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Matrix Biology, 1994
Laminins are extracellular matrix proteins which consist of alpha, beta and gamma chains with molecular masses of 140-400 kDa. Chain association occurs through a large triple alpha-helical coiled-coil domain towards the C-terminus of each chain. Eight genetically distinct laminin chains (alpha 1, alpha 2, alpha 3, beta 1, beta 2, beta 3, gamma 1, gamma
R, Timpl, J C, Brown
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Laminins are extracellular matrix proteins which consist of alpha, beta and gamma chains with molecular masses of 140-400 kDa. Chain association occurs through a large triple alpha-helical coiled-coil domain towards the C-terminus of each chain. Eight genetically distinct laminin chains (alpha 1, alpha 2, alpha 3, beta 1, beta 2, beta 3, gamma 1, gamma
R, Timpl, J C, Brown
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The International Journal of Biochemistry & Cell Biology, 1996
The laminins are a family of extracellular matrix glycoproteins localized in the basement membrane that separates epithelial cells from the underlying stroma. They are also found in basement membrane surrounding fat, muscle and peripheral nerve cells. The laminins are large trimeric glycoproteins comprising three disulphide-bonded chains.
K M, Malinda, H K, Kleinman
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The laminins are a family of extracellular matrix glycoproteins localized in the basement membrane that separates epithelial cells from the underlying stroma. They are also found in basement membrane surrounding fat, muscle and peripheral nerve cells. The laminins are large trimeric glycoproteins comprising three disulphide-bonded chains.
K M, Malinda, H K, Kleinman
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Cell and Tissue Research, 2009
Laminins are cell adhesion molecules that comprise a family of glycoproteins found predominantly in basement membranes, which are the thin sheets of extracellular matrix that underlie epithelial and endothelial cells and surround muscle cells, Schwann cells, and fat cells.
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Laminins are cell adhesion molecules that comprise a family of glycoproteins found predominantly in basement membranes, which are the thin sheets of extracellular matrix that underlie epithelial and endothelial cells and surround muscle cells, Schwann cells, and fat cells.
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BioEssays, 1991
AbstractCells express many proteins that bind to laminin, the major adhesive component of basement membranes. Some of these, specifically integrins, function as transmembrane receptors that ‘signal’ the presence of laminin on the cell surface to the cytoplasm.
Mercurio, Arthur M., Shaw, Leslie M.
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AbstractCells express many proteins that bind to laminin, the major adhesive component of basement membranes. Some of these, specifically integrins, function as transmembrane receptors that ‘signal’ the presence of laminin on the cell surface to the cytoplasm.
Mercurio, Arthur M., Shaw, Leslie M.
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Journal of Cellular Biochemistry, 1996
Extracellular matrix molecules are often very large and made up of several independent domains, frequently with autonomous activities. Laminin is no exception. A number of globular and rod-like domains can be identified in laminin and its isoforms by sequence analysis as well as by electron microscopy.
Engvall, E, Wewer, U M
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Extracellular matrix molecules are often very large and made up of several independent domains, frequently with autonomous activities. Laminin is no exception. A number of globular and rod-like domains can be identified in laminin and its isoforms by sequence analysis as well as by electron microscopy.
Engvall, E, Wewer, U M
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Gynecologic and Obstetric Investigation, 1986
Laminin, a noncollagenous glycoprotein component of basement membranes, was measured in human serum by radioimmunoassay for the laminin P1 fragment. The concentration of immunoreactive laminin increased during pregnancy. Before delivery it was nearly twice the level found in nonpregnant women. After delivery levels dropped.
C, Bieglmayer, A, Feiks, R, Rudelstorfer
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Laminin, a noncollagenous glycoprotein component of basement membranes, was measured in human serum by radioimmunoassay for the laminin P1 fragment. The concentration of immunoreactive laminin increased during pregnancy. Before delivery it was nearly twice the level found in nonpregnant women. After delivery levels dropped.
C, Bieglmayer, A, Feiks, R, Rudelstorfer
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Clinical Immunology, 2016
Laminins are ubiquitous constituents of the basement membranes with major architectural and functional role as supported by the fact that absence or mutations of laminins lead to either lethal or severely impairing phenotypes. Besides genetic defects, laminins are involved in a wide range of human diseases including cancer, infections, and inflammatory
Florina Florea +3 more
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Laminins are ubiquitous constituents of the basement membranes with major architectural and functional role as supported by the fact that absence or mutations of laminins lead to either lethal or severely impairing phenotypes. Besides genetic defects, laminins are involved in a wide range of human diseases including cancer, infections, and inflammatory
Florina Florea +3 more
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Studies on human laminin and laminin-collagen complexes
Connective Tissue Research, 1991Intact human laminin and laminin type IV collagen complexes were extracted from term placental membranes and their structures were examined by electroimmunoblot and by rotary shadowing electron microscopy. Rotary shadowing electron microscopy revealed a structure of human laminin which is essentially similar to the cruciform structure of the mouse ...
M, Ohno, N, Ohno, N A, Kefalides
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2016
Laminins are a major constituent of the basement membrane which is an intricate meshwork of proteins separating the epithelium, mesothelium and endothelium from connective tissue. There are 15 different laminins each consisting of a unique combination of 3 subchains. The combination of chains confers some tissue specificity.
Rasmussen, Daniel Guldager Kring +1 more
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Laminins are a major constituent of the basement membrane which is an intricate meshwork of proteins separating the epithelium, mesothelium and endothelium from connective tissue. There are 15 different laminins each consisting of a unique combination of 3 subchains. The combination of chains confers some tissue specificity.
Rasmussen, Daniel Guldager Kring +1 more
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Current Opinion in Cell Biology, 1993
During the preceding year significant progress has been made in our understanding of laminin structure and expression. Highlights include the identification of new subunit chains and molecular isoforms as well as new information on tissue-specific gene expression, laminin self-assembly and interactions with other matrix components.
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During the preceding year significant progress has been made in our understanding of laminin structure and expression. Highlights include the identification of new subunit chains and molecular isoforms as well as new information on tissue-specific gene expression, laminin self-assembly and interactions with other matrix components.
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