about
Aggregation as bacterial inclusion bodies does not imply inactivation of enzymes and fluorescent proteinsConformational strain in the hydrophobic core and its implications for protein folding and designStructure and dynamics of the potato carboxypeptidase inhibitor by 1H and 15N NMRDirect interaction between a human digestive protease and the mucoadhesive poly(acrylic acid)The NMR structures of the major intermediates of the two-domain tick carboxypeptidase inhibitor reveal symmetry in its folding and unfolding pathwaysDeciphering the Structural Basis That Guides the Oxidative Folding of Leech-derived Tryptase InhibitorAmyloid properties of the leader peptide of variant B cystatin C: implications for Alzheimer and macular degenerationHuman stefin B role in cell's response to misfolded proteins and autophagySpecific Hsp100 Chaperones Determine the Fate of the First Enzyme of the Plastidial Isoprenoid Pathway for Either Refolding or Degradation by the Stromal Clp Protease in ArabidopsisProcarboxypeptidase in rat pancreas. Overall characterization and comparison of the activation processesMultiple β-sheet molecular dynamics of amyloid formation from two ABl-SH3 domain peptides.Contribution of disulfide bonds to stability, folding, and amyloid fibril formation: the PI3-SH3 domain case.The in vivo and in vitro aggregation properties of globular proteins correlate with their conformational stability: the SH3 case.Detection of transient protein-protein interactions by bimolecular fluorescence complementation: the Abl-SH3 case.Amyloid fibril formation by a partially structured intermediate state of alpha-chymotrypsin.Folding specificity induced by loop stiffnessInsights into the origin of the tendency of the PI3-SH3 domain to form amyloid fibrils.Self-assembly of human latexin into amyloid-like oligomers.AGGRESCAN3D (A3D): server for prediction of aggregation properties of protein structures.Data on correlation between Aβ42 structural aggregation propensity and toxicity in bacteria.Study and selection of in vivo protein interactions by coupling bimolecular fluorescence complementation and flow cytometry.Folding of small disulfide-rich proteins: clarifying the puzzle.Amyloidogenic regions and interaction surfaces overlap in globular proteins related to conformational diseases.Protein aggregation profile of the bacterial cytosol.Amyloid-like protein inclusions in tobacco transgenic plants.Linking amyloid protein aggregation and yeast survival.Discovery of novel inhibitors of amyloid β-peptide 1-42 aggregation.Detailed molecular comparison between the inhibition mode of A/B-type carboxypeptidases in the zymogen state and by the endogenous inhibitor latexin.DisProt 7.0: a major update of the database of disordered proteins.The N-terminal helix controls the transition between the soluble and amyloid states of an FF domainStructure-based analysis of A19D, a variant of transthyretin involved in familial amyloid cardiomyopathy.What makes a protein sequence a prion?Intradomain Confinement of Disulfides in the Folding of Two Consecutive Modules of the LDL ReceptorDesigning proteins from the inside out.A fast and specific method to screen for intracellular amyloid inhibitors using bacterial model systems.Benzbromarone, Quercetin, and Folic Acid Inhibit Amylin AggregationStaphylococcal Bap Proteins Build Amyloid Scaffold Biofilm Matrices in Response to Environmental Signals.High-Throughput Screening Methodology to Identify Alpha-Synuclein Aggregation Inhibitors.Protein quality in bacterial inclusion bodies.Repositioning tolcapone as a potent inhibitor of transthyretin amyloidogenesis and associated cellular toxicity.
P50
Q24815513-44F04D5C-4C38-43E0-831E-64412BA74D45Q27638976-C2F3B16D-C811-4911-B399-278F2FB3E5E3Q27640399-55D9C620-BBC3-43D1-9CF8-19586BE9722CQ27650902-98DACEE1-001D-4674-AA2E-10F2147570B8Q27651262-C720F3BF-5025-40AB-BEAC-89DC4111D33DQ27657754-CFE7CD3F-1F79-428E-996C-BC263B7D5E02Q28118595-87C45FD0-864C-48E2-9932-AA266840BE23Q28540970-41ACBF3C-4F01-434A-B26B-193DBE98DA01Q28552929-7DAA3264-86FA-4349-809C-D93E36C04198Q28576937-1E08625E-E798-4093-A252-206EA4140E2EQ30009967-F3D42ADF-FC0E-4DCE-82B9-9CF28CD32E3BQ30010266-90EFDFF3-5BAD-4B78-9866-7ED40D31DA97Q30157694-DF576F61-4112-49FF-AF3E-C707295CA87CQ30158031-382A70FA-D07E-4053-82E3-DFCA1D963F70Q30163872-DF502165-FAA4-4B42-90A3-5A8EDE08F440Q30164658-C72A6295-E83A-43C8-B5CB-43A263EB4923Q30165168-ABE5D648-BE9B-41D8-8F76-45576A44DB79Q30365734-E94521D4-FF6E-4F6E-A47C-C855EEF9E2AAQ30373803-A4B35CE2-1D16-47D2-8AFA-71C8A120CC0EQ31114259-2B6B643A-CA4F-4B0A-8CB0-8B7CB1B06041Q33314548-60ABE42F-D55C-449E-A052-A49CFDB765A3Q33342293-887E9A06-13EE-4CCC-803D-E67913FA21D9Q33495551-C37D6BE0-7793-4814-BD6E-2D6695E8F9DEQ33535929-0694D9B3-868F-4AF2-9372-7825AAE6FFCFQ33535929-75A6D68B-E7CF-4A07-BA42-3E5D12245E14Q33737666-981B4259-A6E9-4D9E-8F83-8A802C852C21Q33794914-3EA13FE7-8C52-4429-A4F2-EE64BED2535EQ34420890-529B5EE0-073F-49B8-A9A8-83D56A2E78A1Q34441836-B3270F31-99D3-4E17-AE18-A5B9420638E1Q34546157-B5C8070C-977D-4604-BC11-45562668FEEDQ34625713-5DEFB429-1DA8-4768-AB13-533F33D39BAAQ35072784-5733DBD2-A09D-42BD-ABB2-47E4D73D02BBQ35539958-D4E3948E-2F87-4605-919E-FFA6C92A143EQ35689620-FCE1C1FF-EEB6-4D10-8FB4-07C6FAA0123EQ35783481-13CE85C5-7008-46F0-A942-0E2BED27A0ABQ35853137-3AF6D05E-A145-47EC-880D-51B4FDE27320Q36056679-E3728365-7399-4404-B8D6-B6855B65AB05Q36057962-0018993A-1115-4B80-91FA-F2DC32261266Q36296440-48C90785-0926-422C-B156-5ACEB198BFC7Q36406887-42A6690D-A9BB-4C75-9CAD-AD3C4E5F88E9
P50
description
hulumtues
@sq
researcher
@en
ricercatore
@it
wetenschapper
@nl
հետազոտող
@hy
name
Salvador Ventura
@ast
Salvador Ventura
@en
Salvador Ventura
@es
Salvador Ventura
@nl
Salvador Ventura
@sl
type
label
Salvador Ventura
@ast
Salvador Ventura
@en
Salvador Ventura
@es
Salvador Ventura
@nl
Salvador Ventura
@sl
prefLabel
Salvador Ventura
@ast
Salvador Ventura
@en
Salvador Ventura
@es
Salvador Ventura
@nl
Salvador Ventura
@sl
P214
P1053
C-7021-2008
P106
P21
P214
P2456
P2798
P31
P3829
P496
0000-0002-9652-6351
P734
P735
P7859
viaf-304932702