Results 1 to 10 of about 75,721 (187)
The Journal of Cell Biology, 2004 Laminin-1 is emerging as the key molecule in early embryonic basement membrane assembly. Here we review recent insights into its functions gained from the synergistic application of genetic and structural methods.
Takako Sasaki +2 more
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Cell Adhesion & Migration, 2013 Laminins are large molecular weight glycoproteins constituted by the assembly of three disulfide-linked polypeptides, the α, β and γ chains. The human genome encodes 11 genetically distinct laminin chains. Structurally, laminin chains differ by the number, size and organization of a few constitutive domains, endowing the various members of the laminin ...
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Experimental Lung Research, 1997 Laminins are essential components of basement membranes, playing important roles in cell adhesion, proliferation, and differentiation. These heterotrimeric glycoproteins are composed of an alpha, beta, and gamma chains held together by disulfide bonds. The first laminin identified, from the mouse Engelbreth-Holm-Swarm (EHS) tumor, is now referred to as
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Cold Spring Harbor Symposia on Quantitative Biology, 1990 J R, Sanes +3 more
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Some of the next articles are maybe not open access.
The International Journal of Biochemistry & Cell Biology, 1999
Laminins are a family of glycoproteins which are ubiquitous components of basement membranes and play key structural and functional roles. Eleven isoforms have been identified to date; each is an alpha beta gamma heterotrimer assembled from a repertoire of five alpha, three beta and two gamma chains.
J H, Miner, B L, Patton
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Laminins are a family of glycoproteins which are ubiquitous components of basement membranes and play key structural and functional roles. Eleven isoforms have been identified to date; each is an alpha beta gamma heterotrimer assembled from a repertoire of five alpha, three beta and two gamma chains.
J H, Miner, B L, Patton
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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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