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  1. AU="Bergado, Gretchen"
  2. AU="Schomberg, Harry H"
  3. AU="Halder, Prolay"
  4. AU="Miyaguchi, Ken"
  5. AU="Zhan, Na-ping"
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  1. Artikel: Bacitracin is a non-competitive inhibitor of porcine M1 family neutral and glutamyl aminopeptidases

    Arrebola, Yarini / Rivera, Laura / Pedroso, Alejandro / McGuire, Rory / Tresanco, Mario E. Valdes / Bergado, Gretchen / Charli, Jean-Louis / Sánchez, Belinda / Pascual Alonso, Isel

    Natural product research. 2021 Aug. 19, v. 35, no. 17

    2021  

    Abstract: Membrane alanyl and glutamyl aminopeptidases (APN and APA, respectively) are established targets for the development of biomedical tools in human pathologies. APN overexpression correlates with the progression of tumours, including melanoma. Bacitracin, ... ...

    Abstract Membrane alanyl and glutamyl aminopeptidases (APN and APA, respectively) are established targets for the development of biomedical tools in human pathologies. APN overexpression correlates with the progression of tumours, including melanoma. Bacitracin, widely used as a topical antibiotic, inhibits subtilisin-like serine peptidases and disulphide isomerases. In the present contribution, we demonstrate that bacitracin is a non-competitive α = 1 and α < 1 inhibitor of porcine kidney APN and APA, respectively, with Kᵢ values in the micromolar range. To test a potential application of this result, we assayed the effect of bacitracin on murine melanoma MB16F10 cell line viability. We demonstrated the cell line expresses an APN-like activity inhibited by bacitracin and bestatin. Additionally, we identified a cytotoxic effect of bacitracin. Further experiments are required to understand in depth the mechanisms of action of bacitracin on melanoma cells. They will clarify the therapeutic potential of bacitracin for melanoma treatment.
    Schlagwörter aminopeptidases ; bacitracin ; cell lines ; cytotoxicity ; disulfides ; humans ; isomerases ; kidneys ; melanoma ; mice ; research ; serine ; swine ; therapeutics ; viability
    Sprache Englisch
    Erscheinungsverlauf 2021-0819
    Umfang p. 2958-2962.
    Erscheinungsort Taylor & Francis
    Dokumenttyp Artikel
    ZDB-ID 2185747-7
    ISSN 1478-6427 ; 1478-6419
    ISSN (online) 1478-6427
    ISSN 1478-6419
    DOI 10.1080/14786419.2019.1678611
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  2. Artikel: Discovery of tight-binding competitive inhibitors of dipeptidyl peptidase IV

    Pascual Alonso, Isel / Valiente, Pedro A. / Valdés-Tresanco, Mario E. / Arrebola, Yarini / Almeida García, Fabiola / Díaz, Lisset / García, Gabriela / Guirola, Osmany / Pastor, Daniel / Bergado, Gretchen / Sánchez, Belinda / Charli, Jean-Louis

    International journal of biological macromolecules. 2022 Jan. 31, v. 196

    2022  

    Abstract: Dipeptidyl peptidase IV (DPP-IV, EC 3.4.14.5) is an abundant serine aminopeptidase that preferentially cleaves N-terminal Xaa-Pro or Xaa-Ala dipeptides from oligopeptides. Inhibitors of DPP-IV activity are used for treating type 2 diabetes mellitus and ... ...

    Abstract Dipeptidyl peptidase IV (DPP-IV, EC 3.4.14.5) is an abundant serine aminopeptidase that preferentially cleaves N-terminal Xaa-Pro or Xaa-Ala dipeptides from oligopeptides. Inhibitors of DPP-IV activity are used for treating type 2 diabetes mellitus and other diseases. DPP-IV is also involved in tumor progression. We identified four new non-peptide tight-binding competitive inhibitors of porcine DPP-IV by virtual screening and enzymatic assays. Molecular docking simulations supported the competitive behavior, and the selectivity of one of the compounds in the DPP-IV family. Since three of these inhibitors are also aminopeptidase N (APN) inhibitors, we tested their impact on APN+/DPP-IV+ and DPP-IV+ human tumor cells' viability. Using kinetic assays, we determined that HL-60 tumor cells express both APN and DPP-IV activities and that MDA-MB-231 tumor cells express DPP-IV activity. The inhibitors had a slight inhibitory effect on human HEK-293 cell viability but reduced the viability of APN+/DPP-IV+ and DPP-IV+ human tumor cells more potently. Remarkably, the intraperitoneal injection of these compounds inhibited DPP-IV activity in rat brain, liver, and pancreas. In silico studies suggested inhibitors binding to serum albumin contribute to blood-brain barrier crossing. The spectrum of action of some of these compounds may be useful for niche applications.
    Schlagwörter blood-brain barrier ; brain ; cell viability ; computer simulation ; dipeptides ; dipeptidyl-peptidase IV ; human cell lines ; humans ; intraperitoneal injection ; liver ; membrane alanyl aminopeptidase ; neoplasm progression ; neoplasms ; noninsulin-dependent diabetes mellitus ; pancreas ; rats ; serine ; serum albumin ; swine
    Sprache Englisch
    Erscheinungsverlauf 2022-0131
    Umfang p. 120-130.
    Erscheinungsort Elsevier B.V.
    Dokumenttyp Artikel
    ZDB-ID 282732-3
    ISSN 1879-0003 ; 0141-8130
    ISSN (online) 1879-0003
    ISSN 0141-8130
    DOI 10.1016/j.ijbiomac.2021.12.056
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  3. Artikel ; Online: Bufadienolides preferentially inhibit aminopeptidase N among mammalian metallo-aminopeptidases; relationship with effects on human melanoma MeWo cells.

    Pascual Alonso, Isel / Rivera Méndez, Laura / Almeida García, Fabiola / Valdés-Tresanco, Mario Ernesto / Alonso Bosch, Roberto / Perera, Wilmer H / Arrebola Sánchez, Yarini / Bergado, Gretchen / Sánchez Ramírez, Belinda / Charli, Jean-Louis

    International journal of biological macromolecules

    2022  Band 229, Seite(n) 825–837

    Abstract: Bufadienolides are steroids that inhibit ... ...

    Abstract Bufadienolides are steroids that inhibit Na
    Mesh-Begriff(e) Humans ; Swine ; Animals ; CD13 Antigens ; Aminopeptidases ; Bufanolides/pharmacology ; Bufanolides/metabolism ; Enzyme Inhibitors ; Melanoma/drug therapy ; Mammals/metabolism
    Chemische Substanzen CD13 Antigens (EC 3.4.11.2) ; Aminopeptidases (EC 3.4.11.-) ; Bufanolides ; Enzyme Inhibitors
    Sprache Englisch
    Erscheinungsdatum 2022-12-30
    Erscheinungsland Netherlands
    Dokumenttyp Journal Article
    ZDB-ID 282732-3
    ISSN 1879-0003 ; 0141-8130
    ISSN (online) 1879-0003
    ISSN 0141-8130
    DOI 10.1016/j.ijbiomac.2022.12.280
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  4. Artikel: Bestatin and bacitracin inhibit porcine kidney cortex dipeptidyl peptidase IV activity and reduce human melanoma MeWo cell viability

    Méndez, Laura Rivera / Arrebola, Yarini / Valdés-Tresanco, Mario E / Díaz-Guevara, Lisset / Bergado, Gretchen / Sánchez, Belinda / Charli, Jean-Louis / Pascual Alonso, Isel

    International journal of biological macromolecules. 2020 Dec. 01, v. 164

    2020  

    Abstract: Bestatin and bacitracin are inhibitors of metallo aminopeptidases and bacterial proteases. However, their effects on other human peptidases, like dipeptidyl peptidase IV (DPP-IV, EC 3.4.14.5) are not established. Inhibitors of DPP-IV activity are used ... ...

    Abstract Bestatin and bacitracin are inhibitors of metallo aminopeptidases and bacterial proteases. However, their effects on other human peptidases, like dipeptidyl peptidase IV (DPP-IV, EC 3.4.14.5) are not established. Inhibitors of DPP-IV activity are used for treating type 2 diabetes mellitus, cancers and immune system diseases. Bacitracin and bestatin inhibited porcine membrane-bound DPP-IV (pDPP-IV) activity. Mechanisms were different, i.e. non-competitive with α > 1 (α = 3.9) and Kᵢ value of 75 μM for bestatin, and competitive with Kᵢ value of 630 μM for bacitracin. The binding mode in the tertiary complex enzyme:substrate:bestatin suggested the structural basis of the inhibitory effect and that bestatin is potentially selective for DPP-IV, ineffective vs. S9 family members dipeptidyl peptidase 8/9 and fibroblast activation protein. In the human melanoma MeWo cell line, bestatin and bacitracin inhibited aminopeptidase N (APN) and DPP-IV activities, reduced cell viability and increased DNA fragmentation, suggesting induction of apoptosis. Since bacitracin and bestatin are already marketed drugs, studying in depth the molecular mechanisms underlying their effects on melanoma cells is warranted. Additionally, bestatin emerges as a new lead compound for the development of DPP-IV inhibitors, and a promising dual APN/DPP-IV inhibitor for the treatment of pathologies in which both enzymes are upregulated.
    Schlagwörter DNA fragmentation ; apoptosis ; bacitracin ; cell viability ; cortex ; dipeptidyl-peptidase IV ; fibroblasts ; humans ; immune system ; kidneys ; melanoma ; membrane alanyl aminopeptidase ; noninsulin-dependent diabetes mellitus ; proteinases ; swine
    Sprache Englisch
    Erscheinungsverlauf 2020-1201
    Umfang p. 2944-2952.
    Erscheinungsort Elsevier B.V.
    Dokumenttyp Artikel
    Anmerkung NAL-AP-2-clean
    ZDB-ID 282732-3
    ISSN 1879-0003 ; 0141-8130
    ISSN (online) 1879-0003
    ISSN 0141-8130
    DOI 10.1016/j.ijbiomac.2020.08.157
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  5. Artikel ; Online: Corrigendum to "JM-20 treatment prevents neuronal damage and memory impairment induced by aluminum chloride in rats" [Neurotoxicology 87 (2021) 70-85].

    Wong-Guerra, Maylin / Montano-Peguero, Yanay / Ramírez-Sánchez, Jeney / Jiménez-Martin, Javier / Fonseca-Fonseca, Luis Arturo / Hernández-Enseñat, Daniela / Nonose, Yasmine / Valdés, Odalys / Mondelo-Rodriguez, Abel / Ortiz-Miranda, Yaquelin / Bergado, Gretchen / Carmenate, Tania / Soto Del Valle, Roberto Menéndez / Pardo-Andreu, Gilberto / Outeiro, Tiago Fleming / Padrón-Yaquis, Alejandro Saúl / de Assis, Adriano Martimbianco / Souza, Diogo O / Nuñez-Figueredo, Yanier

    Neurotoxicology

    2023  Band 99, Seite(n) 10–13

    Sprache Englisch
    Erscheinungsdatum 2023-09-10
    Erscheinungsland Netherlands
    Dokumenttyp Published Erratum
    ZDB-ID 800820-6
    ISSN 1872-9711 ; 0161-813X
    ISSN (online) 1872-9711
    ISSN 0161-813X
    DOI 10.1016/j.neuro.2023.09.003
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  6. Artikel ; Online: Discovery of tight-binding competitive inhibitors of dipeptidyl peptidase IV.

    Pascual Alonso, Isel / Valiente, Pedro A / Valdés-Tresanco, Mario E / Arrebola, Yarini / Almeida García, Fabiola / Díaz, Lisset / García, Gabriela / Guirola, Osmany / Pastor, Daniel / Bergado, Gretchen / Sánchez, Belinda / Charli, Jean-Louis

    International journal of biological macromolecules

    2021  Band 196, Seite(n) 120–130

    Abstract: Dipeptidyl peptidase IV (DPP-IV, EC 3.4.14.5) is an abundant serine aminopeptidase that preferentially cleaves N-terminal Xaa-Pro or Xaa-Ala dipeptides from oligopeptides. Inhibitors of DPP-IV activity are used for treating type 2 diabetes mellitus and ... ...

    Abstract Dipeptidyl peptidase IV (DPP-IV, EC 3.4.14.5) is an abundant serine aminopeptidase that preferentially cleaves N-terminal Xaa-Pro or Xaa-Ala dipeptides from oligopeptides. Inhibitors of DPP-IV activity are used for treating type 2 diabetes mellitus and other diseases. DPP-IV is also involved in tumor progression. We identified four new non-peptide tight-binding competitive inhibitors of porcine DPP-IV by virtual screening and enzymatic assays. Molecular docking simulations supported the competitive behavior, and the selectivity of one of the compounds in the DPP-IV family. Since three of these inhibitors are also aminopeptidase N (APN) inhibitors, we tested their impact on APN+/DPP-IV+ and DPP-IV+ human tumor cells' viability. Using kinetic assays, we determined that HL-60 tumor cells express both APN and DPP-IV activities and that MDA-MB-231 tumor cells express DPP-IV activity. The inhibitors had a slight inhibitory effect on human HEK-293 cell viability but reduced the viability of APN+/DPP-IV+ and DPP-IV+ human tumor cells more potently. Remarkably, the intraperitoneal injection of these compounds inhibited DPP-IV activity in rat brain, liver, and pancreas. In silico studies suggested inhibitors binding to serum albumin contribute to blood-brain barrier crossing. The spectrum of action of some of these compounds may be useful for niche applications.
    Mesh-Begriff(e) Animals ; Binding Sites ; Cell Survival/drug effects ; Dipeptidyl Peptidase 4/chemistry ; Dipeptidyl-Peptidase IV Inhibitors/chemistry ; Dipeptidyl-Peptidase IV Inhibitors/pharmacology ; Drug Discovery ; Enzyme Activation ; Humans ; Hydrolysis ; Models, Molecular ; Molecular Conformation ; Molecular Docking Simulation ; Molecular Dynamics Simulation ; Molecular Structure ; Protein Binding ; Substrate Specificity ; Swine
    Chemische Substanzen Dipeptidyl-Peptidase IV Inhibitors ; Dipeptidyl Peptidase 4 (EC 3.4.14.5)
    Sprache Englisch
    Erscheinungsdatum 2021-12-15
    Erscheinungsland Netherlands
    Dokumenttyp Journal Article
    ZDB-ID 282732-3
    ISSN 1879-0003 ; 0141-8130
    ISSN (online) 1879-0003
    ISSN 0141-8130
    DOI 10.1016/j.ijbiomac.2021.12.056
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  7. Artikel: A cell-based ELISA as surrogate of virus neutralization assay for RBD SARS-CoV-2 specific antibodies

    Pi-Estopiñan, Franciscary / Pérez, María Teresa / Fraga, Anitza / Bergado, Gretchen / Díaz, Geidy D. / Orosa, Ivette / Díaz, Marianniz / Solozábal, Joaquín Antonio / Rodríguez, Laura Marta / Garcia-Rivera, Dagmar / Macías, Consuelo / Jerez, Yanet / Casadesús, Ana V. / Fernández-Marrero, Briandy / Bermúdez, Ernesto / Plasencia, Claudia A. / Sánchez, Belinda / Hernández, Tays

    Vaccine. 2022 Mar. 18, v. 40, no. 13

    2022  

    Abstract: SARS-CoV-2, the cause of the COVID-19 pandemic, has provoked a global crisis and death of millions of people. Several serological assays to determine the quality of the immune response against SARS-CoV-2 and the efficacy of vaccines have been developed, ... ...

    Abstract SARS-CoV-2, the cause of the COVID-19 pandemic, has provoked a global crisis and death of millions of people. Several serological assays to determine the quality of the immune response against SARS-CoV-2 and the efficacy of vaccines have been developed, among them the gold standard conventional virus neutralization assays. However, these tests are time consuming, require biosafety level 3 (BSL3), and are low throughput and expensive. This has motivated the development of alternative methods, including molecular inhibition assays. Herein, we present a safe cell-based ELISA-virus neutralization test (cbE-VNT) as a surrogate for the conventional viral neutralization assays that detects the inhibition of SARS-CoV-2 RBD binding to ACE2-bearing cells independently of species. Our test shows a very good correlation with the conventional and molecular neutralization assays and achieves 100% specificity and 95% sensitivity. cbE-VNT is cost-effective, fast and enables a large-scale serological evaluation that can be performed in a BSL2 laboratory, allowing its use in pre-clinical and clinical investigations.
    Schlagwörter COVID-19 infection ; Severe acute respiratory syndrome coronavirus 2 ; biosafety ; cost effectiveness ; death ; immune response ; neutralization ; neutralization tests ; vaccines
    Sprache Englisch
    Erscheinungsverlauf 2022-0318
    Umfang p. 1958-1967.
    Erscheinungsort Elsevier Ltd
    Dokumenttyp Artikel
    ZDB-ID 605674-x
    ISSN 1873-2518 ; 0264-410X
    ISSN (online) 1873-2518
    ISSN 0264-410X
    DOI 10.1016/j.vaccine.2022.02.044
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  8. Artikel ; Online: Bestatin and bacitracin inhibit porcine kidney cortex dipeptidyl peptidase IV activity and reduce human melanoma MeWo cell viability.

    Méndez, Laura Rivera / Arrebola, Yarini / Valdés-Tresanco, Mario E / Díaz-Guevara, Lisset / Bergado, Gretchen / Sánchez, Belinda / Charli, Jean-Louis / Pascual Alonso, Isel

    International journal of biological macromolecules

    2020  Band 164, Seite(n) 2944–2952

    Abstract: Bestatin and bacitracin are inhibitors of metallo aminopeptidases and bacterial proteases. However, their effects on other human peptidases, like dipeptidyl peptidase IV (DPP-IV, EC 3.4.14.5) are not established. Inhibitors of DPP-IV activity are used ... ...

    Abstract Bestatin and bacitracin are inhibitors of metallo aminopeptidases and bacterial proteases. However, their effects on other human peptidases, like dipeptidyl peptidase IV (DPP-IV, EC 3.4.14.5) are not established. Inhibitors of DPP-IV activity are used for treating type 2 diabetes mellitus, cancers and immune system diseases. Bacitracin and bestatin inhibited porcine membrane-bound DPP-IV (pDPP-IV) activity. Mechanisms were different, i.e. non-competitive with α > 1 (α = 3.9) and K
    Mesh-Begriff(e) Animals ; Antineoplastic Agents/pharmacology ; Bacitracin/pharmacology ; Cell Line, Tumor ; Cell Membrane/drug effects ; Cell Membrane/enzymology ; Cell Survival/drug effects ; Dipeptidyl Peptidase 4/chemistry ; Dipeptidyl Peptidase 4/metabolism ; Dipeptidyl-Peptidase IV Inhibitors/pharmacology ; Gene Expression Regulation, Enzymologic/drug effects ; Gene Expression Regulation, Neoplastic/drug effects ; Humans ; Kidney/enzymology ; Leucine/analogs & derivatives ; Leucine/pharmacology ; Melanoma/drug therapy ; Melanoma/enzymology ; Models, Molecular ; Structure-Activity Relationship ; Swine
    Chemische Substanzen Antineoplastic Agents ; Dipeptidyl-Peptidase IV Inhibitors ; Bacitracin (1405-87-4) ; Dipeptidyl Peptidase 4 (EC 3.4.14.5) ; Leucine (GMW67QNF9C) ; ubenimex (I0J33N5627)
    Sprache Englisch
    Erscheinungsdatum 2020-08-23
    Erscheinungsland Netherlands
    Dokumenttyp Journal Article
    ZDB-ID 282732-3
    ISSN 1879-0003 ; 0141-8130
    ISSN (online) 1879-0003
    ISSN 0141-8130
    DOI 10.1016/j.ijbiomac.2020.08.157
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  9. Artikel ; Online: A cell-based ELISA as surrogate of virus neutralization assay for RBD SARS-CoV-2 specific antibodies.

    Pi-Estopiñan, Franciscary / Pérez, María Teresa / Fraga, Anitza / Bergado, Gretchen / Díaz, Geidy D / Orosa, Ivette / Díaz, Marianniz / Solozábal, Joaquín Antonio / Rodríguez, Laura Marta / Garcia-Rivera, Dagmar / Macías, Consuelo / Jerez, Yanet / Casadesús, Ana V / Fernández-Marrero, Briandy / Bermúdez, Ernesto / Plasencia, Claudia A / Sánchez, Belinda / Hernández, Tays

    Vaccine

    2022  Band 40, Heft 13, Seite(n) 1958–1967

    Abstract: SARS-CoV-2, the cause of the COVID-19 pandemic, has provoked a global crisis and death of millions of people. Several serological assays to determine the quality of the immune response against SARS-CoV-2 and the efficacy of vaccines have been developed, ... ...

    Abstract SARS-CoV-2, the cause of the COVID-19 pandemic, has provoked a global crisis and death of millions of people. Several serological assays to determine the quality of the immune response against SARS-CoV-2 and the efficacy of vaccines have been developed, among them the gold standard conventional virus neutralization assays. However, these tests are time consuming, require biosafety level 3 (BSL3), and are low throughput and expensive. This has motivated the development of alternative methods, including molecular inhibition assays. Herein, we present a safe cell-based ELISA-virus neutralization test (cbE-VNT) as a surrogate for the conventional viral neutralization assays that detects the inhibition of SARS-CoV-2 RBD binding to ACE2-bearing cells independently of species. Our test shows a very good correlation with the conventional and molecular neutralization assays and achieves 100% specificity and 95% sensitivity. cbE-VNT is cost-effective, fast and enables a large-scale serological evaluation that can be performed in a BSL2 laboratory, allowing its use in pre-clinical and clinical investigations.
    Mesh-Begriff(e) Antibodies, Neutralizing ; Antibodies, Viral ; COVID-19/diagnosis ; Enzyme-Linked Immunosorbent Assay/methods ; Humans ; Neutralization Tests/methods ; Pandemics/prevention & control ; SARS-CoV-2 ; Spike Glycoprotein, Coronavirus
    Chemische Substanzen Antibodies, Neutralizing ; Antibodies, Viral ; Spike Glycoprotein, Coronavirus ; spike protein, SARS-CoV-2
    Sprache Englisch
    Erscheinungsdatum 2022-02-15
    Erscheinungsland Netherlands
    Dokumenttyp Journal Article
    ZDB-ID 605674-x
    ISSN 1873-2518 ; 0264-410X
    ISSN (online) 1873-2518
    ISSN 0264-410X
    DOI 10.1016/j.vaccine.2022.02.044
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  10. Artikel ; Online: Bacitracin is a non-competitive inhibitor of porcine M1 family neutral and glutamyl aminopeptidases.

    Arrebola, Yarini / Rivera, Laura / Pedroso, Alejandro / McGuire, Rory / Tresanco, Mario E Valdes / Bergado, Gretchen / Charli, Jean-Louis / Sánchez, Belinda / Pascual Alonso, Isel

    Natural product research

    2019  Band 35, Heft 17, Seite(n) 2958–2962

    Abstract: Membrane alanyl and glutamyl aminopeptidases (APN and APA, respectively) are established targets for the development of biomedical tools in human pathologies. APN overexpression correlates with the progression of tumours, including melanoma. Bacitracin, ... ...

    Abstract Membrane alanyl and glutamyl aminopeptidases (APN and APA, respectively) are established targets for the development of biomedical tools in human pathologies. APN overexpression correlates with the progression of tumours, including melanoma. Bacitracin, widely used as a topical antibiotic, inhibits subtilisin-like serine peptidases and disulphide isomerases. In the present contribution, we demonstrate that bacitracin is a non-competitive
    Mesh-Begriff(e) Animals ; Bacitracin/pharmacology ; CD13 Antigens/antagonists & inhibitors ; Cell Line, Tumor ; Glutamyl Aminopeptidase/antagonists & inhibitors ; Kidney ; Mice ; Swine
    Chemische Substanzen Bacitracin (1405-87-4) ; CD13 Antigens (EC 3.4.11.2) ; Glutamyl Aminopeptidase (EC 3.4.11.7)
    Sprache Englisch
    Erscheinungsdatum 2019-10-25
    Erscheinungsland England
    Dokumenttyp Journal Article
    ZDB-ID 2185747-7
    ISSN 1478-6427 ; 1478-6419
    ISSN (online) 1478-6427
    ISSN 1478-6419
    DOI 10.1080/14786419.2019.1678611
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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