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Molecular, functional and structural properties of the prolyl oligopeptidase ofTrypanosoma cruzi(POP Tc80), which is required for parasite entry into mammalian cells
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1006/bbrc.1995.2782openalex-snapshot
The Cysteine-Rich Region of Dipeptidyl Peptidase IV (CD 26) Is the Collagen Binding Site
inferredcites →https://doi.org/10.1006/expr.1993.1039openalex-snapshot
Plasmodium falciparum: A Molecular View of Protein Transport from the Parasite into the Host Erythrocyte
inferredcites →https://doi.org/10.1006/jmbi.1997.1070openalex-snapshot
Cytochrome cd1 Structure: unusual haem environments in a nitrite reductase and analysis of factors contributing to β-propeller folds
inferredcites →https://doi.org/10.1016/0024-3205(75)90272-6openalex-snapshot
Purification and properties
inferredcites →https://doi.org/10.1016/0092-8674(84)90267-8openalex-snapshot
Identification of a small rna containing the trypanosome spliced leader: A donor of shared 5′ sequences of trypanosomatid mRNAs?
inferredcites →https://doi.org/10.1016/0092-8674(86)90834-2openalex-snapshot
A tandemly repeated sequence determines the binding domain for an erythrocyte receptor binding protein of P. falciparum
inferredcites →https://doi.org/10.1016/0092-8674(95)90054-3openalex-snapshot
Cloning the P. falciparum gene encoding PfEMP1, a malarial variant antigen and adherence receptor on the surface of parasitized human erythrocytes
inferredcites →https://doi.org/10.1016/0166-6851(93)90231-lopenalex-snapshot
Rapid isolation of DNA from trypanosomatid protozoa using a simple ‘mini-prep’ procedure
inferredcites →https://doi.org/10.1016/0166-6851(95)00066-aopenalex-snapshot
Molecular karyotype of clone CL Brener chosen for the Trypanosoma cruzi Genome Project
inferredcites →https://doi.org/10.1016/0378-1119(94)90177-5openalex-snapshot
Cloning and sequence analysis of the gene encoding human lymphocyte prolyl endopeptidase
inferredcites →https://doi.org/10.1016/c2013-0-04221-1openalex-snapshot
Principles of Enzyme Kinetics
inferredcites →https://doi.org/10.1016/j.jmb.2003.11.030openalex-snapshot
Structure of the Integrin α2β1-binding Collagen Peptide
inferredcites →https://doi.org/10.1016/j.jmb.2004.05.011openalex-snapshot
Concerted Structural Changes in the Peptidase and the Propeller Domains of Prolyl Oligopeptidase are Required for Substrate Binding
inferredcites →https://doi.org/10.1016/s0021-9258(17)34859-7openalex-snapshot
Post-proline cleaving enzyme and post-proline dipeptidyl aminopeptidase. Comparison of two peptidases with high specificity for proline residues.
inferredcites →https://doi.org/10.1016/s0021-9258(18)68866-0openalex-snapshot
Mammalian protein secretion without signal peptide removal. Biosynthesis of plasminogen activator inhibitor-2 in U-937 cells.
inferredcites →https://doi.org/10.1016/s0021-9258(19)85566-7openalex-snapshot
Proline-specific endopeptidase from Flavobacterium. Purification and properties.
inferredcites →https://doi.org/10.1016/s0021-9258(19)86614-0openalex-snapshot
Characterization of “thyroliberin-deamidating enzyme” as a post-proline-cleaving enzyme. Partial purification and enzyme-chemical analysis of the enzyme from anterior pituitary tissue.
inferredcites →https://doi.org/10.1016/s0092-8674(05)80061-3openalex-snapshot
Lysosome recruitment and fusion are early events required for trypanosome invasion of mammalian cells
inferredcites →https://doi.org/10.1016/s0223-5234(00)00118-5openalex-snapshot
Synthesis and activity of pyrrolidinyl- and thiazolidinyl-dipeptide derivatives as inhibitors of the Tc80 prolyl oligopeptidase from Trypanosoma cruzi
inferredcites →https://doi.org/10.1016/s0960-894x(03)00579-1openalex-snapshot
Prolylisoxazoles: potent inhibitors of prolyloligopeptidase with antitrypanosomal activity
inferredcites →https://doi.org/10.1016/s0962-8924(99)01673-6openalex-snapshot
The kelch repeat superfamily of proteins: propellers of cell function
inferredcites →https://doi.org/10.1016/s0968-0004(96)80163-0openalex-snapshot
Post-translational protein translocation: not all hsc70s are created equal
inferredcites →https://doi.org/10.1016/s0968-0896(02)00035-4openalex-snapshot
Comparison of the Inhibition of Human and Trypanosoma cruzi Prolyl Endopeptidases
inferredcites →https://doi.org/10.1016/s0969-2126(01)00185-xopenalex-snapshot
A helping hand for collagenases: the haemopexin-like domain
inferredcites →https://doi.org/10.1016/s0969-2126(01)00188-5openalex-snapshot
Structure of full-length porcine synovial collagenase reveals a C-terminal domain containing a calcium-linked, four-bladed β-propeller
inferredcites →https://doi.org/10.1016/s1093-3263(99)00042-xopenalex-snapshot
Construction of a 3D model of oligopeptidase B, a potential processing enzyme in prokaryotes
inferredcites →https://doi.org/10.1021/bi00222a025openalex-snapshot
cDNA cloning of porcine brain prolyl endopeptidase and identification of the active-site seryl residue
inferredcites →https://doi.org/10.1021/bi026846sopenalex-snapshot
Structural Requirements for Catalysis, Expression, and Dimerization in the CD26/DPIV Gene Family
inferredcites →https://doi.org/10.1038/227680a0openalex-snapshot
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
inferredcites →https://doi.org/10.1038/nsb882openalex-snapshot
Crystal structure of human dipeptidyl peptidase IV/CD26 in complex with a substrate analog
inferredcites →https://doi.org/10.1042/bj3250129openalex-snapshot
A Trypanosoma cruzi-secreted 80 kDa proteinase with specificity for human collagen types I and IV
inferredcites →https://doi.org/10.1074/jbc.273.37.24207openalex-snapshot
Lung Endothelial Dipeptidyl Peptidase IV Promotes Adhesion and Metastasis of Rat Breast Cancer Cells via Tumor Cell Surface-associated Fibronectin
inferredcites →https://doi.org/10.1074/jbc.274.37.26149openalex-snapshot
Oligopeptidase B from Trypanosoma brucei, a New Member of an Emerging Subgroup of Serine Oligopeptidases
inferredcites →https://doi.org/10.1074/jbc.274.51.36505openalex-snapshot
Fibroblast Activation Protein, a Dual Specificity Serine Protease Expressed in Reactive Human Tumor Stromal Fibroblasts
inferredcites →https://doi.org/10.1074/jbc.274.6.3461openalex-snapshot
Cloning of a Surface Membrane Glycoprotein Specific for the Infective Form of Trypanosoma cruzi Having Adhesive Properties to Laminin
inferredcites →https://doi.org/10.1074/jbc.m106017200openalex-snapshot
Trypanosoma cruzi Prolyl Oligopeptidase Tc80 Is Involved in Nonphagocytic Mammalian Cell Invasion by Trypomastigotes
inferredcites →https://doi.org/10.1083/jcb.136.3.609openalex-snapshot
A Cytosolic Serine Endopeptidase from Trypanosoma cruzi Is Required for the Generation of Ca2+ Signaling in Mammalian Cells
inferredcites →https://doi.org/10.1084/jem.171.2.401openalex-snapshot
The exit of Trypanosoma cruzi from the phagosome is inhibited by raising the pH of acidic compartments.
inferredcites →https://doi.org/10.1093/emboj/18.10.2734openalex-snapshot
Loss of a prolyl oligopeptidase confers resistance to lithium by elevation of inositol (1,4,5) trisphosphate
inferredcites →https://doi.org/10.1093/nar/14.21.8265openalex-snapshot
Structure of the RESA gene ofPiasmodium falciparum
inferredcites →https://doi.org/10.1093/nar/22.22.4673openalex-snapshot
CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
inferredcites →https://doi.org/10.1093/oxfordjournals.jbchem.a122404openalex-snapshot
Porcine Muscle Prolyl Endopeptidase and Its Endogenous Substrates
inferredcites →https://doi.org/10.1093/oxfordjournals.jbchem.a124120openalex-snapshot
Prolyl Endopeptidase from Aeromonas hydrophila: Cloning, Sequencing, and Expression of the Enzyme Gene, and Characterization of the Expressed Enzyme1
inferredcites →https://doi.org/10.1107/s0021889892009944openalex-snapshot
PROCHECK: a program to check the stereochemical quality of protein structures
inferredcites →https://doi.org/10.1128/jb.184.12.3329-3337.2002openalex-snapshot
Substrate Recognition Properties of Oligopeptidase B fromSalmonella entericaSerovar Typhimurium
inferredcites →https://doi.org/10.1146/annurev.biophys.29.1.291openalex-snapshot
Comparative Protein Structure Modeling of Genes and Genomes
inferredcites →https://doi.org/10.1159/000350087openalex-snapshot
Short-Term Effects of Nose-Only Cigarette Smoke Exposure on Glutathione Redox Homeostasis, Cytochrome P450 1A1/2 and Respiratory Enzyme Activities in Mice Tissues
inferredcites →https://doi.org/10.1189/jlb.69.6.963openalex-snapshot
Involvement of cytosolic prolyl endopeptidase in degradation of p40-phox splice variant protein in myeloid cells
inferredcites →https://doi.org/10.1248/cpb.47.194openalex-snapshot
Identification of Inhibitors of an 80kDa Protease from Trypanosoma cruzi through the Screening of a Combinatorial Peptide Library.
inferredcites →https://doi.org/10.1271/bbb1961.42.2417openalex-snapshot
Proline specific endopeptidase from Flavobacterium.
inferredcites →https://doi.org/10.1515/bchm3.1992.373.2.353openalex-snapshot
Oligopeptidases, and the Emergence of the Prolyl Oligopeptidase Family
inferredcites →https://doi.org/10.1590/s0074-02761999000700079openalex-snapshot
Progress towards interruption of transmission of Chagas disease
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
inferred← citeshttps://doi.org/10.2139/ssrn.4658480openalex-extracted
Oligopeptidase B of Dioscorea Opposita “Nagaimo”: Isolation, Biochemical Characterization, and Primary Structure
inferred← citeshttps://doi.org/10.1002/biof.1100openalex-snapshot
Secreted proteases of Trypanosoma brucei gambiense : Possible targets for sleeping sickness control?
inferred← citeshttps://doi.org/10.1007/978-1-4614-9233-7_9openalex-snapshot
Proteases as Virulence Factors in Leishmania: Focus on Serine Proteases as Possible Therapeutic Targets
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Trypanosoma cruzi serinecarboxipeptidase is a sulfated glycoprotein and a minor antigen in human Chagas disease infection
inferred← citeshttps://doi.org/10.1007/s00436-009-1383-3openalex-snapshot
Perspectives on the Trypanosoma cruzi–host cell receptor interactions
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Multiple effects of pepstatin A on Trypanosoma cruzi epimastigote forms
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Identification of novel Trypanosoma cruzi prolyl oligopeptidase inhibitors by structure-based virtual screening
inferred← citeshttps://doi.org/10.1007/s10930-022-10080-7openalex-snapshot
Proteomic Analysis Reveals Differential Protein Expression Induced by Inhibition of Prolyl Oligopeptidase in Filarial Parasites
inferred← citeshttps://doi.org/10.1016/b978-0-12-385863-4.00013-7openalex-snapshot
Aspects of Trypanosoma cruzi Stage Differentiation
inferred← citeshttps://doi.org/10.1016/j.bbadis.2019.165658openalex-snapshot
Chagas disease vaccine design: the search for an efficient Trypanosoma cruzi immune-mediated control
inferred← citeshttps://doi.org/10.1016/j.bbapap.2011.05.011openalex-snapshot
The peptidases of Trypanosoma cruzi: Digestive enzymes, virulence factors, and mediators of autophagy and programmed cell death
inferred← citeshttps://doi.org/10.1016/j.bbapap.2020.140577openalex-snapshot
Update on relevant trypanosome peptidases: Validated targets and future challenges
inferred← citeshttps://doi.org/10.1016/j.bbrep.2025.102071openalex-snapshot
Isolation, biochemical characterization, and primary structure and active site determination of Dioscorea opposita (‘Nagaimo’) oligopeptidase B
inferred← citeshttps://doi.org/10.1016/j.biochi.2007.10.011openalex-snapshot
Oligopeptidase B: A processing peptidase involved in pathogenesis
inferred← citeshttps://doi.org/10.1016/j.biochi.2007.11.002openalex-snapshot
Localization of post-proline cleaving peptidases in Tenebrio molitor larval midgut
inferred← citeshttps://doi.org/10.1016/j.bmc.2007.11.015openalex-snapshot
Inhibitors of proteases and amide hydrolases that employ an α-ketoheterocycle as a key enabling functionality
inferred← citeshttps://doi.org/10.1016/j.cca.2006.09.001openalex-snapshot
Suggested functions for prolyl oligopeptidase: A puzzling paradox
inferred← citeshttps://doi.org/10.1016/j.exppara.2010.01.023openalex-snapshot
Detection of matrix metallopeptidase-9-like proteins in Trypanosoma cruzi
inferred← citeshttps://doi.org/10.1016/j.exppara.2011.09.002openalex-snapshot
Infestin 1R, an intestinal subtilisin inhibitor from Triatoma infestans able to impair mammalian cell invasion by Trypanosoma cruzi
inferred← citeshttps://doi.org/10.1016/j.foodchem.2011.04.081openalex-snapshot
Angiotensin-I-converting enzyme and prolyl endopeptidase inhibitory peptides from natural sources with a focus on marine processing by-products
inferred← citeshttps://doi.org/10.1016/j.micinf.2006.08.001openalex-snapshot
Lagochilascaris minor third-stage larvae secrete metalloproteases with specificity for fibrinogen and native collagen
inferred← citeshttps://doi.org/10.1016/j.micinf.2010.02.007openalex-snapshot
Prolyl oligopeptidase of Trypanosoma brucei hydrolyzes native collagen, peptide hormones and is active in the plasma of infected mice
inferred← citeshttps://doi.org/10.1016/j.micinf.2012.09.003openalex-snapshot
Virulence factors of Trypanosoma cruzi: who is who?
inferred← citeshttps://doi.org/10.1016/j.molbiopara.2010.09.003openalex-snapshot
Oligopeptidase B deficient mutants of Leishmania major
inferred← citeshttps://doi.org/10.1016/j.molbiopara.2013.11.001openalex-snapshot
A Protein Phosphatase 1 involved in correct nucleus positioning in trypanosomes
inferred← citeshttps://doi.org/10.1016/j.pt.2011.01.005openalex-snapshot
Area 51: How do Acanthamoeba invade the central nervous system?
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Fungalysin and dipeptidyl-peptidase gene transcription in Microsporum canis strains isolated from symptomatic and asymptomatic cats
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Prolyl oligopeptidase-like deficient Trypanosoma evansi parasites are associated with reduced interleukin-10 concentrations in vivo and in vitro
inferred← citeshttps://doi.org/10.1017/s0031182012001448openalex-snapshot
Trypanosoma cruzi heparin-binding proteins present a flagellar membrane localization and serine proteinase activity
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The genome ofStrongyloidesspp. gives insights into protein families with a putative role in nematode parasitism
inferred← citeshttps://doi.org/10.1021/acs.jcim.4c02152openalex-snapshot
Structure-Based Identification of Non-covalent Prolyl Oligopeptidase 80 Inhibitors Targeting Trypanosoma cruzi Cell Entry
inferred← citeshttps://doi.org/10.1021/jm3002839openalex-snapshot
Virtual Screening and Computational Optimization for the Discovery of Covalent Prolyl Oligopeptidase Inhibitors with Activity in Human Cells
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Inhibitors of Prolyl Oligopeptidases for the Therapy of Human Diseases: Defining Diseases and Inhibitors
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Proteomic Analysis of Trypanosoma cruzi Secretome: Characterization of Two Populations of Extracellular Vesicles and Soluble Proteins
inferred← citeshttps://doi.org/10.1038/s41467-025-62068-3openalex-snapshot
Cryo-EM led analysis of open and closed conformations of Chagas vaccine candidate TcPOP
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Pyroglutamyl peptidase type I from Trypanosoma brucei: a new virulence factor from African trypanosomes that de-blocks regulatory peptides in the plasma of infected hosts
inferred← citeshttps://doi.org/10.1042/bj20060973openalex-snapshot
Two metallocarboxypeptidases from the protozoan Trypanosoma cruzi belong to the M32 family, found so far only in prokaryotes
inferred← citeshttps://doi.org/10.1074/jbc.m114.574525openalex-snapshot
Role of Δ1-Pyrroline-5-Carboxylate Dehydrogenase Supports Mitochondrial Metabolism and Host-Cell Invasion of Trypanosoma cruzi
inferred← citeshttps://doi.org/10.1080/10629360903438198openalex-snapshot
Molecular dynamics study of prolyl oligopeptidase with inhibitor in binding cavity
inferred← citeshttps://doi.org/10.1093/jb/mvaa069openalex-snapshot
Molecular characterization of a prolyl endopeptidase from a feather-degrading thermophile Meiothermus ruber H328
inferred← citeshttps://doi.org/10.1093/jb/mvp156openalex-snapshot
A critical role for highly conserved Glu610 residue of oligopeptidase B from Trypanosoma brucei in thermal stability
inferred← citeshttps://doi.org/10.1093/nar/gkn512openalex-snapshot
Interactions between branched DNAs and peptide inhibitors of DNA repair
inferred← citeshttps://doi.org/10.1097/qco.0b013e328315cca9openalex-snapshot
Development of protease inhibitors for protozoan infections
inferred← citeshttps://doi.org/10.1101/2024.03.26.586384openalex-snapshot
Cryo-EM led analysis of open and closed conformations of Chagas vaccine candidate TcPOP and its antibody response characterisation
inferred← citeshttps://doi.org/10.1111/j.1439-0507.2011.02081.xopenalex-snapshot
Mechanisms of skin adherence and invasion by dermatophytes
inferred← citeshttps://doi.org/10.1111/j.1574-695x.2008.00479.xopenalex-snapshot
Secreted dipeptidyl peptidases as potential virulence factors forMicrosporum canis
inferred← citeshttps://doi.org/10.1111/j.1574-6976.2012.00340.xopenalex-snapshot
Human pathogens utilize host extracellular matrix proteins laminin and collagen for adhesion and invasion of the host
inferred← citeshttps://doi.org/10.1111/j.1742-4658.2008.06333.xopenalex-snapshot
Functional domains of the human epididymal protease inhibitor, eppin
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Fibronectin-Degrading Activity of Trypanosoma cruzi Cysteine Proteinase Plays a Role in Host Cell Invasion
inferred← citeshttps://doi.org/10.1128/iai.05329-11openalex-snapshot
Differential Expression and Characterization of a Member of the Mucin-Associated Surface Protein Family Secreted by Trypanosoma cruzi
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The major leucyl aminopeptidase of Trypanosoma cruzi (LAPTc) assembles into a homohexamer and belongs to the M17 family of metallopeptidases
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Characterization of prolyl oligopeptidase from hyperthermophilic archaeon Thermococcus sp. NA1
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Prolyl Oligopeptidase from the Blood Fluke Schistosoma mansoni: From Functional Analysis to Anti-schistosomal Inhibitors
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Trypanosoma cruzi 80 kDa prolyl oligopeptidase (Tc80) as a novel immunogen for Chagas disease vaccine
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Genome Sequence of the Endosymbiont Rickettsia peacockii and Comparison with Virulent Rickettsia rickettsii: Identification of Virulence Factors
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The Trypanosoma cruzi Virulence Factor Oligopeptidase B (OPBTc) Assembles into an Active and Stable Dimer
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Molecular Characterization of Trypanosoma cruzi SAP Proteins with Host-Cell Lysosome Exocytosis-Inducing Activity Required for Parasite Invasion
inferred← citeshttps://doi.org/10.1371/journal.pone.0123241openalex-snapshot
An Essential Signal Peptide Peptidase Identified in an RNAi Screen of Serine Peptidases of Trypanosoma brucei
inferred← citeshttps://doi.org/10.1385/cbb:44:3:349openalex-snapshot
Structure-Function Properties of Prolyl Oligopeptidase Family Enzymes
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Molecular basis of mammalian cell invasion by Trypanosoma cruzi
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Parasite Prolyl Oligopeptidases and the Challenge of Designing Chemotherapeuticals for Chagas Disease, Leishmaniasis and African Trypanosomiasis
inferred← citeshttps://doi.org/10.2174/157340810794578506openalex-snapshot
Peptidase Inhibitors as a Possible Therapeutic Strategy for Chagas Disease
inferred← citeshttps://doi.org/10.2174/157489107779561625openalex-snapshot
An Insight on Targets and Patented Drugs for Chemotherapy of Chagas Disease
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A Decade of Targets and Patented Drugs for Chemotherapy of Chagas Disease
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Targets and Patented Drugs for Chemotherapy of Chagas Disease in the Last 15 Years-Period
inferred← citeshttps://doi.org/10.2174/1874421401004010005openalex-snapshot
Biological Roles of Peptidases in Trypanosomatids
inferred← citeshttps://doi.org/10.2174/1874421401004010030openalex-snapshot
Trypanosomatids: Odd Organisms, Devastating Diseases
inferred← citeshttps://doi.org/10.2174/1874421401004010060openalex-snapshot
Trypanosoma cruzi Cysteine Proteases, Acting at the Interface Between the Vascular and Immune Systems, Influence Pathogenic Outcome in Experimental Chagas Disease
inferred← citeshttps://doi.org/10.2174/1874421401004010120openalex-snapshot
Trypanosoma cruzi Peptidases: An Overview
inferred← citeshttps://doi.org/10.2741/2961openalex-snapshot
Molecular analysis of early host cell infection by Trypanosoma cruzi
inferred← citeshttps://doi.org/10.32604/biocell.2006.30.479openalex-snapshot
Cysteine proteinases of Trypanosoma cruzi: from digestive enzymes to programmed cell death mediators
inferred← citeshttps://doi.org/10.3389/fcimb.2023.1028496openalex-snapshot
Hallmarks of the relationship between host and Trypanosoma cruzi sulfated glycoconjugates along the course of Chagas disease
inferred← citeshttps://doi.org/10.3389/fmicb.2016.00388openalex-snapshot
Interactions between Trypanosoma cruzi Secreted Proteins and Host Cell Signaling Pathways
inferred← citeshttps://doi.org/10.3389/fmicb.2017.00155openalex-snapshot
Mycobacterium tuberculosis Prolyl Oligopeptidase Induces In vitro Secretion of Proinflammatory Cytokines by Peritoneal Macrophages
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A Carbohydrate Moiety of Secreted Stage-Specific Glycoprotein 4 Participates in Host Cell Invasion by Trypanosoma cruzi Extracellular Amastigotes
inferred← citeshttps://doi.org/10.3389/fmicb.2020.01060openalex-snapshot
Prolyl Oligopeptidase From Leishmania infantum: Biochemical Characterization and Involvement in Macrophage Infection
inferred← citeshttps://doi.org/10.3389/fphar.2022.929493openalex-snapshot
Discovery of Leishmania Druggable Serine Proteases by Activity-Based Protein Profiling
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Anti-Trypanosoma cruzi Properties of Sesquiterpene Lactones Isolated from Stevia spp.: In Vitro and In Silico Studies
inferred← citeshttps://doi.org/10.3390/plants11101330openalex-snapshot
Post-Proline Cleaving Enzymes (PPCEs): Classification, Structure, Molecular Properties, and Applications
inferred← citeshttps://doi.org/10.3390/vaccines10040587openalex-snapshot
Vaccine Design against Chagas Disease Focused on the Use of Nucleic Acids
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Prolyl Oligopeptidase and Its Role in the Organism: Attention to the Most Promising and Clinically Relevant Inhibitors
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Novel Therapeutic Strategies for Chagas` Disease
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