about
Identification and characterization of three members of the human metallocarboxypeptidase gene familyNna1-like proteins are active metallocarboxypeptidases of a new and diverse M14 subfamilyThe structure of human prokallikrein 6 reveals a novel activation mechanism for the kallikrein familyFunctional segregation and emerging role of cilia-related cytosolic carboxypeptidases (CCPs)The cytosolic carboxypeptidases CCP2 and CCP3 catalyze posttranslational removal of acidic amino acidsNMR 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 hexapeptideThe NMR structure and dynamics of the two-domain tick carboxypeptidase inhibitor reveal flexibility in its free form and stiffness upon binding to human carboxypeptidase BDirect 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 pathwaysStructure of activated thrombin-activatable fibrinolysis inhibitor, a molecular link between coagulation and fibrinolysisThe molecular analysis of Trypanosoma cruzi metallocarboxypeptidase 1 provides insight into fold and substrate specificityMammalian metallopeptidase inhibition at the defense barrier of Ascaris parasiteAnalysis of a new crystal form of procarboxypeptidase B: further insights into the catalytic mechanismDeciphering the Structural Basis That Guides the Oxidative Folding of Leech-derived Tryptase InhibitorThe X-Ray Structure of Carboxypeptidase A Inhibited by a Thiirane Mechanism-Based InhibitorInsights into the molecular inactivation mechanism of human activated thrombin-activatable fibrinolysis inhibitorStructure-function analysis of the short splicing variant carboxypeptidase encoded by Drosophila melanogaster silverFlexibility of the Thrombin-activatable Fibrinolysis Inhibitor Pro-domain Enables Productive Binding of Protein SubstratesStructural and Functional Analysis of the Complex between Citrate and the Zinc Peptidase Carboxypeptidase AOxidative folding and structural analyses of a Kunitz-related inhibitor and its disulfide intermediates: functional implicationsCrystal Structure of Novel Metallocarboxypeptidase Inhibitor from Marine Mollusk Nerita versicolor in Complex with Human Carboxypeptidase A4The novel structure of a cytosolic M14 metallocarboxypeptidase (CCP) from Pseudomonas aeruginosa: a model for mammalian CCPsA noncanonical mechanism of carboxypeptidase inhibition revealed by the crystal structure of the Tri-Kunitz SmCI in complex with human CPA4Procarboxypeptidase in rat pancreas. Overall characterization and comparison of the activation processesA novel subfamily of mouse cytosolic carboxypeptidasesDetection 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.Short amino acid stretches can mediate amyloid formation in globular proteins: the Src homology 3 (SH3) case.Ligand screening by exoproteolysis and mass spectrometry in combination with computer modelling.Automated structure-based prediction of functional sites in proteins: applications to assessing the validity of inheriting protein function from homology in genome annotation and to protein docking.Structural similarity to link sequence space: new potential superfamilies and implications for structural genomics.Protein secondary structure and stability determined by combining exoproteolysis and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry.Prediction of the conformation and geometry of loops in globular proteins: testing ArchDB, a structural classification of loops.Self-assembly of human latexin into amyloid-like oligomers.Automated classification of antibody complementarity determining region 3 of the heavy chain (H3) loops into canonical forms and its application to protein structure prediction.Proteome-derived peptide libraries to study the substrate specificity profiles of carboxypeptidases.
P50
Q24292275-4950080C-F97C-44F0-B76F-16A6921CB817Q24294268-1F4AE2F4-6644-421B-A7A8-C9E3C7D9155CQ24297626-09CF28E4-2C39-4EE3-9F1B-61A752C9B52BQ24301396-7C920C85-202A-4C76-B68D-08F4DE66F765Q24301782-1F017D09-2838-4ED7-B756-A24B9566A3C0Q24649175-7F9109EE-5BD3-47D1-B428-9D669D4DD677Q24815235-1D6EDB46-41BE-46E6-BF61-C49C80C4F800Q27635551-6F0F49BD-D48A-4245-A56A-206C1FDF95B0Q27639463-6191E04B-A420-45CA-938F-25AB71E91D50Q27644800-F3DBF201-58D0-4B89-9B2F-C6F4DD10BAC4Q27650854-8A760EC8-4427-4580-B03E-410BC83E049AQ27650902-9E0A6C61-34DB-4690-BB65-3A7D02A891C6Q27651262-967E9B08-38A5-4332-812C-32AC9B83F427Q27651752-53CF6969-548B-4102-900D-69751448D84EQ27652153-CC35E6EA-D897-4434-B448-631ABA98FE36Q27653602-9064A6D2-C593-4BBA-A27A-A925EF72D02EQ27657663-0F37AACB-27F2-431F-B0F0-DF1CF5DAA144Q27657754-CA700D64-B81B-4CE5-877F-438E28963509Q27658086-D8305A31-8212-408B-88D0-07CA4923DC46Q27659054-7C7BD1F6-6690-4065-B08B-676C1F4C38DFQ27663043-9419310E-DB10-4AFB-BE9A-B6DBDE0B5B52Q27664776-3FEBE07C-8598-4721-A43B-C4D92A5DE10CQ27671316-97E4FC74-A82C-40DC-B3CF-3FBAE36A2245Q27675259-FFF9A934-CEB8-4E37-89FE-6DC01B3143EAQ27676977-02621E19-EC1A-4488-9057-D554B5B664E1Q27679349-58895BD6-CD2C-45D7-BAF7-A30ABB738EAAQ27684772-3C5A61A6-39E0-4862-92A6-2FE489DE1DB7Q28576937-492FD6E1-1FFA-472D-B954-E1C95B100518Q28594898-9420787F-B0B1-402D-9F6E-EBA4462AF0AEQ30158031-5E253FBC-EAB5-40AF-8DDD-BF98AAA9A18FQ30163872-CF5A849D-153A-4B08-AAAC-160AE2649C75Q30164098-55754DE7-8F45-4771-B05D-04AB75D18D1FQ30164621-999A280F-122C-4993-9522-7ECCE0FF9906Q30328488-45E28505-3F74-4431-81B5-333F68B53037Q30330199-D4DB2DFF-63A1-4995-8E3F-BC9DA660F449Q30331776-F42D37FB-8DC6-4B10-8C29-2B23DDB874ECQ30351051-BB67CBBF-8195-465C-A95E-29A655FA0517Q30365734-CDC1989B-787C-4E0A-921A-78F96CE449B9Q30430828-0D090A10-AC5C-4411-9CE4-CD7138EA063EQ30542279-F923F72F-531D-4B7B-A3DA-77704B380841
P50
description
hulumtues
@sq
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Francesc X Aviles
@nl
Francesc X Aviles
@sl
Francesc X. Aviles
@en
Francesc X. Aviles
@es
type
label
Francesc X Aviles
@nl
Francesc X Aviles
@sl
Francesc X. Aviles
@en
Francesc X. Aviles
@es
prefLabel
Francesc X Aviles
@nl
Francesc X Aviles
@sl
Francesc X. Aviles
@en
Francesc X. Aviles
@es
P106
P1153
7005688779
P21
P2456
P31
P3835
francesc-xavier-aviles
P496
0000-0002-1399-6789