Enolase as a plasminogen binding protein in Leishmania mexicana
about
Proteomic analysis of the secretome of Leishmania donovaniThe site of the bite: Leishmania interaction with macrophages, neutrophils and the extracellular matrix in the dermisA hypothetical model of crossing Bombyx mori nucleopolyhedrovirus through its host midgut physical barrierPhysical Features of Intracellular Proteins that Moonlight on the Cell SurfaceCarbon partitioning in green algae (chlorophyta) and the enolase enzymeSurface-expressed enolase contributes to the pathogenesis of clinical isolate SSU of Aeromonas hydrophilaThe interaction of canine plasminogen with Streptococcus pyogenes enolase: they bind to one another but what is the nature of the structures involved?Immunodominant antigens of Leishmania chagasi associated with protection against human visceral leishmaniasis.The oligopeptidase B of Leishmania regulates parasite enolase and immune evasion.Definition of the extracellular proteome of pathogenic-phase Histoplasma capsulatumEnolase: a key player in the metabolism and a probable virulence factor of trypanosomatid parasites-perspectives for its use as a therapeutic target.Alterations of protein expression in conditions of copper-deprivation for Paracoccidioides lutzii in the presence of extracellular matrix components.Seahorse-derived peptide suppresses invasive migration of HT1080 fibrosarcoma cells by competing with intracellular α-enolase for plasminogen binding and inhibiting uPA-mediated activation of plasminogenSaliva from nymph and adult females of Haemaphysalis longicornis: a proteomic studyExternalized glycolytic enzymes are novel, conserved, and early biomarkers of apoptosisUnique behavior of Trypanosoma cruzi mevalonate kinase: A conserved glycosomal enzyme involved in host cell invasion and signalingMoonlighting enzymes in parasitic protozoa.Complete Molecular and Immunoprotective Characterization of Babesia microti Enolase.Glycobiology of the Leishmania parasite and emerging targets for antileishmanial drug discovery.An introduction to protein moonlighting.Exploiting death: apoptotic immunity in microbial pathogenesis.Importance of enolase in Giardia lamblia differentiation.RNAi-mediated silencing of enolase confirms its biological importance in Clonorchis sinensis.A New Trick for a Conserved Enzyme: Mevalonate Kinase, a Glycosomal Enzyme, Can Be Secreted by Trypanosoma cruzi and Modulate Cell Invasion and Signaling. Is It Another Moonlighting Enzyme?Extracellular matrix degradation via enolase/plasminogen interaction: Evidence for a mechanism conserved in Metazoa.Protein moonlighting: what is it, and why is it important?Enolase of Angiostrongylus cantonensis: more likely a structural component?Serodiagnostic Potential of Alpha-Enolase From Sarcoptes scabiei and Its Possible Role in Host-Mite Interactions.Development of a Nanobody-based lateral flow assay to detect active Trypanosoma congolense infections.Plasminogen-binding proteins as an evasion mechanism of the host's innate immunity in infectious diseases
P2860
Q21184106-0F14D12B-65F0-405B-9182-1AD6B475BE83Q26752781-01EB8F95-BD91-4806-8F32-316615F967DAQ28542703-08D1AE2F-1A90-419E-89F5-8A42558810BDQ28545748-EF7680F4-66B5-4552-9BC9-A05A05837C98Q28654779-582251A1-F913-4CFE-AFC2-4CD9E29DEC11Q28910346-1A6D6977-A712-4A4A-9F8D-C21D4169777CQ34103104-5217597F-0376-4083-8411-2BC52916AD54Q34314499-0ECFADEB-D97B-41E1-BB15-84EA2B9DC747Q34452594-82837614-D9A1-415E-B32E-1D84D354F65CQ34754597-8B5AB1C1-DB9F-43DD-9B1B-76CAEEC629D4Q34975047-AF53AC26-22B9-4499-93D9-9CFA2E15ADA9Q34998179-21F11D99-6F9F-4A31-850F-A583B3A0AC5CQ35134419-871F8D6F-9EEB-4FEA-899B-F6C8970E83CBQ35794429-A8BD9137-9A97-4E58-AE1D-BCAA993797C6Q35880023-2E86AA93-E105-46A2-8E1B-B85694EB32CAQ36835636-B38AD9FC-07BC-46CD-88FD-73E2A07BD454Q37710181-35DE3A5E-6478-4E6C-BCA5-48BD0D7FFBC2Q37747000-6948FF81-5727-40F0-AD0F-A1C68946FB60Q37763950-E8639927-8ED4-4728-9291-1412CD7D4337Q38268468-EFA1A7A3-7333-4867-ACEF-2A8CFB53D2B6Q38760691-E07EDC9E-45A2-4C21-9C0A-A2752E452BD7Q41768810-96A9BFFD-82AE-44E9-AA23-AC2F168D6B04Q42231580-38FA8C06-4BC5-4620-B247-16C3804AC880Q42369950-AE732352-8EC5-40EB-90AE-EFAFC5182D10Q46600140-C351307B-4E29-427F-B67B-BE0A24CC5F94Q52761281-0CB589D3-DC0A-499A-916F-840EE6A408E2Q54196412-AE1CA11F-FF88-415D-9126-26C0F4816179Q55000487-F33B2B80-1239-466A-B3CB-4BC188A00304Q55416122-7496F164-C54F-405C-8476-DCB8351065B9Q57044366-34546B5F-664F-4CA0-89FD-D4885E455832
P2860
Enolase as a plasminogen binding protein in Leishmania mexicana
description
2007 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 2007
@ast
scientific journal article
@en
wetenschappelijk artikel (gepubliceerd op 2007/11/01)
@nl
наукова стаття, опублікована в листопаді 2007
@uk
مقالة علمية (نشرت في نوفمبر 2007)
@ar
name
Enolase as a plasminogen binding protein in Leishmania mexicana
@ast
Enolase as a plasminogen binding protein in Leishmania mexicana
@en
type
label
Enolase as a plasminogen binding protein in Leishmania mexicana
@ast
Enolase as a plasminogen binding protein in Leishmania mexicana
@en
prefLabel
Enolase as a plasminogen binding protein in Leishmania mexicana
@ast
Enolase as a plasminogen binding protein in Leishmania mexicana
@en
P2093
P3181
P1476
Enolase as a plasminogen binding protein in Leishmania mexicana
@en
P2093
Cesar Carrasco-López
Fernando Albericio
Gilmer Vanegas
Juan Luis Concepción
Luisana Avilán
Wilfredo Quiñones
P2888
P304
P3181
P356
10.1007/S00436-007-0668-7
P577
2007-11-01T00:00:00Z
P6179
1024557425