Search results for "For the Record"

showing 2 items of 2 documents

Amino acid sequence and homology modeling of obtustatin, a novel non-RGD-containing short disintegrin isolated from the venom of Vipera lebetina obtu…

2003

Disintegrins represent a group of cysteine-rich peptides occurring in Crotalidae and Viperidae snake venoms, and are potent antagonists of several integrin receptors. A novel disintegrin, obtustatin, was isolated from the venom of the Vipera lebetina obtusa viper, and represents the first potent and selective inhibitor of the binding of integrin alpha(1)beta(1) to collagen IV. The primary structure of obtustatin contains 41 amino acids and is the shortest disintegrin described to date. Obtustatin shares the pattern of cysteines of other short disintegrins. However, in contrast to known short disintegrins, the integrin-binding loop of obtustatin is two residues shorter and does not express t…

chemistry.chemical_classificationModels MolecularbiologyDisintegrinsMolecular Sequence DataProtein primary structureVenomViper VenomsViper VenomsBiochemistryAmino acidBiochemistrychemistryViperidaebiology.animalFor the RecordDisintegrinbiology.proteinViperidaeAnimalsHomology modelingAmino Acid SequenceMolecular BiologyPeptide sequenceOligopeptides
researchProduct

The kinetic behavior of insulin fibrillation is determined by heterogeneous nucleation pathways

2005

When subjected to acidic conditions and high temperature, insulin is known to produce fibrils that display the common properties of disease amyloids. Thus, clarifying the mechanisms of insulin fibrillation can help the general understanding of amyloidal aggregation. Insulin fibrillation exhibits a very sharp time dependence, with a pronounced lag phase and subsequent explosive growth of amyloidal aggregates. Here we show that the initial stages of this process can be well described by exponential growth of the fibrillated proteins. This indicates that the process is mainly controlled by a secondary nucleation pathway.

AmyloidProtein DenaturationTime FactorsAmyloidmedicine.medical_treatmentKineticsNucleationmacromolecular substancesProtein aggregationFibrilBiochemistryExponential growthmedicineAnimalsInsulinMolecular BiologyFibrillationChemistryInsulinTemperatureHydrogen-Ion ConcentrationKineticsBiochemistryFor the RecordBiophysicsCattlemedicine.symptomProtein Science
researchProduct