"Receptors, Fibronectin" - Books

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See fn1.S (FIBRONECTIN) fibronectin 1 S homeolog in the Gene database

fibronectin in Xenopus laevis (2)Xenopus tropicalis All 3 Gene records

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Select item 14152801.

Madame Curie Bioscience Database [Internet].

Austin (TX): Landes Bioscience; 2000-2013.

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Select item 44036682.

StatPearls [Internet].

Treasure Island (FL): StatPearls Publishing; 2025 Jan-.

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Select item 42037203.

Streptococcus pyogenes : Basic Biology to Clinical Manifestations [Internet].

Ferretti JJ, Stevens DL, Fischetti VA, editors.

Oklahoma City (OK): University of Oklahoma Health Sciences Center; 2016-.

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Select item 16686904.

Holland-Frei Cancer Medicine. 6th edition.

Kufe DW, Pollock RE, Weichselbaum RR, et al., editors.

Hamilton (ON): BC Decker; 2003.

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Select item 54017685.

Streptococcus pyogenes: Basic Biology to Clinical Manifestations [Internet]. 2nd edition.

Ferretti JJ, Stevens DL, Fischetti VA, editors.

Oklahoma City (OK): University of Oklahoma Health Sciences Center; 2022 Oct 8.

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Select item 18957886.

Molecular Biology of the Cell. 4th edition.

Alberts B, Johnson A, Lewis J, et al.

New York: Garland Science; 2002.

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Select item 15027927.

Molecular Imaging and Contrast Agent Database (MICAD) [Internet].

Bethesda (MD): National Center for Biotechnology Information (US); 2004-2013.

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Select item 46666228.

Mechanisms of Vascular Disease: A Reference Book for Vascular Specialists [Internet].

Fitridge R, Thompson M, editors.

Adelaide (AU): University of Adelaide Press; 2011.

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Select item 16072129.

Developmental Biology. 6th edition.

Gilbert SF.

Sunderland (MA): Sinauer Associates; 2000.

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Select item 340129410.

Endotext [Internet].

Feingold KR, Ahmed SF, Anawalt B, et al., editors.

South Dartmouth (MA): MDText.com, Inc.; 2000-.

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Select item 532167211.

Essentials of Glycobiology [Internet]. 4th edition.

Varki A, Cummings RD, Esko JD, et al., editors.

Cold Spring Harbor (NY): Cold Spring Harbor Laboratory Press; 2022.

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Select item 140373812.

Polymicrobial Diseases.

Brogden KA, Guthmiller JM, editors.

Washington (DC): ASM Press; 2002.

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Select item 446506413.

Autoimmunity: From Bench to Bedside [Internet].

Anaya JM, Shoenfeld Y, Rojas-Villarraga A, et al., editors.

Bogota (Colombia): El Rosario University Press; 2013 Jul 18.

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Select item 326098014.

Contraceptive Research and Development: Looking to the Future.

Institute of Medicine (US) Committee on Contraceptive Research and Development; Harrison PF, Rosenfield A, editors.

Washington (DC): National Academies Press (US); 1996.

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Select item 296478815.

Pancreatic Cancer and Tumor Microenvironment.

Grippo PJ, Munshi HG, editors.

Trivandrum (India): Transworld Research Network; 2012.

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Select item 247336416.

Regulation of Endothelial Barrier Function.

Yuan SY, Rigor RR.

San Rafael (CA): Morgan & Claypool Life Sciences; 2010.

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Select item 219516217.

StemBook [Internet].

Cambridge (MA): Harvard Stem Cell Institute; 2008-.

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Select item 157694218.

Mechanosensitivity in Cells and Tissues.

Kamkin A, Kiseleva I, editors.

Moscow: Academia; 2005.

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Select item 159128619.

Comparative Oncology.

Baba AI, Câtoi C.

Bucharest (RO): The Publishing House of the Romanian Academy; 2007.

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Select item 159952420.

The Cell: A Molecular Approach. 2nd edition.

Cooper GM.

Sunderland (MA): Sinauer Associates; 2000.

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Figure 19-61Coalignment of extracellular fibronectin filaments and intracellular actin filament bundles

The fibronectin is visualized in two rat fibroblasts in culture by the binding of rhodamine-coupled anti-fibronectin antibodies (A). The actin is visualized by the binding of fluorescein-coupled anti-actin antibodies (B). (From R.O. Hynes and A.T. Destree, Cell 15:875-886, 1978. © Cell Press.)

Extracellular Matrix Receptors on Animal Cells: The Integrins.

Alberts B, Bray D, Lewis J, et al. Molecular Biology of the Cell. 3rd edition. New York: Garland Science; 1994.
Figure 1

Cytokines and receptors in hematopoiesis. The interaction of cytokines with their cell surface receptors characteristically induces receptor aggregation, activation and initiation of intracellular signal transduction. Receptors in the hematopoietin receptor family may form hetero-oligomeric structures, as exemplified by the IL-6 receptor, which combines an IL-6-specific α-chain with the gp130 signalling chain that is also used by other IL-6 family receptors, or homodimers such as with the G-CSF receptor and c-Mpl, the TPO receptor. Receptors of this class exhibit characteristic extracellular domain cysteine residues (C C) and WSXWS pentapeptide motif (WS). The hematopoietin receptor extracellular domains also contain fibronectin type-III-like (stippled) and immunoglobulin-like domains (shaded). Activation of tyrosine kinase receptors also involves cytokine-induced receptor oligomerisation, typified by the Flt3/Flk2 receptor and c-Kit, the receptor for SCF. These receptors also contain an intracellular tyrosine kinase domain (filled box), which is activated upon ligand binding and initiates signal transduction. Members of the TNF receptor family such as the TNFR and Fas, are though to trimerise upon ligand binding. The death domains (striped boxes) within the intracellular receptor region link the activated receptors with the cellular apoptosis machinery.

Knockout Mouse Models of Cytokine Action in Hematopoietic Stem Cell Regulation.

Madame Curie Bioscience Database [Internet]. Austin (TX): Landes Bioscience; 2000-2013.
Figure 1

Morphology and molecular interactions of extracellular galectins. A) Morphological changes during epithelial-mesenchymal transition (EMT) and galectin inhibition (nucleus is dark blue, cell membrane is light blue, fibronectin is red, and galectin is yellow). In the absence of galectin inhibition, fibronectin fibrillogenesis and actin polymerization occur and promote EMT. In contrast, galectin inhibition result is the blockade of EMT. B) In the absence of branched N-glycans there is reduced integrin and receptor tyrosine kinase receptor binding to fibronectin and absence of galectin binding. C) In the presence of branched N-glycans, there is increased binding of galectins to receptor tyrosine kinases, integrins and fibronectin, and ultimately promotes fibrillogenesis, EMT and metastatic phenotypic behavior. When branched N-glycans are present, the galectin lattice clusters membrane receptors, preventing endocytosis, and stabilizes adhesions during matrix remodeling, actin remodeling, receptor signaling, invasion, and metastasis.

Role of Galectins in Metastatic Breast Cancer.

Mayrovitz HN, editor. Breast Cancer [Internet]. Brisbane (AU): Exon Publications; 2022 Aug 6.
Figure 5.

Model for differential ingestion of S. pyogenes mediated by Sfb1 and M1 proteins. Interactions of fibronectin bound to Sfb1 and M1 protein with epithelial cells lead to different ingestion pathways. Sfb1-Fn complexes promote uptake of streptococci via caveolae, while M1-Fn complexes foster receptor-mediated endocytosis. The model proposes that these two different streptococcal fibronectin binding proteins direct distinct changes in the quaternary structure of fibronectin, which in turn generate divergent signals when fibronectin engages α5β1 receptors at the surface of epithelial cells. In the end, streptococci are either deposited into relatively safe caveosomes or into bactericidal phagolysosomes. Common components of the signal cascade include PI3K, ILK, and Paxillin; however, data suggest that the signals diverge at the point of Paxillin phosphorylation.

Adhesion and invasion of Streptococcus pyogenes into host cells and clinical relevance of intracellular streptococci.

Ferretti JJ, Stevens DL, Fischetti VA, editors. Streptococcus pyogenes: Basic Biology to Clinical Manifestations [Internet]. 2nd edition. Oklahoma City (OK): University of Oklahoma Health Sciences Center; 2022 Oct 8.