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Protamine: a unique and potent inhibitor of oligopeptidase B

https://doi.org/10.1002/psc.683
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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1002/(sici)1097-0134(199707)28:3<375::aid-prot7>3.0.co;2-bopenalex-snapshot
A potential processing enzyme in prokaryotes: Oligopeptidase B, a new type of serine peptidase
inferredcites →https://doi.org/10.1006/abio.1976.9999openalex-snapshot
A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye Binding
inferredcites →https://doi.org/10.1016/0003-9861(92)90360-9openalex-snapshot
Characterization of an endopeptidase of Trypanosoma brucei brucei
inferredcites →https://doi.org/10.1016/0005-2744(79)90053-6openalex-snapshot
Post-proline cleaving enzyme
inferredcites →https://doi.org/10.1016/s0006-2952(00)00459-7openalex-snapshot
Characterisation of the antitrypanosomal activity of peptidyl α-aminoalkyl phosphonate diphenyl esters
inferredcites →https://doi.org/10.1016/s0014-5793(98)00914-4openalex-snapshot
A trypanosome oligopeptidase as a target for the trypanocidal agents pentamidine, diminazene and suramin
inferredcites →https://doi.org/10.1016/s0021-9258(18)71591-3openalex-snapshot
Isolation and Characterization of a Novel Large Protease Accumulated in Mammalian Cells in the Presence of Inhibitors
inferredcites →https://doi.org/10.1016/s0021-9258(19)40882-xopenalex-snapshot
Protease II from Escherichia coli. Purification and characterization.
inferredcites →https://doi.org/10.1016/s0092-8674(00)81416-6openalex-snapshot
Prolyl Oligopeptidase
inferredcites →https://doi.org/10.1016/s0166-6851(99)00097-3openalex-snapshot
Purification and characterisation of a trypsin-like serine oligopeptidase from Trypanosoma congolense
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/10.1038/227680a0openalex-snapshot
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
inferredcites →https://doi.org/10.1042/bj20030342openalex-snapshot
Subsite specificity (S3, S2, S1', S2' and S3') of oligopeptidase B from Trypanosoma cruzi and Trypanosoma brucei using fluorescent quenched peptides: comparative study and identification of specific carboxypeptidase activity
inferredcites →https://doi.org/10.1042/bj2790907openalex-snapshot
A new family of serine-type peptidases related to prolyl oligopeptidase
inferredcites →https://doi.org/10.1046/j.1462-5822.2002.00226.xopenalex-snapshot
Cell signalling andTrypanosoma cruziinvasion
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.m003848200openalex-snapshot
Polyarginines Are Potent Furin Inhibitors
inferredcites →https://doi.org/10.1074/jbc.m400484200openalex-snapshot
Inhibition of Furin by Polyarginine-containing Peptides
inferredcites →https://doi.org/10.1074/jbc.m410066200openalex-snapshot
Oligopeptidase B from Trypanosoma evansi
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/10.1093/jb/mvh163openalex-snapshot
Identification of Oligopeptidase B in Higher Plants. Purification and Characterization of Oligopeptidase B from Quiescent Wheat Embryo, Triticum aestivum
inferredcites →https://doi.org/10.1093/oxfordjournals.jbchem.a123577openalex-snapshot
Protease II from Escherichia coli: Sequencing and Expression of the Enzyme Gene and Characterization of the Expressed Enzyme1
inferredcites →https://doi.org/10.1093/oxfordjournals.jbchem.a123682openalex-snapshot
Prolyl Endopeptidase from Flavobacterium meningosepticum: Cloning and Sequencing of the Enzyme Gene1
inferredcites →https://doi.org/10.1093/protein/15.2.123openalex-snapshot
Development of selectivity of α1-antitrypsin variant by mutagenesis in its reactive site loop against proprotein convertase. A crucial role of the P4 arginine in PACE4 inhibition
inferredcites →https://doi.org/10.1107/s0907444998004181openalex-snapshot
Crystallization and preliminary X-ray analysis of porcine muscle prolyl oligopeptidase
inferredcites →https://doi.org/10.1111/j.1432-1033.1986.tb09759.xopenalex-snapshot
Rainbow trout protamines. Amino acid sequences of six distinct proteins from a single testis
inferredcites →https://doi.org/10.1111/j.1432-1033.1996.0728w.xopenalex-snapshot
Proteases from Trypanosoma brucei brucei
inferredcites →https://doi.org/10.1111/j.1432-1033.2004.04199.xopenalex-snapshot
Evolutionary relationships of the prolyl oligopeptidase family enzymes
inferredcites →https://doi.org/10.1126/science.1071006openalex-snapshot
Functional Annotation of a Full-Length Arabidopsis cDNA Collection
inferredcites →https://doi.org/10.1128/iai.69.4.2757-2761.2001openalex-snapshot
Trypanosome-Derived Oligopeptidase B Is Released into the Plasma of Infected Rodents, Where It Persists and Retains Full Catalytic Activity
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/10.1248/bpb.20.1047openalex-snapshot
Cloning and Expression of the cDNA Encoding Prolyl Oligopeptidase (Prolyl Endopeptidase) from Bovine Brain.

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/10.1007/s10895-024-04122-9openalex-snapshot
A Pyrene-Derived Fluorescent Probe for the Visual Detection of Protamine and Trypsin Activity
inferred← citeshttps://doi.org/10.1007/s43630-026-00926-9openalex-snapshot
A long-wavelength tetraphenylethylene-derived fluorescent probe for sensitive detection of heparin and protamine
inferred← citeshttps://doi.org/10.1016/b978-0-12-382219-2.00743-2openalex-snapshot
Oligopeptidase B
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.2019.10.006openalex-snapshot
Oligopeptidase B, a missing enzyme in mammals and a potential drug target for trypanosomatid diseases
inferred← citeshttps://doi.org/10.1016/j.dyepig.2025.112656openalex-snapshot
A novel tetraphenylbenzene-derived fluorescent probe for the detection of protamine and heparin
inferred← citeshttps://doi.org/10.1016/j.microc.2025.116334openalex-snapshot
Switchable nanozyme-based colorimetric assay for protamine and heparin using silver citrate nanoparticles
inferred← citeshttps://doi.org/10.1016/j.saa.2026.127878openalex-snapshot
A terthiophene-derived fluorescent probe with long-emission wavelength for highly sensitive detection of heparin and protamine
inferred← citeshttps://doi.org/10.1039/d6ay01478jopenalex-snapshot
Emissive nanoaggregate-based dual sensing of heparin and protamine sulphate
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/10.1111/j.1745-7254.2008.00720.xopenalex-snapshot
Derivatives of aryl-4-guanidinomethylbenzoate and N-aryl-4-guanidinomethylbenzamide as new antibacterial agents: synthesis and bioactivity
inferred← citeshttps://doi.org/10.1248/bpb.b12-00544openalex-snapshot
Assessment of Substrate Inhibition of Bacterial Oligopeptidase B
inferred← citeshttps://doi.org/10.1371/journal.pone.0009796openalex-snapshot
Proteomics of Trypanosoma evansi Infection in Rodents
inferred← citeshttps://doi.org/10.2174/0929867311320250006openalex-snapshot
Parasite Prolyl Oligopeptidases and the Challenge of Designing Chemotherapeuticals for Chagas Disease, Leishmaniasis and African Trypanosomiasis
inferred← citeshttps://doi.org/10.2174/09298673113209990121openalex-snapshot
Parasite Prolyl Oligopeptidases and the Challenge of Designing Chemotherapeuticals for Chagas Disease, Leishmaniasis and African Trypanosomiasis
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