Artigos de revistas: "Extracellular matrix proteins"

1

Ruggiero, Florence, e Manuel Koch. "Making recombinant extracellular matrix proteins". Methods 45, n.º 1 (maio de 2008): 75–85. http://dx.doi.org/10.1016/j.ymeth.2008.01.003.

Texto completo da fonte

Estilos ABNT, Harvard, Vancouver, APA, etc.

2

GOLDFARB, RONALD H., e LANCE A. LIOTTA. "Thrombin Cleavage of Extracellular Matrix Proteins". Annals of the New York Academy of Sciences 485, n.º 1 Bioregulatory (dezembro de 1986): 288–92. http://dx.doi.org/10.1111/j.1749-6632.1986.tb34590.x.

Texto completo da fonte

Estilos ABNT, Harvard, Vancouver, APA, etc.

3

Coito, Ana J., e Jerzy W. Kupiec-Weglinski. "EXTRACELLULAR MATRIX PROTEINS IN ORGAN TRANSPLANTATION1". Transplantation 69, n.º 12 (junho de 2000): 2465–73. http://dx.doi.org/10.1097/00007890-200006270-00001.

Texto completo da fonte

Estilos ABNT, Harvard, Vancouver, APA, etc.

4

Giomarelli, Barbara, Livia Visai, Karolin Hijazi, Simonetta Rindi, Michela Ponzio, Francesco Iannelli, Pietro Speziale e Gianni Pozzi. "Binding ofStreptococcus gordoniito extracellular matrix proteins". FEMS Microbiology Letters 265, n.º 2 (dezembro de 2006): 172–77. http://dx.doi.org/10.1111/j.1574-6968.2006.00479.x.

Texto completo da fonte

Estilos ABNT, Harvard, Vancouver, APA, etc.

5

Moran, A. P., P. Kuusela e T. U. Kosunen. "Interaction ofHelicobacter pyloriwith extracellular matrix proteins". Journal of Applied Bacteriology 75, n.º 2 (agosto de 1993): 184–89. http://dx.doi.org/10.1111/j.1365-2672.1993.tb02765.x.

Texto completo da fonte

Estilos ABNT, Harvard, Vancouver, APA, etc.

6

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

Texto completo da fonte

Estilos ABNT, Harvard, Vancouver, APA, etc.

7

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

Texto completo da fonte

Resumo:

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.

Estilos ABNT, Harvard, Vancouver, APA, etc.

8

Patel, Trushar R., e Joerg Stetefeld. "Solution Conformation of Extracellular Matrix Proteins". Biophysical Journal 102, n.º 3 (janeiro de 2012): 381a. http://dx.doi.org/10.1016/j.bpj.2011.11.2086.

Texto completo da fonte

Estilos ABNT, Harvard, Vancouver, APA, etc.

9

Pakianathan, Deepika R. "Extracellular matrix proteins and leukocyte function". Journal of Leukocyte Biology 57, n.º 5 (maio de 1995): 699–702. http://dx.doi.org/10.1002/jlb.57.5.699a.

Texto completo da fonte

Estilos ABNT, Harvard, Vancouver, APA, etc.

10

Dolmatov, Igor Yu, e Vladimir A. Nizhnichenko. "Extracellular Matrix of Echinoderms". Marine Drugs 21, n.º 7 (22 de julho de 2023): 417. http://dx.doi.org/10.3390/md21070417.

Texto completo da fonte

Resumo:

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.

Estilos ABNT, Harvard, Vancouver, APA, etc.

11

Flinn, Barry S. "Plant extracellular matrix metalloproteinases". Functional Plant Biology 35, n.º 12 (2008): 1183. http://dx.doi.org/10.1071/fp08182.

Texto completo da fonte

Resumo:

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.

Estilos ABNT, Harvard, Vancouver, APA, etc.

12

Hynes, Richard O. "The evolution of metazoan extracellular matrix". Journal of Cell Biology 196, n.º 6 (19 de março de 2012): 671–79. http://dx.doi.org/10.1083/jcb.201109041.

Texto completo da fonte

Resumo:

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.

Estilos ABNT, Harvard, Vancouver, APA, etc.

13

Aasebø, Elise, Annette K. Brenner, Even Birkeland, Tor Henrik Anderson Tvedt, Frode Selheim, Frode S. Berven e 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, n.º 7 (25 de março de 2021): 1509. http://dx.doi.org/10.3390/cancers13071509.

Texto completo da fonte

Resumo:

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.

Estilos ABNT, Harvard, Vancouver, APA, etc.

14

Gordon-Weeks, Alex, e Arseniy Yuzhalin. "Cancer Extracellular Matrix Proteins Regulate Tumour Immunity". Cancers 12, n.º 11 (11 de novembro de 2020): 3331. http://dx.doi.org/10.3390/cancers12113331.

Texto completo da fonte

Resumo:

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.

Estilos ABNT, Harvard, Vancouver, APA, etc.

15

Villa-Verde, Dea Maria S., e 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.

Texto completo da fonte

Estilos ABNT, Harvard, Vancouver, APA, etc.

16

Bergmeier, W., e R. O. Hynes. "Extracellular Matrix Proteins in Hemostasis and Thrombosis". Cold Spring Harbor Perspectives in Biology 4, n.º 2 (21 de setembro de 2011): a005132. http://dx.doi.org/10.1101/cshperspect.a005132.

Texto completo da fonte

Estilos ABNT, Harvard, Vancouver, APA, etc.

17

Xiao, Jianguo, Magnus HÃ¶Ã¶k, George M. Weinstock e Barbara E. Murray. "Conditional adherence ofEnterococcus faecalisto extracellular matrix proteins". FEMS Immunology & Medical Microbiology 21, n.º 4 (agosto de 1998): 287–95. http://dx.doi.org/10.1111/j.1574-695x.1998.tb01176.x.

Texto completo da fonte

Estilos ABNT, Harvard, Vancouver, APA, etc.

18

KORNBLIHTT, ALBERTO R., e ALEJANDRO GUTMAN. "MOLECULAR BIOLOGY OF THE EXTRACELLULAR MATRIX PROTEINS". Biological Reviews 63, n.º 4 (novembro de 1988): 465–507. http://dx.doi.org/10.1111/j.1469-185x.1988.tb00668.x.

Texto completo da fonte

Estilos ABNT, Harvard, Vancouver, APA, etc.

19

Klotz, Stephen A., e Robert L. Smith. "Glycosaminoglycans inhibitCandida albicansadherence to extracellular matrix proteins". FEMS Microbiology Letters 99, n.º 2-3 (dezembro de 1992): 205–8. http://dx.doi.org/10.1111/j.1574-6968.1992.tb05567.x.

Texto completo da fonte

Estilos ABNT, Harvard, Vancouver, APA, etc.

20

LÖW, PETER, NOÉMI H. BORHEGYI, MIKLÓS SASS, LAJOS LÁSZLÓ e STUART E. REYNOLDS. "Ubiquitinated extracellular matrix proteins in insect cuticle". Biochemical Society Transactions 25, n.º 3 (1 de agosto de 1997): 379S. http://dx.doi.org/10.1042/bst025379s.

Texto completo da fonte

Estilos ABNT, Harvard, Vancouver, APA, etc.

21

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

Texto completo da fonte

Estilos ABNT, Harvard, Vancouver, APA, etc.

22

Zare¸ba, Tomasz W., Corina Pascu, Waleria Hryniewicz e Torkel Wadström. "Binding of Extracellular Matrix Proteins by Enterococci". Current Microbiology 34, n.º 1 (1 de janeiro de 1997): 6–11. http://dx.doi.org/10.1007/s002849900135.

Texto completo da fonte

Estilos ABNT, Harvard, Vancouver, APA, etc.

23

Hook, Magnus, Martin J. McGavin, Rampyari Raja, Giuseppe Raucci, Magnus Hook, Lech M. Switalski, Per-Eric Lindgren, Martin Lindberg e Christer Signas. "Interactions of bacteria with extracellular matrix proteins". Cell Differentiation and Development 32, n.º 3 (dezembro de 1990): 433–38. http://dx.doi.org/10.1016/0922-3371(90)90060-a.

Texto completo da fonte

Estilos ABNT, Harvard, Vancouver, APA, etc.

24

Štyriak, I., B. Žatkovič e S. Maršalková. "Binding of extracellular matrix proteins by lactobacilli". Folia Microbiologica 46, n.º 1 (fevereiro de 2001): 83–85. http://dx.doi.org/10.1007/bf02825894.

Texto completo da fonte

Estilos ABNT, Harvard, Vancouver, APA, etc.

25

Maillard, Elisa, Marie-Christine Sencier, A. Langlois, William Bietiger, MP Krafft, Michel Pinget e Séverine Sigrist. "Extracellular matrix proteins involved in pseudoislets formation". Islets 1, n.º 3 (novembro de 2009): 232–41. http://dx.doi.org/10.4161/isl.1.3.9754.

Texto completo da fonte

Estilos ABNT, Harvard, Vancouver, APA, etc.

26

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

Texto completo da fonte

Estilos ABNT, Harvard, Vancouver, APA, etc.

27

Ma, Jun, Chao Ma, Jingjing Li, Yao Sun, Fangfu Ye, Kai Liu e Hongjie Zhang. "Extracellular Matrix Proteins Involved in Alzheimer's Disease". Chemistry – A European Journal 26, n.º 53 (23 de julho de 2020): 12101–10. http://dx.doi.org/10.1002/chem.202000782.

Texto completo da fonte

Estilos ABNT, Harvard, Vancouver, APA, etc.

28

Boskey, Adele L. "The Role of Extracellular Matrix Components in Dentin Mineralization". Critical Reviews in Oral Biology & Medicine 2, n.º 3 (julho de 1991): 369–87. http://dx.doi.org/10.1177/10454411910020030501.

Texto completo da fonte

Resumo:

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.

Estilos ABNT, Harvard, Vancouver, APA, etc.

29

SMITH, ANTHONY J., ROSALIND S. TOBIAS, CLIVE G. PLANT, ROGER M. BROWNE, HERVE LESOT e JEAN-VICTOR RUCH. "Morphogenese proteins from dentine extracellular matrix and cell-Matrix interactions". Biochemical Society Transactions 19, n.º 2 (1 de abril de 1991): 187S. http://dx.doi.org/10.1042/bst019187s.

Texto completo da fonte

Estilos ABNT, Harvard, Vancouver, APA, etc.

30

Ma, Zihan, Chenfeng Mao, Yiting Jia, Yi Fu e Wei Kong. "Extracellular matrix dynamics in vascular remodeling". American Journal of Physiology-Cell Physiology 319, n.º 3 (1 de setembro de 2020): C481—C499. http://dx.doi.org/10.1152/ajpcell.00147.2020.

Texto completo da fonte

Resumo:

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.

Estilos ABNT, Harvard, Vancouver, APA, etc.

31

Hynes, Richard O. "The Extracellular Matrix: Not Just Pretty Fibrils". Science 326, n.º 5957 (26 de novembro de 2009): 1216–19. http://dx.doi.org/10.1126/science.1176009.

Texto completo da fonte

Resumo:

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.

Estilos ABNT, Harvard, Vancouver, APA, etc.

32

Aasebø, Elise, Even Birkeland, Frode Selheim, Frode Berven, Annette K. Brenner e 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, n.º 1 (28 de dezembro de 2020): 62. http://dx.doi.org/10.3390/cancers13010062.

Texto completo da fonte

Resumo:

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.

Estilos ABNT, Harvard, Vancouver, APA, etc.

33

Lorite, María J., Ariana Casas-Román, Lourdes Girard, Sergio Encarnación, Natalia Díaz-Garrido, Josefa Badía, Laura Baldomá, Daniel Pérez-Mendoza e Juan Sanjuán. "Impact of c-di-GMP on the Extracellular Proteome of Rhizobium etli". Biology 12, n.º 1 (26 de dezembro de 2022): 44. http://dx.doi.org/10.3390/biology12010044.

Texto completo da fonte

Resumo:

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.

Estilos ABNT, Harvard, Vancouver, APA, etc.

34

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

Texto completo da fonte

Estilos ABNT, Harvard, Vancouver, APA, etc.

35

Xu, Xuehong, e Bruce E. Vogel. "A new job for ancient extracellular matrix proteins". Communicative & Integrative Biology 4, n.º 4 (julho de 2011): 433–35. http://dx.doi.org/10.4161/cib.15324.

Texto completo da fonte

Estilos ABNT, Harvard, Vancouver, APA, etc.

36

Kanasaki, Haruhiko. "Extracellular Matrix Proteins in the Anterior Pituitary Gland". Open Neuroendocrinology Journal 4, n.º 1 (6 de maio de 2011): 111–19. http://dx.doi.org/10.2174/1876528901104010111.

Texto completo da fonte

Estilos ABNT, Harvard, Vancouver, APA, etc.

37

Ahmadi, Arash J., e Frederick A. Jakobiec. "Corneal Wound Healing: Cytokines and Extracellular Matrix Proteins". International Ophthalmology Clinics 42, n.º 3 (2002): 13–22. http://dx.doi.org/10.1097/00004397-200207000-00004.

Texto completo da fonte

Estilos ABNT, Harvard, Vancouver, APA, etc.

38

SMITH, ANTHONY J., HERVE LESOT, JOHN B. MATTHEWS, JEAN-VICTOR RUCH e VERA KARCHER-DJURICIC. "Relationship between keratins and dental extracellular matrix proteins". Biochemical Society Transactions 15, n.º 5 (1 de outubro de 1987): 855–56. http://dx.doi.org/10.1042/bst0150855.

Texto completo da fonte

Estilos ABNT, Harvard, Vancouver, APA, etc.

39

Rodier, Marie-HÃ©lÃ¨ne, Brahim El Moudni, Catherine Kauffmann-Lacroix, Gyslaine Daniault e Jean-Louis Jacquemin. "ACandida albicansmetallopeptidase degrades constitutive proteins of extracellular matrix". FEMS Microbiology Letters 177, n.º 2 (agosto de 1999): 205–10. http://dx.doi.org/10.1111/j.1574-6968.1999.tb13733.x.

Texto completo da fonte

Estilos ABNT, Harvard, Vancouver, APA, etc.

40

Westerlund, B., e T. K. Korhonen. "Bacterial proteins binding to the mammalian extracellular matrix". Molecular Microbiology 9, n.º 4 (agosto de 1993): 687–94. http://dx.doi.org/10.1111/j.1365-2958.1993.tb01729.x.

Texto completo da fonte

Estilos ABNT, Harvard, Vancouver, APA, etc.

41

Gonzalez, Angel, Beatriz L. Gomez, Angela Restrepo, Andrew John Hamilton e Luz Elena Cano. "Recognition of extracellular matrix proteins byParacoccidioides brasiliensisyeast cells". Medical Mycology 43, n.º 7 (janeiro de 2005): 637–45. http://dx.doi.org/10.1080/13693780500064599.

Texto completo da fonte

Estilos ABNT, Harvard, Vancouver, APA, etc.

42

Bauer, Margaret E., e Stanley M. Spinola. "Binding of Haemophilus ducreyi to Extracellular Matrix Proteins". Infection and Immunity 67, n.º 5 (1 de maio de 1999): 2649–52. http://dx.doi.org/10.1128/iai.67.5.2649-2652.1999.

Texto completo da fonte

Resumo:

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.

Estilos ABNT, Harvard, Vancouver, APA, etc.

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, n.º 35 (29 de agosto de 2008): 12849–54. http://dx.doi.org/10.1073/pnas.0803640105.

Texto completo da fonte

Estilos ABNT, Harvard, Vancouver, APA, etc.

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 e Christiane Pienna Soares. "Binding of extracellular matrix proteins to Paracoccidioides brasiliensis". Microbes and Infection 8, n.º 6 (maio de 2006): 1550–59. http://dx.doi.org/10.1016/j.micinf.2006.01.012.

Texto completo da fonte

Estilos ABNT, Harvard, Vancouver, APA, etc.

45

Esgleas, Miriam, Sonia Lacouture e Marcelo Gottschalk. "Streptococcus suisserotype 2 binding to extracellular matrix proteins". FEMS Microbiology Letters 244, n.º 1 (março de 2005): 33–40. http://dx.doi.org/10.1016/j.femsle.2005.01.017.

Texto completo da fonte

Estilos ABNT, Harvard, Vancouver, APA, etc.

46

Abeck, Dietrich, Alan P. Johnson e H. Mensing. "Binding of Haemophilus ducreyi to extracellular matrix proteins". Microbial Pathogenesis 13, n.º 1 (julho de 1992): 81–84. http://dx.doi.org/10.1016/0882-4010(92)90034-l.

Texto completo da fonte

Estilos ABNT, Harvard, Vancouver, APA, etc.

47

Tan, Kemin, e Jack Lawler. "The interaction of Thrombospondins with extracellular matrix proteins". Journal of Cell Communication and Signaling 3, n.º 3-4 (16 de outubro de 2009): 177–87. http://dx.doi.org/10.1007/s12079-009-0074-2.

Texto completo da fonte

Estilos ABNT, Harvard, Vancouver, APA, etc.

48

Hedrick, Lora. "Guidebook to the extracellular matrix and adhesion proteins". Trends in Cell Biology 4, n.º 2 (fevereiro de 1994): 65. http://dx.doi.org/10.1016/0962-8924(94)90013-2.

Texto completo da fonte

Estilos ABNT, Harvard, Vancouver, APA, etc.

49

Chiquet-Ehrismann, R. "Tenascins, a growing family of extracellular matrix proteins". Experientia 51, n.º 9-10 (setembro de 1995): 853–62. http://dx.doi.org/10.1007/bf01921736.

Texto completo da fonte

Estilos ABNT, Harvard, Vancouver, APA, etc.

50

Pollard, Thomas D. "Guidebook to the extracellular matrix and adhesion proteins". Trends in Biochemical Sciences 19, n.º 2 (fevereiro de 1994): 96–97. http://dx.doi.org/10.1016/0968-0004(94)90044-2.

Texto completo da fonte

Estilos ABNT, Harvard, Vancouver, APA, etc.

Artigos de revistas sobre o tema "Extracellular matrix proteins"

Crie uma referência precisa em APA, MLA, Chicago, Harvard, e outros estilos