Results 201 to 210 of about 108,751 (260)

α-Parvin regulation of cell rearrangement is critical for ureteric bud branching morphogenesis. [PDF]

open access: yesSci Adv
Dong X   +15 more
europepmc   +1 more source

Nipah virus infects the brain and triggers neuronal and glial damage in a hamster model. [PDF]

open access: yesJ Neuroinflammation
Valerdi K   +8 more
europepmc   +1 more source

The laminin family [PDF]

open access: yesCell Adhesion and 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 ...
Monique Aumailley
exaly   +3 more sources
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Domains of laminin

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.
Eva Engvall
exaly   +3 more sources

The laminins

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
openaire   +2 more sources

The laminins

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
openaire   +2 more sources

Laminin-11

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
openaire   +2 more sources

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