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The continuing saga of snake venom disintegrins
Toxicon, 2013Disintegrins, a family of polypeptides released in the venoms of viperid snakes (vipers and rattlesnakes) by the proteolytic processing of multidomain metalloproteinases, selectively block the function of β(1) and β(3) integrin receptors. Few of the proteins isolated and characterized from snake venoms have proven to be more structural and functional ...
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2010
Disintegrins represent a class of low molecular weight, Arg-Gly-Asp(RGD)/Lys-Gly-Asp(KGD)-containing, cysteine-rich polypeptides derived from venoms of various viper snakes. They bind to various integrins (e.g. αIIbβ3, αvβ3, α5β1 and others) expressed on cell membrane surface, with various degrees of affinity and specificity.
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Disintegrins represent a class of low molecular weight, Arg-Gly-Asp(RGD)/Lys-Gly-Asp(KGD)-containing, cysteine-rich polypeptides derived from venoms of various viper snakes. They bind to various integrins (e.g. αIIbβ3, αvβ3, α5β1 and others) expressed on cell membrane surface, with various degrees of affinity and specificity.
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Toxicon, 2001
The homodimeric disintegrin contortrostatin was compared directly to the monomeric disintegrins echistatin and flavoridin for the ability to affect protein tyrosine phosphorylation in tumor cells. It was observed that contortrostatin had a dramatic effect on the tyrosine phosphorylation status of several proteins in T24 human bladder cancer cells ...
Matthew R. Ritter, Francis S. Markland
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The homodimeric disintegrin contortrostatin was compared directly to the monomeric disintegrins echistatin and flavoridin for the ability to affect protein tyrosine phosphorylation in tumor cells. It was observed that contortrostatin had a dramatic effect on the tyrosine phosphorylation status of several proteins in T24 human bladder cancer cells ...
Matthew R. Ritter, Francis S. Markland
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Snake Venom Disintegrins: An Overview of their Interaction with Integrins
Current Drug Targets, 2019Disintegrins are non-enzymatic proteins that interfere on cell–cell interactions and signal transduction, contributing to the toxicity of snake venoms and play an essential role in envenomations. Most of their pharmacological and toxic effects are the result of the interaction of these molecules with cell surface ligands, which has been widely ...
Cesar, Pedro Henrique Souza +4 more
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Regulation of the proteolytic disintegrin metalloproteinases, the ‘Sheddases’
Seminars in Cell & Developmental Biology, 2009The proteolytically functional ADAMs, of which there are 13 in the human, play key roles in the way that many different types of cells respond to their environment. They act as 'signalling scissors' within various membrane environments, including at the cell surface, orchestrating rapid changes in the status of their transmembrane protein substrates ...
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Snake venom disintegrins: evolution of structure and function
Toxicon, 2005Disintegrins represent a family of polypeptides present in the venoms of various vipers that selectively block the function of integrin receptors. Here, we review our current view and hypothesis on the emergence and the structural and functional diversification of disintegrins by accelerated evolution and the selective loss of disulfide bonds of ...
Paula Juárez +7 more
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ADAMs, a disintegrin and metalloproteinases, mediate shedding of oxytocinase
Biochemical and Biophysical Research Communications, 2004Placental leucine aminopeptidase (P-LAP), a type-II transmembrane protease responsible for oxytocin degradation during pregnancy, is converted to a soluble form through proteolytic cleavage. The goal of this study was to determine the nature of the P-LAP secretase activity.
Norio Ito +7 more
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Inhibition of tumor formation by snake venom disintegrin
Toxicon, 2005The metastasis of tumor cells to bone involves migration, invasion and adhesion to bone. Breast and prostate cancer cells have predilection for spreading to bone. Snake venom-derived arginine-glycine-aspartic acid (RGD)-containing disintegrins (e.g. rhodostomin) have been demonstrated to inhibit cell adhesion.
Chih-Hsin Tang +6 more
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Contortrostatin, a Homodimeric Disintegrin, Binds to Integrin αvβ5
Biochemical and Biophysical Research Communications, 2000Contortrostatin is a homodimeric disintegrin from snake venom. We have shown that contortrostatin binds to integrins alphaIIbbeta3, alpha5beta1, and alphavbeta3. We now use several criteria to demonstrate the binding of contortrostatin to alphavbeta5.
Stephen Swenson +7 more
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Journal of the American Chemical Society, 2013
A disintegrin and metalloprotease-17 (ADAM17) is a major sheddase responsible for the regulation of a wide range of biological processes, like cellular differentiation, regeneration, or cancer progression. Hitherto, the mechanism regulating the enzymatic
Stefan Düsterhöft +6 more
semanticscholar +1 more source
A disintegrin and metalloprotease-17 (ADAM17) is a major sheddase responsible for the regulation of a wide range of biological processes, like cellular differentiation, regeneration, or cancer progression. Hitherto, the mechanism regulating the enzymatic
Stefan Düsterhöft +6 more
semanticscholar +1 more source