about
Advances in translational bioinformatics: computational approaches for the hunting of disease genesMolecular and biochemical trajectories from diabetes to Alzheimer's disease: A critical appraisalWrecked regulation of intrinsically disordered proteins in diseases: pathogenicity of deregulated regulatorsRapid Brownian Motion Primes Ultrafast Reconstruction of Intrinsically Disordered Phe-Gly Repeats Inside the Nuclear Pore Complex.The unfoldomics decade: an update on intrinsically disordered proteins.DisoMCS: Accurately Predicting Protein Intrinsically Disordered Regions Using a Multi-Class Conservative Score Approach.Correlating disease-related mutations to their effect on protein stability: a large-scale analysis of the human proteome.High-throughput characterization of intrinsic disorder in proteins from the Protein Structure Initiative.At low concentrations, 3,4-dihydroxyphenylacetic acid (DOPAC) binds non-covalently to alpha-synuclein and prevents its fibrillationInsights into the regulation of intrinsically disordered proteins in the human proteome by analyzing sequence and gene expression data.Protein disorder in the human diseasome: unfoldomics of human genetic diseases.Pathological unfoldomics of uncontrolled chaos: intrinsically disordered proteins and human diseasesIn-silico prediction of disorder content using hybrid sequence representation.Single molecule characterization of α-synuclein in aggregation-prone states.Insights into the evolutionary features of human neurodegenerative diseases.Discordant and chameleon sequences: their distribution and implications for amyloidogenicity.Use of a small peptide fragment as an inhibitor of insulin fibrillation process: a study by high and low resolution spectroscopyStructural analysis of peptide-analogues of human Zona Pellucida ZP1 protein with amyloidogenic properties: insights into mammalian Zona Pellucida formationOpposing effects of glutamine and asparagine govern prion formation by intrinsically disordered proteins.De novo design and experimental characterization of ultrashort self-associating peptidesComputational modeling of the relationship between amyloid and disease.Effect of methionine oxidation on the structural properties, conformational stability, and aggregation of immunoglobulin light chain LEN.Guiding protein aggregation with macromolecular crowdingShedding light on protein folding landscapes by single-molecule fluorescence.Protein intrinsic disorder and oligomericity in cell signaling.Finding order within disorder: elucidating the structure of proteins associated with neurodegenerative disease.Role of metal ions in aggregation of intrinsically disordered proteins in neurodegenerative diseases.Protein intrinsic disorder as a flexible armor and a weapon of HIV-1.Chain collapse of an amyloidogenic intrinsically disordered protein.Sensing Tryptophan Microenvironment of Amyloid Protein Utilizing Wavelength-Selective Fluorescence Approach.MFDp2: Accurate predictor of disorder in proteins by fusion of disorder probabilities, content and profiles.The intrinsically disordered N-terminal region of AtREM1.3 remorin protein mediates protein-protein interactions.The SCHOOL of nature: II. Protein order, disorder and oligomericity in transmembrane signaling.Human stefin B normal and patho-physiological role: molecular and cellular aspects of amyloid-type aggregation of certain EPM1 mutants.Unusual biophysics of immune signaling-related intrinsically disordered proteins.Aging and neurogenesis, a lesion from Alzheimer's disease.On the intrinsic disorder status of the major players in programmed cell death pathways.Suppression of amyloid fibrils using the GroEL apical domain.Orthogonal high-throughput thermal scanning method for rank ordering protein formulations.The role of intrinsically unstructured proteins in neurodegenerative diseases.
P2860
Q24642050-E1A6D6F2-4FD7-451A-A3EC-D9B8A7FFB16AQ26783344-74ABAF9A-6D85-4472-A697-9D8F5436252CQ27000495-A8AACE33-CF3A-46A0-AD16-083FB1A25710Q27324789-3585FCAE-1C72-41A4-BA6E-A8142433FB31Q30372413-C2EF69AC-6976-4CA9-964F-43579B2CBF17Q30375859-917EAB97-AFBB-49BF-845D-23476D4AF352Q30406158-9644405E-39E5-4AA7-B7AD-E356D0B9807CQ30417432-E158F5F7-5D00-4611-88F0-5A0491D16813Q30481562-97DD9B55-68BD-4AC9-AC7D-7C69131E331EQ33443462-1B117F1A-1402-43F0-B5B5-CCD9FC8DF1D7Q33481211-289D3505-00BF-4AAB-BE36-7D02EB217438Q33909288-4F7C121A-17A3-40C5-996D-8849947EBC70Q33935454-265FAD40-3B27-451C-AB1E-55E33174121BQ34250768-D6E27CE9-6D57-43B5-8EAF-6264DA374BEBQ34465001-2E46CF72-22DB-4732-99C9-BF09889F2782Q34724075-935199F5-425E-4348-B552-94DD1F5D01B9Q34979518-4FA9A22D-768B-4D5F-9081-9852EB0C681CQ34998612-EB2BB80C-A01D-48C3-AA77-655AB3F62222Q35094005-FE9663CE-A0E9-4A3E-9261-A4F0450D0D4EQ35204571-A788C3CA-F6A4-42AF-98F0-5F0F49B9525DQ36677013-11982D49-EDF6-4699-884C-CEBE7199B485Q37178747-8F9AD273-0EF2-4054-A243-ED627397D252Q37178759-C5931B01-53C5-4E4B-91E3-0F6D1081FEF8Q37645549-9208AA65-2C5A-4CBA-B121-470B1D8D1672Q37696321-3CA3DC9A-BC5E-47DD-9EF6-6BCBB153A2DCQ37855889-D73ABE5C-F802-49B2-AFC1-57D436461F11Q37922607-24C8B561-B166-4DEE-B8B5-BE52A22B73C8Q37950254-E6FB493B-3FCA-4659-BA87-A43D26EAC4CAQ38597911-0DAA88C7-A066-499E-BD49-9A1FF36E3474Q38688729-FA1D7B04-0411-4DC6-919A-CA3A1D79E7ACQ38779764-59B25496-E947-4141-8B75-723E1C04A91FQ41462823-2423E745-6F70-4C77-8739-8170822FA4E9Q41768887-A2E67BDE-38BA-4C03-A82A-557092016A87Q41840051-DF9178A0-DCE3-4811-8C29-AD20C99C71C0Q41864976-98A06AE1-B555-4679-98EA-355D5FDC869CQ41877527-C6DB0570-8112-4070-99F3-CE24C99BA214Q41906667-D9D91D5B-175F-4C3F-89AC-D520699814A6Q41907342-B8EAEB03-674C-4A0E-A4C0-4B7DF8EE103CQ41951670-6949BC14-C4C0-4C81-A09A-D7D2BC934DE5Q42174981-6F65997F-2292-4F25-B69C-3E7A957630C8
P2860
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on June 2008
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Amyloidogenesis of natively unfolded proteins.
@en
Amyloidogenesis of natively unfolded proteins.
@nl
type
label
Amyloidogenesis of natively unfolded proteins.
@en
Amyloidogenesis of natively unfolded proteins.
@nl
prefLabel
Amyloidogenesis of natively unfolded proteins.
@en
Amyloidogenesis of natively unfolded proteins.
@nl
P2860
P1476
Amyloidogenesis of natively unfolded proteins.
@en
P2860
P304
P356
10.2174/156720508784533312
P577
2008-06-01T00:00:00Z