about
Identification and characterization of three members of the human metallocarboxypeptidase gene familyNMR solution structure of the activation domain of human procarboxypeptidase A2Prediction of "hot spots" of aggregation in disease-linked polypeptidesCrystal structure of a novel mid-gut procarboxypeptidase from the cotton pest Helicoverpa armigeraHuman procarboxypeptidase B: three-dimensional structure and implications for thrombin-activatable fibrinolysis inhibitor (TAFI)Caught after the Act: a human A-type metallocarboxypeptidase in a product complex with a cleaved hexapeptideDirect interaction between a human digestive protease and the mucoadhesive poly(acrylic acid)Analysis of a new crystal form of procarboxypeptidase B: further insights into the catalytic mechanismThe X-Ray Structure of Carboxypeptidase A Inhibited by a Thiirane Mechanism-Based InhibitorStructural and Functional Analysis of the Complex between Citrate and the Zinc Peptidase Carboxypeptidase AA functional and structural study of the major metalloprotease secreted by the pathogenic fungus Aspergillus fumigatusAmyloid fibril formation by a partially structured intermediate state of alpha-chymotrypsin.Self-assembly of human latexin into amyloid-like oligomers.Procarboxypeptidase A from the insect pest Helicoverpa armigera and its derived enzyme. Two forms with new functional properties.AGGRESCAN: a server for the prediction and evaluation of "hot spots" of aggregation in polypeptides.Linking amyloid protein aggregation and yeast survival.Structure of human carboxypeptidase A4 with its endogenous protein inhibitor, latexin.Structural basis of the resistance of an insect carboxypeptidase to plant protease inhibitorsDetailed molecular comparison between the inhibition mode of A/B-type carboxypeptidases in the zymogen state and by the endogenous inhibitor latexin.Progress in metallocarboxypeptidases and their small molecular weight inhibitors.Mutagenesis of the central hydrophobic cluster in Abeta42 Alzheimer's peptide. Side-chain properties correlate with aggregation propensities.A new type of five-membered heterocyclic inhibitors of basic metallocarboxypeptidases.Response of the digestive system of Helicoverpa zea to ingestion of potato carboxypeptidase inhibitor and characterization of an uninhibited carboxypeptidase B.Ile-phe dipeptide self-assembly: clues to amyloid formation.The unfolding pathway of leech carboxypeptidase inhibitor.The crystal structure of thrombin-activable fibrinolysis inhibitor (TAFI) provides the structural basis for its intrinsic activity and the short half-life of TAFIa.Major kinetic traps for the oxidative folding of leech carboxypeptidase inhibitor.Aromatic organic compounds as scaffolds for metallocarboxypeptidase inhibitor design.Design, selection, and characterization of thioflavin-based intercalation compounds with metal chelating properties for application in Alzheimer's disease.Thioxophosphoranyl aryl- and heteroaryloxiranes as the representants of a new class of metallocarboxypeptidase inhibitors.Secondary binding site of the potato carboxypeptidase inhibitor. Contribution to its structure, folding, and biological properties.Cyclobutane-containing peptides: evaluation as novel metallocarboxypeptidase inhibitors and modelling of their mode of action.Discovery of Mechanism-Based Inactivators for Human Pancreatic Carboxypeptidase A from a Focused Synthetic Library.Structural and functional characterization of binding sites in metallocarboxypeptidases based on Optimal Docking Area analysis.Carboxypeptidase BInsect Gut Carboxypeptidase 3
P50
Q24292275-C49BD174-D9B9-4109-9B51-C11BCF68C87FQ24649175-B2167B04-9BF3-458D-A0DC-C6DF1C85EF23Q24815235-6566288E-8479-4E2B-86B2-0BD6C998A2F5Q27635551-4266C0C0-D682-48B2-BF12-2C157683CC2CQ27639463-309406CB-DA43-4251-AB5D-190F3BE7A334Q27644800-7145446F-2364-4E6E-8A32-682400D0C257Q27650902-10C64106-4F53-4CF9-A69D-FCEDD26F466FQ27657663-5691B7B9-3636-48E6-9631-C04D3ACB801AQ27658086-6A2C167B-042E-45F1-B62E-682DC298CE55Q27671316-37CF6EC7-2151-4B97-A303-F3BA47F3C25BQ27686974-ABEBE75C-7B5C-491F-9F6D-98A695CA6582Q30163872-C5472AF0-B43A-464C-93CC-857011041456Q30365734-ECE54189-B17B-4B44-B68B-644DC1C125B0Q30959379-3837233A-F7EE-4A6E-B5DD-4AF42F213588Q33275645-A45D6969-6F79-4928-A69A-53EFA80C4ACDQ33794914-E4C90654-F7D8-4BFB-A47E-6617C6E383C0Q33932645-56996668-A45E-4E43-AF43-1BADBD108AD8Q34133226-829F8716-8BCD-405C-B3E8-E81BE42836F1Q34441836-375133B9-A4C0-4B0E-B203-9546C7B310F2Q37751100-BD63DF12-6EF3-47C9-8FDF-5240E1FB1BCFQ40328062-F55F9662-22D7-49F4-B904-DAA2A90ED031Q42025624-978B5678-B1C2-4DF9-B333-FFC654D63B30Q42036564-8C27139F-61D5-496A-904B-41DF2B9807A4Q42117835-66F644BF-6E4C-4E11-8307-4638348467E8Q42672161-5D4E8F9D-B9EE-4A2D-9E02-AE14C8EE70CCQ43154963-1CBD42BA-995D-4F9A-9405-F4DAA570E57CQ44461322-EFDDA3AE-D416-490B-8EE7-DD6DBA462074Q46157708-EEB852BE-3BD4-49B0-A096-39809DC146A6Q46169343-4A0CA670-D079-4155-86CE-70C4661991E3Q46658417-BDE8463C-8BD1-49B6-93A6-BD1D08BE93D0Q47347379-2FF638E3-1265-436D-B97B-E17222149A58Q47886921-882F171E-730C-4FD5-8076-7A0F70C7E9DDQ50066125-C9E27041-E1A6-4D2E-8E1B-EC4F061262A3Q52678573-3067FAD9-75DB-4E02-B615-0ED06DD32807Q57956708-1C24A396-5638-4950-972E-3F9CFE0B1583Q57956711-1F4162E4-FE8A-466D-8C35-47603B49BD5C
P50
description
Spaans onderzoeker
@nl
hulumtues
@sq
researcher
@en
taighdeoir
@ga
հետազոտող
@hy
name
Josep Vendrell
@ast
Josep Vendrell
@en
Josep Vendrell
@es
Josep Vendrell
@ga
Josep Vendrell
@nl
Josep Vendrell
@sl
type
label
Josep Vendrell
@ast
Josep Vendrell
@en
Josep Vendrell
@es
Josep Vendrell
@ga
Josep Vendrell
@nl
Josep Vendrell
@sl
prefLabel
Josep Vendrell
@ast
Josep Vendrell
@en
Josep Vendrell
@es
Josep Vendrell
@ga
Josep Vendrell
@nl
Josep Vendrell
@sl
P1053
A-6731-2010
P106
P21
P27
P31
P3829
P496
0000-0002-9378-4742