A novel plasma proteinase potentiates alpha2-antiplasmin inhibition of fibrin digestion.
about
Neuropeptide Y, B-type natriuretic peptide, substance P and peptide YY are novel substrates of fibroblast activation protein-αThe effect of a single nucleotide polymorphism on human alpha 2-antiplasmin activityFibroblast activation protein α in tumor microenvironment: recent progression and implications (review)Fibrin stabilization (factor XIII), fibrin structure and thrombosisSelective inhibition of fibroblast activation protein protease based on dipeptide substrate specificity.Addition of a sequence from alpha2-antiplasmin transforms human serum albumin into a blood clot component that speeds clot lysisUsing substrate specificity of antiplasmin-cleaving enzyme for fibroblast activation protein inhibitor design.Circulating fibroblast activation protein activity and antigen levels correlate strongly when measured in liver disease and coronary heart disease.Noncovalent interaction of alpha(2)-antiplasmin with fibrin(ogen): localization of alpha(2)-antiplasmin-binding sites.Incorporation of albumin fusion proteins into fibrin clots in vitro and in vivo: comparison of different fusion motifs recognized by factor XIIIa.Fibroblast activation protein (FAP) is essential for the migration of bone marrow mesenchymal stem cells through RhoA activationEvaluating factor XIII specificity for glutamine-containing substrates using a matrix-assisted laser desorption/ionization time-of-flight mass spectrometry assay.Effect of fibroblast activation protein and alpha2-antiplasmin cleaving enzyme on collagen types I, III, and IV.Targeting carcinoma-associated fibroblasts within the tumor stroma with a fibroblast activation protein-activated prodrug.Circulating FGF21 proteolytic processing mediated by fibroblast activation protein.Targeting inhibition of fibroblast activation protein-α and prolyl oligopeptidase activities on cells common to metastatic tumor microenvironmentsQuantitation of fibroblast activation protein (FAP)-specific protease activity in mouse, baboon and human fluids and organs.The dipeptidyl peptidase IV family in cancer and cell biology.Hypofibrinolysis in diabetes: a therapeutic target for the reduction of cardiovascular risk.The plasmin-antiplasmin system: structural and functional aspects.Factor XIII: a coagulation factor with multiple plasmatic and cellular functions.Recent patents of dipeptidyl peptidase IV inhibitors.Fibroblast activation protein: A potential therapeutic target in cancer.Positional expression profiling indicates candidate genes in deletion hotspots of hepatocellular carcinoma.Unravelling the immunological roles of dipeptidyl peptidase 4 (DPP4) activity and/or structure homologue (DASH) proteins.Can Targeting Stroma Pave the Way to Enhanced Antitumor Immunity and Immunotherapy of Solid Tumors?The expression of proline-specific enzymes in the human lungEvidence that alpha2-antiplasmin becomes covalently ligated to plasma fibrinogen in the circulation: a new role for plasma factor XIII in fibrinolysis regulation.The antifibrinolytic function of factor XIII is exclusively expressed through α₂-antiplasmin cross-linking.Enhancement of fibrinolysis by inhibiting enzymatic cleavage of precursor α2-antiplasmin.A non-reactive glutamine residue of alpha2-antiplasmin promotes interactions with the factor XIII active site region.A fibrinogen concentrate Haemocomplettan (Riastap) or a Factor XIII concentrate Fibrogammin combined with a mini dose of tranexamic acid can reverse the fibrin instability to fibrinolysis induced by thrombin- or FXa-inhibitor.Peptide substrate profiling defines fibroblast activation protein as an endopeptidase of strict Gly(2)-Pro(1)-cleaving specificity.Why alpha-antiplasmin must be converted to a derivative form for optimal function.Fibroblast activation protein-α in fibrogenic disorders and cancer: more than a prolyl-specific peptidase?Generation and characterization of monoclonal antibodies against the N-terminus of alpha-2-antiplasmin.Increased N-terminal cleavage of alpha-2-antiplasmin in patients with liver cirrhosis.Inhibition of Fibrinolysis by Coagulation Factor XIII.Compaction of fibrin clots reveals the antifibrinolytic effect of factor XIII.
P2860
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P2860
A novel plasma proteinase potentiates alpha2-antiplasmin inhibition of fibrin digestion.
description
2004 nî lūn-bûn
@nan
2004 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
A novel plasma proteinase potentiates alpha2-antiplasmin inhibition of fibrin digestion.
@ast
A novel plasma proteinase potentiates alpha2-antiplasmin inhibition of fibrin digestion.
@en
A novel plasma proteinase potentiates alpha2-antiplasmin inhibition of fibrin digestion.
@nl
type
label
A novel plasma proteinase potentiates alpha2-antiplasmin inhibition of fibrin digestion.
@ast
A novel plasma proteinase potentiates alpha2-antiplasmin inhibition of fibrin digestion.
@en
A novel plasma proteinase potentiates alpha2-antiplasmin inhibition of fibrin digestion.
@nl
prefLabel
A novel plasma proteinase potentiates alpha2-antiplasmin inhibition of fibrin digestion.
@ast
A novel plasma proteinase potentiates alpha2-antiplasmin inhibition of fibrin digestion.
@en
A novel plasma proteinase potentiates alpha2-antiplasmin inhibition of fibrin digestion.
@nl
P2093
P1433
P1476
A novel plasma proteinase potentiates alpha2-antiplasmin inhibition of fibrin digestion.
@en
P2093
Kenneth W Jackson
Keun H Chung
Kyung N Lee
Patrick A McKee
Victoria J Christiansen
P304
P356
10.1182/BLOOD-2003-12-4240
P407
P577
2004-01-29T00:00:00Z