about
tert-butyl N-[2-[N-(N, N'-dicyclohexylureidocarbonylethyl)carbamoyl]prop-2-yl]carbamate.Bacterial inclusion bodies contain amyloid-like structureElucidating the role of disulfide bond on amyloid formation and fibril reversibility of somatostatin-14: relevance to its storage and secretionMolecular interpretation of ACTH-β-endorphin coaggregation: relevance to secretory granule biogenesisIn vivo demonstration that alpha-synuclein oligomers are toxic.Familial Parkinson disease-associated mutations alter the site-specific microenvironment and dynamics of α-synuclein.Cytotoxic helix-rich oligomer formation by melittin and pancreatic polypeptideFunctional genetic variants of the catecholamine-release-inhibitory peptide catestatin in an Indian population: allele-specific effects on metabolic traits.Cell Adhesion on Amyloid Fibrils Lacking Integrin Recognition Motif.Amyloid formation of growth hormone in presence of zinc: Relevance to its storage in secretory granulesThe fold of alpha-synuclein fibrils.Amino acid position-specific contributions to amyloid beta-protein oligomerization.Structure-activity relationship of amyloid fibrils.Naturally occurring variants of the dysglycemic peptide pancreastatin: differential potencies for multiple cellular functions and structure-function correlation.A minimal conformational switching-dependent model for amyloid self-assembly.Evidence of a prion-like transmission of p53 amyloid in Saccharomyces cerevisiae.Alteration of Structure and Aggregation of a-Synuclein by Familial Parkinson's Disease Associated Mutations.Self healing hydrogels composed of amyloid nano fibrils for cell culture and stem cell differentiation.Structure based aggregation studies reveal the presence of helix-rich intermediate during α-Synuclein aggregation.α-synuclein aggregation and its modulation.Site-specific structural dynamics of α-Synuclein revealed by time-resolved fluorescence spectroscopy: a review.Curcumin modulates α-synuclein aggregation and toxicity.Effect of curcumin analogs onα-synuclein aggregation and cytotoxicity.Influence of retinoic acid on mesenchymal stem cell differentiation in amyloid hydrogels.Mistic: cellular localization, solution behavior, polymerization, and fibril formationThe Parkinson's disease-associated H50Q mutation accelerates α-Synuclein aggregation in vitro.Comparison of α-Synuclein Fibril Inhibition by Four Different Amyloid Inhibitors.p53 amyloid formation leading to its loss of function: implications in cancer pathogenesis.Site-specific fluorescence dynamics of α-synuclein fibrils using time-resolved fluorescence studies: effect of familial Parkinson's disease-associated mutations.Complexation of amyloid fibrils with charged conjugated polymers.Distinct structural and functional roles of conserved residues in the first extracellular domain of receptors for corticotropin-releasing factor and related G-protein-coupled receptors.Complexation of NAC derived peptide ligands with C-terminus of α-synuclein accelerates its aggregation.Controlled Exposure of Bioactive Growth Factor in 3D Amyloid Hydrogel for Stem Cells Differentiation.Investigating the intrinsic aggregation potential of evolutionarily conserved segments in p53.Differential copper binding to alpha-synuclein and its disease-associated mutants affect the aggregation and amyloid formation.Defining a physical basis for diversity in protein self-assemblies using a minimal model.A magnet-actuated biomimetic device for isolating biological entities in microwellsMolecular interactions of the physiological anti-hypertensive peptide catestatin with the neuronal nicotinic acetylcholine receptorGlycosaminoglycans have variable effects on α-synuclein aggregation and differentially affect the activities of the resulting amyloid fibrilsThe newly discovered Parkinson's disease associated Finnish mutation (A53E) attenuates α-synuclein aggregation and membrane binding
P50
Q31440202-E619BF6A-A351-4FAE-8B1B-5F6593FDFA8EQ33358275-C7400337-7544-4710-99AE-D73A7D02E7E9Q33761231-83D8EF1E-5D02-4755-9DE4-F8A55ECF5C37Q34189316-7108F008-7CA3-4202-A38F-289B0701490CQ34652122-6DF50FFE-4718-4D87-A7C3-DA313331A22CQ35199433-C1903601-22BE-4D8A-A569-071F50613DA0Q35585206-FD94F017-8E4C-4775-8A1F-B4979697A286Q36481887-63FA5F6E-8E2D-4ED0-943A-03D355E4FABAQ36650385-7FA8D34F-DCFE-42E8-A9C0-1DC617ABA3C1Q36719261-DAF2848C-A2B4-4920-812B-3AABC2DAC0FFQ36735295-F0DE2185-2A0A-4D07-8F98-E71F9AF31DADQ37358158-32582DB3-3C18-43C7-AB8A-A1FE58019B90Q37549331-D1E8E778-D40F-43E9-B6FD-E858BD9E7492Q37583609-61008F2F-B45C-48F3-9889-5DC24998BF98Q38528499-51383A51-0D9E-43EB-BCDE-7F5491F331BEQ38718360-6838C50B-98F1-4556-BCE2-C3F9924D63B1Q38773110-FEE40969-F866-4085-8E23-E6D13A15045BQ38883078-6273D0DD-97BC-4563-B7C7-EAF31EDE6E2AQ38898283-48657F00-5488-4C92-8F37-BDE4554FE116Q38979838-F2EDC154-1537-4B8E-B917-DF245F852022Q39133493-6FE3219A-B545-449B-B725-7C30BBA7B189Q39178579-763E5FE7-9490-45CC-82AD-A6A63B06363DQ39659132-2DF7B230-7E33-405A-A061-9EB32CA123D2Q40133621-6F447A7D-430A-42C3-8A64-9739FEA6B902Q42063399-26128AA7-E450-4E0F-B50E-3B5B3646A7A9Q43977429-B994528B-4C7A-45F5-84F5-A5871CFAAA98Q46312110-717AEDF6-23EE-4177-B7CB-5342CCD04ECEQ46345550-BD6A4993-FDD4-483F-9AA3-175733200263Q46643028-613F6194-DA8E-4E38-A3C4-085233FA7F84Q46912921-87D9B8BA-AE62-4039-923D-0C74F8A42774Q46947611-DABD4BB8-DA62-4B84-A6DF-C970BDB67634Q47245456-56E5DEED-83D9-4B89-8840-1B9522D181F1Q47889447-81851F88-610A-466C-B583-37B721FC2168Q51044625-89AEE73B-E61E-4B8C-A2E1-EDBE1527F639Q51286153-CF9B08CE-AAFA-451E-8A71-1A22D9ACBDA9Q51444398-02928AA5-7032-485D-8A2F-469EAC355BB4Q58708252-15EB1182-E1C3-4A29-9099-DDEEBC2C8E50Q63384541-804DB45C-D504-45DE-BD97-8528693AFA13Q64866213-27F0A3DD-E9C4-431A-997D-32D7BC181AA0Q85652193-BAC71C27-C6FC-4FA1-9470-5045158DCD41
P50
description
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Samir K Maji
@ast
Samir K Maji
@en
Samir K Maji
@es
Samir K Maji
@nl
type
label
Samir K Maji
@ast
Samir K Maji
@en
Samir K Maji
@es
Samir K Maji
@nl
prefLabel
Samir K Maji
@ast
Samir K Maji
@en
Samir K Maji
@es
Samir K Maji
@nl
P106
P1153
6701745986
P31
P496
0000-0002-9110-1565