Birkeland, Frode Selheim, Frode Berven, Annette K. Brenner, and Øystein Bruserud. "The Extracellular Bone Marrow Microenvironment—A Proteomic Comparison of Constitutive Protein Release by In Vitro Cultured Osteoblasts and Mesenchymal Stem Cells." Cancers 13, no. 1 (December 28, 2020): 62. http://dx.doi.org/10.3390/cancers13010062.

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Mesenchymal stem cells (MSCs) and osteoblasts are bone marrow stromal cells that contribute to the formation of stem cell niches and support normal hematopoiesis, leukemogenesis and development of metastases from distant cancers. This support is mediated through cell–cell contact, release of soluble mediators and formation of extracellular matrix. By using a proteomic approach, we characterized the protein release by in vitro cultured human MSCs (10 donors) and osteoblasts (nine donors). We identified 1379 molecules released by these cells, including 340 proteins belonging to the GO-term Extracellular matrix. Both cell types released a wide range of functionally heterogeneous proteins including extracellular matrix molecules (especially collagens), several enzymes and especially proteases, cytokines and soluble adhesion molecules, but also several intracellular molecules including chaperones, cytoplasmic mediators, histones and non-histone nuclear molecules. The levels of most proteins did not differ between MSCs and osteoblasts, but 82 proteins were more abundant for MSC (especially extracellular matrix proteins and proteases) and 36 proteins more abundant for osteoblasts. Finally, a large number of exosomal proteins were identified. To conclude, MSCs and osteoblasts show extracellular release of a wide range of functionally diverse proteins, including several extracellular matrix molecules known to support cancer progression (e.g., metastases from distant tumors, increased relapse risk for hematological malignancies), and the large number of identified exosomal proteins suggests that exocytosis is an important mechanism of protein release.
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33

Lorite, María J., Ariana Casas-Román, Lourdes Girard, Sergio Encarnación, Natalia Díaz-Garrido, Josefa Badía, Laura Baldomá, Daniel Pérez-Mendoza, and Juan Sanjuán. "Impact of c-di-GMP on the Extracellular Proteome of Rhizobium etli." Biology 12, no. 1 (December 26, 2022): 44. http://dx.doi.org/10.3390/biology12010044.

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Extracellular matrix components of bacterial biofilms include biopolymers such as polysaccharides, nucleic acids and proteins. Similar to polysaccharides, the secretion of adhesins and other matrix proteins can be regulated by the second messenger cyclic diguanylate (cdG). We have performed quantitative proteomics to determine the extracellular protein contents of a Rhizobium etli strain expressing high cdG intracellular levels. cdG promoted the exportation of proteins that likely participate in adhesion and biofilm formation: the rhizobial adhesion protein RapA and two previously undescribed likely adhesins, along with flagellins. Unexpectedly, cdG also promoted the selective exportation of cytoplasmic proteins. Nearly 50% of these cytoplasmic proteins have been previously described as moonlighting or candidate moonlighting proteins in other organisms, often found extracellularly. Western blot assays confirmed cdG-promoted export of two of these cytoplasmic proteins, the translation elongation factor (EF-Tu) and glyceraldehyde 3-phosphate dehydrogenase (Gap). Transmission Electron Microscopy immunolabeling located the Gap protein in the cytoplasm but was also associated with cell membranes and extracellularly, indicative of an active process of exportation that would be enhanced by cdG. We also obtained evidence that cdG increases the number of extracellular Gap proteoforms, suggesting a link between cdG, the post-translational modification and the export of cytoplasmic proteins.
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34

Hahn, U. "Extracellular Matrix Proteins in Small-Intestinal Cell Cultures." Scandinavian Journal of Gastroenterology 23, sup151 (January 1988): 70–78. http://dx.doi.org/10.3109/00365528809095916.

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35

Xu, Xuehong, and Bruce E. Vogel. "A new job for ancient extracellular matrix proteins." Communicative & Integrative Biology 4, no. 4 (July 2011): 433–35. http://dx.doi.org/10.4161/cib.15324.

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36

Kanasaki, Haruhiko. "Extracellular Matrix Proteins in the Anterior Pituitary Gland." Open Neuroendocrinology Journal 4, no. 1 (May 6, 2011): 111–19. http://dx.doi.org/10.2174/1876528901104010111.

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37

Ahmadi, Arash J., and Frederick A. Jakobiec. "Corneal Wound Healing: Cytokines and Extracellular Matrix Proteins." International Ophthalmology Clinics 42, no. 3 (2002): 13–22. http://dx.doi.org/10.1097/00004397-200207000-00004.

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38

SMITH, ANTHONY J., HERVE LESOT, JOHN B. MATTHEWS, JEAN-VICTOR RUCH, and VERA KARCHER-DJURICIC. "Relationship between keratins and dental extracellular matrix proteins." Biochemical Society Transactions 15, no. 5 (October 1, 1987): 855–56. http://dx.doi.org/10.1042/bst0150855.

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39

Rodier, Marie-Hélène, Brahim El Moudni, Catherine Kauffmann-Lacroix, Gyslaine Daniault, and Jean-Louis Jacquemin. "ACandida albicansmetallopeptidase degrades constitutive proteins of extracellular matrix." FEMS Microbiology Letters 177, no. 2 (August 1999): 205–10. http://dx.doi.org/10.1111/j.1574-6968.1999.tb13733.x.

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40

Westerlund, B., and T. K. Korhonen. "Bacterial proteins binding to the mammalian extracellular matrix." Molecular Microbiology 9, no. 4 (August 1993): 687–94. http://dx.doi.org/10.1111/j.1365-2958.1993.tb01729.x.

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41

Gonzalez, Angel, Beatriz L. Gomez, Angela Restrepo, Andrew John Hamilton, and Luz Elena Cano. "Recognition of extracellular matrix proteins byParacoccidioides brasiliensisyeast cells." Medical Mycology 43, no. 7 (January 2005): 637–45. http://dx.doi.org/10.1080/13693780500064599.

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42

Bauer, Margaret E., and Stanley M. Spinola. "Binding of Haemophilus ducreyi to Extracellular Matrix Proteins." Infection and Immunity 67, no. 5 (May 1, 1999): 2649–52. http://dx.doi.org/10.1128/iai.67.5.2649-2652.1999.

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ABSTRACT We developed an enzyme-linked immunosorbent assay-based assay to assess Haemophilus ducreyi binding to extracellular matrix (ECM) proteins. H. ducreyi 35000HP bound to fibronectin, laminin, and type I and III collagen but not to type IV, V, or VI collagen or elastin. Isogenic strains with mutations inftpA or losB bound as well as the parent, suggesting that neither pili nor full-length lipooligosaccharide is required for H. ducreyi to bind to ECM proteins.
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43

Manabe, R. i., K. Tsutsui, T. Yamada, M. Kimura, I. Nakano, C. Shimono, N. Sanzen, et al. "Transcriptome-based systematic identification of extracellular matrix proteins." Proceedings of the National Academy of Sciences 105, no. 35 (August 29, 2008): 12849–54. http://dx.doi.org/10.1073/pnas.0803640105.

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44

Mendes-Giannini, Maria José Soares, Patrícia Ferrari Andreotti, Luciana Raquel Vincenzi, Juliana Leal Monteiro da Silva, Henrique Leonel Lenzi, Gil Benard, Roseli Zancopé-Oliveira, Herbert Leonel de Matos Guedes, and Christiane Pienna Soares. "Binding of extracellular matrix proteins to Paracoccidioides brasiliensis." Microbes and Infection 8, no. 6 (May 2006): 1550–59. http://dx.doi.org/10.1016/j.micinf.2006.01.012.

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45

Esgleas, Miriam, Sonia Lacouture, and Marcelo Gottschalk. "Streptococcus suisserotype 2 binding to extracellular matrix proteins." FEMS Microbiology Letters 244, no. 1 (March 2005): 33–40. http://dx.doi.org/10.1016/j.femsle.2005.01.017.

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46

Abeck, Dietrich, Alan P. Johnson, and H. Mensing. "Binding of Haemophilus ducreyi to extracellular matrix proteins." Microbial Pathogenesis 13, no. 1 (July 1992): 81–84. http://dx.doi.org/10.1016/0882-4010(92)90034-l.

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47

Tan, Kemin, and Jack Lawler. "The interaction of Thrombospondins with extracellular matrix proteins." Journal of Cell Communication and Signaling 3, no. 3-4 (October 16, 2009): 177–87. http://dx.doi.org/10.1007/s12079-009-0074-2.

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48

Hedrick, Lora. "Guidebook to the extracellular matrix and adhesion proteins." Trends in Cell Biology 4, no. 2 (February 1994): 65. http://dx.doi.org/10.1016/0962-8924(94)90013-2.

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49

Chiquet-Ehrismann, R. "Tenascins, a growing family of extracellular matrix proteins." Experientia 51, no. 9-10 (September 1995): 853–62. http://dx.doi.org/10.1007/bf01921736.

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50

Pollard, Thomas D. "Guidebook to the extracellular matrix and adhesion proteins." Trends in Biochemical Sciences 19, no. 2 (February 1994): 96–97. http://dx.doi.org/10.1016/0968-0004(94)90044-2.

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