Results 241 to 250 of about 75,759 (281)
Class-I myosin responds to changes in membrane tension during clathrin-mediated endocytosis in human induced pluripotent stem cells. [PDF]
Smith SL +7 more
europepmc +1 more source
A Mitochondrial Plasma Proteomic Signature Identifies Metastatic Chromophobe Renal Cell Carcinoma. [PDF]
Steiner C +15 more
europepmc +1 more source
Altered cell-matrix associated ADAM proteins in Alzheimer disease
Alterations in cell-matrix 'contact' are often related to a disruption of cell cycle regulation and, as such, occur variously in neoplasia. Given the recent findings showing cell cycle alterations in Alzheimer disease, we undertook a study of ADAM-1 and 2 (A Disintegrin And Metalloprotease), developmentally-regulated, integrin-binding, membrane-bound ...
Arun K Raina +2 more
exaly +5 more sources
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ADAM family proteins in the immune system
Trends in Immunology, 1999CD156 is a member of a family proteins characterized by a disintegrin and a metalloprotease domain (ADAM). These molecules are phylogenically conserved but have individual roles in a variety of cells. Here, Shunsuke Yamamoto and colleagues discuss data suggesting that ADAM family proteins have important roles in the immune system.
Yasunori Higuchi +2 more
exaly +3 more sources
Sexual Selection and the Molecular Evolution of ADAM Proteins
Journal of Molecular Evolution, 2010Rapid evolution has been identified for many reproductive genes and recent studies have combined phylogenetic tests and information on species mating systems to test sexual selection. Here we examined the molecular evolution of the ADAM gene family, a diverse group of 35 proteins capable of adhesion to and cleavage of other proteins, using sequence ...
Alberto Civetta, Civetta Alberto
exaly +3 more sources
The ADAM gene family: surface proteins with adhesion and protease activity
Trends in Genetics, 2000An ADAM is a transmembrane protein that contains a disintegrin and metalloprotease domain and, therefore, it potentially has both cell adhesion and protease activities. Currently, the ADAM gene family has 29 members, although the function of most ADAM gene products is unknown.
Paul Primakoff, Diana G Myles
exaly +3 more sources
Journal of Clinical Neuroscience, 2004
ADAM proteins are a family of metalloproteinases with a disintegrin domain. They have proteolytic as well as adhesive functions and can be involved in cell fusion events. Some ADAM proteins are expressed in a highly tissue restricted fashion, whereas others are expressed quite ubiquitously. In the brain, ADAM proteins have a role in neural development,
exaly +3 more sources
ADAM proteins are a family of metalloproteinases with a disintegrin domain. They have proteolytic as well as adhesive functions and can be involved in cell fusion events. Some ADAM proteins are expressed in a highly tissue restricted fashion, whereas others are expressed quite ubiquitously. In the brain, ADAM proteins have a role in neural development,
exaly +3 more sources
Donn Adam Gito: Exploring The Non-Classical Properties of Proteins
A group of proteins can generate electrical charges under applied stress, a functional property known as piezoelectricity. Although, the fundamentals of piezoelectricity are based on inorganic crystals and not on organic materials. Hence, there is ambiguity in the relationship between the structure of the proteins and their piezoelectric response.
Donn Adam Gito (12290738)
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