A quinolin-8-ol sub-millimolar inhibitor of UGGT, the ER glycoprotein folding quality control checkpoint
- Autores
- Guay, Kevin P.; Ibba, Roberta; Kiappes, J. L.; Vasiljevic, Snezana; Bonì, Francesco; De Benedictis, Maria; Zeni, Ilaria; Le Cornu, James D.; Hensen, Mario; Chandran, Anu V.; Kantsadi, Anastassia L.; Caputo, Alessandro T.; Blanco Capurro, Juan Ignacio; Bayo, Yusupha; Hill, Johan C.; Hudson, Kieran; Lia, Andrea; Brun, Juliane; Withers, Stephen G.; Marti, Marcelo Adrian; Biasini, Emiliano; Santino, Angelo; De Rosa, Matteo; Milani, Mario; Modenutti, Carlos Pablo; Hebert, Daniel N.; Zitzmann, Nicole; Roversi, Pietro
- Año de publicación
- 2023
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Misfolded glycoprotein recognition and endoplasmic reticulum (ER) retention are mediated by the ER glycoprotein folding quality control (ERQC) checkpoint enzyme, UDP-glucose glycoprotein glucosyltransferase (UGGT). UGGT modulation is a promising strategy for broad-spectrum antivirals, rescue-of-secretion therapy in rare disease caused by responsive mutations in glycoprotein genes, and many cancers, but to date no selective UGGT inhibitors are known. The small molecule 5-[(morpholin-4-yl)methyl]quinolin-8-ol (5M-8OH-Q) binds a CtUGGTGT24 "WY" conserved surface motif conserved across UGGTs but not present in other GT24 family glycosyltransferases. 5M-8OH-Q has a 47 μM binding affinity for CtUGGTGT24in vitro as measured by ligand-enhanced fluorescence. In cellula, 5M-8OH-Q inhibits both human UGGT isoforms at concentrations higher than 750 μM. 5M-8OH-Q binding to CtUGGTGT24 appears to be mutually exclusive to M5-9 glycan binding in an in vitro competition experiment. A medicinal program based on 5M-8OH-Q will yield the next generation of UGGT inhibitors.
Fil: Guay, Kevin P.. Massachusetts Institute of Technology; Estados Unidos
Fil: Ibba, Roberta. University of Sassari; Italia
Fil: Kiappes, J. L.. Institute for Nanoscience Discovery; Reino Unido
Fil: Vasiljevic, Snezana. Institute for Nanoscience Discovery; Reino Unido
Fil: Bonì, Francesco. Università degli Studi di Milano; Italia
Fil: De Benedictis, Maria. Institute of Sciences of Food Production; Italia
Fil: Zeni, Ilaria. Universita degli Studi di Trento; Italia
Fil: Le Cornu, James D.. University of Edinburgh; Reino Unido
Fil: Hensen, Mario. Institute for Nanoscience Discovery; Reino Unido
Fil: Chandran, Anu V.. Institute for Nanoscience Discovery; Reino Unido
Fil: Kantsadi, Anastassia L.. Institute for Nanoscience Discovery; Reino Unido
Fil: Caputo, Alessandro T.. Commonwealth Scientific And Industrial Research Organisation (csiro);
Fil: Blanco Capurro, Juan Ignacio. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina
Fil: Bayo, Yusupha. Università degli Studi di Milano; Italia
Fil: Hill, Johan C.. Institute for Nanoscience Discovery; Reino Unido
Fil: Hudson, Kieran. University of British Columbia; Canadá
Fil: Lia, Andrea. Institute for Nanoscience Discovery; Reino Unido
Fil: Brun, Juliane. Institute for Nanoscience Discovery; Reino Unido
Fil: Withers, Stephen G.. University of British Columbia; Canadá
Fil: Marti, Marcelo Adrian. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina
Fil: Biasini, Emiliano. Universita degli Studi di Trento; Italia
Fil: Santino, Angelo. Institute of Sciences of Food Production; Italia
Fil: De Rosa, Matteo. Università degli Studi di Milano; Italia
Fil: Milani, Mario. Università degli Studi di Milano; Italia
Fil: Modenutti, Carlos Pablo. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina
Fil: Hebert, Daniel N.. Massachusetts Institute of Technology; Estados Unidos
Fil: Zitzmann, Nicole. Institute for Nanoscience Discovery; Reino Unido
Fil: Roversi, Pietro. University of Leicester; Reino Unido - Materia
- Misfolded glycoprotein
- Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
- Repositorio
.jpg)
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/261574
Ver los metadatos del registro completo
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A quinolin-8-ol sub-millimolar inhibitor of UGGT, the ER glycoprotein folding quality control checkpointGuay, Kevin P.Ibba, RobertaKiappes, J. L.Vasiljevic, SnezanaBonì, FrancescoDe Benedictis, MariaZeni, IlariaLe Cornu, James D.Hensen, MarioChandran, Anu V.Kantsadi, Anastassia L.Caputo, Alessandro T.Blanco Capurro, Juan IgnacioBayo, YusuphaHill, Johan C.Hudson, KieranLia, AndreaBrun, JulianeWithers, Stephen G.Marti, Marcelo AdrianBiasini, EmilianoSantino, AngeloDe Rosa, MatteoMilani, MarioModenutti, Carlos PabloHebert, Daniel N.Zitzmann, NicoleRoversi, PietroMisfolded glycoproteinhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Misfolded glycoprotein recognition and endoplasmic reticulum (ER) retention are mediated by the ER glycoprotein folding quality control (ERQC) checkpoint enzyme, UDP-glucose glycoprotein glucosyltransferase (UGGT). UGGT modulation is a promising strategy for broad-spectrum antivirals, rescue-of-secretion therapy in rare disease caused by responsive mutations in glycoprotein genes, and many cancers, but to date no selective UGGT inhibitors are known. The small molecule 5-[(morpholin-4-yl)methyl]quinolin-8-ol (5M-8OH-Q) binds a CtUGGTGT24 "WY" conserved surface motif conserved across UGGTs but not present in other GT24 family glycosyltransferases. 5M-8OH-Q has a 47 μM binding affinity for CtUGGTGT24in vitro as measured by ligand-enhanced fluorescence. In cellula, 5M-8OH-Q inhibits both human UGGT isoforms at concentrations higher than 750 μM. 5M-8OH-Q binding to CtUGGTGT24 appears to be mutually exclusive to M5-9 glycan binding in an in vitro competition experiment. A medicinal program based on 5M-8OH-Q will yield the next generation of UGGT inhibitors.Fil: Guay, Kevin P.. Massachusetts Institute of Technology; Estados UnidosFil: Ibba, Roberta. University of Sassari; ItaliaFil: Kiappes, J. L.. Institute for Nanoscience Discovery; Reino UnidoFil: Vasiljevic, Snezana. Institute for Nanoscience Discovery; Reino UnidoFil: Bonì, Francesco. Università degli Studi di Milano; ItaliaFil: De Benedictis, Maria. Institute of Sciences of Food Production; ItaliaFil: Zeni, Ilaria. Universita degli Studi di Trento; ItaliaFil: Le Cornu, James D.. University of Edinburgh; Reino UnidoFil: Hensen, Mario. Institute for Nanoscience Discovery; Reino UnidoFil: Chandran, Anu V.. Institute for Nanoscience Discovery; Reino UnidoFil: Kantsadi, Anastassia L.. Institute for Nanoscience Discovery; Reino UnidoFil: Caputo, Alessandro T.. Commonwealth Scientific And Industrial Research Organisation (csiro);Fil: Blanco Capurro, Juan Ignacio. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; ArgentinaFil: Bayo, Yusupha. Università degli Studi di Milano; ItaliaFil: Hill, Johan C.. Institute for Nanoscience Discovery; Reino UnidoFil: Hudson, Kieran. University of British Columbia; CanadáFil: Lia, Andrea. Institute for Nanoscience Discovery; Reino UnidoFil: Brun, Juliane. Institute for Nanoscience Discovery; Reino UnidoFil: Withers, Stephen G.. University of British Columbia; CanadáFil: Marti, Marcelo Adrian. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; ArgentinaFil: Biasini, Emiliano. Universita degli Studi di Trento; ItaliaFil: Santino, Angelo. Institute of Sciences of Food Production; ItaliaFil: De Rosa, Matteo. Università degli Studi di Milano; ItaliaFil: Milani, Mario. Università degli Studi di Milano; ItaliaFil: Modenutti, Carlos Pablo. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; ArgentinaFil: Hebert, Daniel N.. Massachusetts Institute of Technology; Estados UnidosFil: Zitzmann, Nicole. Institute for Nanoscience Discovery; Reino UnidoFil: Roversi, Pietro. University of Leicester; Reino UnidoCell Press2023-10info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/261574Guay, Kevin P.; Ibba, Roberta; Kiappes, J. L.; Vasiljevic, Snezana; Bonì, Francesco; et al.; A quinolin-8-ol sub-millimolar inhibitor of UGGT, the ER glycoprotein folding quality control checkpoint; Cell Press; iScience; 26; 10; 10-2023; 1-192589-0042CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://linkinghub.elsevier.com/retrieve/pii/S258900422301996Xinfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.isci.2023.107919info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:37:32Zoai:ri.conicet.gov.ar:11336/261574instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 10:37:32.66CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
| dc.title.none.fl_str_mv |
A quinolin-8-ol sub-millimolar inhibitor of UGGT, the ER glycoprotein folding quality control checkpoint |
| title |
A quinolin-8-ol sub-millimolar inhibitor of UGGT, the ER glycoprotein folding quality control checkpoint |
| spellingShingle |
A quinolin-8-ol sub-millimolar inhibitor of UGGT, the ER glycoprotein folding quality control checkpoint Guay, Kevin P. Misfolded glycoprotein |
| title_short |
A quinolin-8-ol sub-millimolar inhibitor of UGGT, the ER glycoprotein folding quality control checkpoint |
| title_full |
A quinolin-8-ol sub-millimolar inhibitor of UGGT, the ER glycoprotein folding quality control checkpoint |
| title_fullStr |
A quinolin-8-ol sub-millimolar inhibitor of UGGT, the ER glycoprotein folding quality control checkpoint |
| title_full_unstemmed |
A quinolin-8-ol sub-millimolar inhibitor of UGGT, the ER glycoprotein folding quality control checkpoint |
| title_sort |
A quinolin-8-ol sub-millimolar inhibitor of UGGT, the ER glycoprotein folding quality control checkpoint |
| dc.creator.none.fl_str_mv |
Guay, Kevin P. Ibba, Roberta Kiappes, J. L. Vasiljevic, Snezana Bonì, Francesco De Benedictis, Maria Zeni, Ilaria Le Cornu, James D. Hensen, Mario Chandran, Anu V. Kantsadi, Anastassia L. Caputo, Alessandro T. Blanco Capurro, Juan Ignacio Bayo, Yusupha Hill, Johan C. Hudson, Kieran Lia, Andrea Brun, Juliane Withers, Stephen G. Marti, Marcelo Adrian Biasini, Emiliano Santino, Angelo De Rosa, Matteo Milani, Mario Modenutti, Carlos Pablo Hebert, Daniel N. Zitzmann, Nicole Roversi, Pietro |
| author |
Guay, Kevin P. |
| author_facet |
Guay, Kevin P. Ibba, Roberta Kiappes, J. L. Vasiljevic, Snezana Bonì, Francesco De Benedictis, Maria Zeni, Ilaria Le Cornu, James D. Hensen, Mario Chandran, Anu V. Kantsadi, Anastassia L. Caputo, Alessandro T. Blanco Capurro, Juan Ignacio Bayo, Yusupha Hill, Johan C. Hudson, Kieran Lia, Andrea Brun, Juliane Withers, Stephen G. Marti, Marcelo Adrian Biasini, Emiliano Santino, Angelo De Rosa, Matteo Milani, Mario Modenutti, Carlos Pablo Hebert, Daniel N. Zitzmann, Nicole Roversi, Pietro |
| author_role |
author |
| author2 |
Ibba, Roberta Kiappes, J. L. Vasiljevic, Snezana Bonì, Francesco De Benedictis, Maria Zeni, Ilaria Le Cornu, James D. Hensen, Mario Chandran, Anu V. Kantsadi, Anastassia L. Caputo, Alessandro T. Blanco Capurro, Juan Ignacio Bayo, Yusupha Hill, Johan C. Hudson, Kieran Lia, Andrea Brun, Juliane Withers, Stephen G. Marti, Marcelo Adrian Biasini, Emiliano Santino, Angelo De Rosa, Matteo Milani, Mario Modenutti, Carlos Pablo Hebert, Daniel N. Zitzmann, Nicole Roversi, Pietro |
| author2_role |
author author author author author author author author author author author author author author author author author author author author author author author author author author author |
| dc.subject.none.fl_str_mv |
Misfolded glycoprotein |
| topic |
Misfolded glycoprotein |
| purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
| dc.description.none.fl_txt_mv |
Misfolded glycoprotein recognition and endoplasmic reticulum (ER) retention are mediated by the ER glycoprotein folding quality control (ERQC) checkpoint enzyme, UDP-glucose glycoprotein glucosyltransferase (UGGT). UGGT modulation is a promising strategy for broad-spectrum antivirals, rescue-of-secretion therapy in rare disease caused by responsive mutations in glycoprotein genes, and many cancers, but to date no selective UGGT inhibitors are known. The small molecule 5-[(morpholin-4-yl)methyl]quinolin-8-ol (5M-8OH-Q) binds a CtUGGTGT24 "WY" conserved surface motif conserved across UGGTs but not present in other GT24 family glycosyltransferases. 5M-8OH-Q has a 47 μM binding affinity for CtUGGTGT24in vitro as measured by ligand-enhanced fluorescence. In cellula, 5M-8OH-Q inhibits both human UGGT isoforms at concentrations higher than 750 μM. 5M-8OH-Q binding to CtUGGTGT24 appears to be mutually exclusive to M5-9 glycan binding in an in vitro competition experiment. A medicinal program based on 5M-8OH-Q will yield the next generation of UGGT inhibitors. Fil: Guay, Kevin P.. Massachusetts Institute of Technology; Estados Unidos Fil: Ibba, Roberta. University of Sassari; Italia Fil: Kiappes, J. L.. Institute for Nanoscience Discovery; Reino Unido Fil: Vasiljevic, Snezana. Institute for Nanoscience Discovery; Reino Unido Fil: Bonì, Francesco. Università degli Studi di Milano; Italia Fil: De Benedictis, Maria. Institute of Sciences of Food Production; Italia Fil: Zeni, Ilaria. Universita degli Studi di Trento; Italia Fil: Le Cornu, James D.. University of Edinburgh; Reino Unido Fil: Hensen, Mario. Institute for Nanoscience Discovery; Reino Unido Fil: Chandran, Anu V.. Institute for Nanoscience Discovery; Reino Unido Fil: Kantsadi, Anastassia L.. Institute for Nanoscience Discovery; Reino Unido Fil: Caputo, Alessandro T.. Commonwealth Scientific And Industrial Research Organisation (csiro); Fil: Blanco Capurro, Juan Ignacio. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina Fil: Bayo, Yusupha. Università degli Studi di Milano; Italia Fil: Hill, Johan C.. Institute for Nanoscience Discovery; Reino Unido Fil: Hudson, Kieran. University of British Columbia; Canadá Fil: Lia, Andrea. Institute for Nanoscience Discovery; Reino Unido Fil: Brun, Juliane. Institute for Nanoscience Discovery; Reino Unido Fil: Withers, Stephen G.. University of British Columbia; Canadá Fil: Marti, Marcelo Adrian. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina Fil: Biasini, Emiliano. Universita degli Studi di Trento; Italia Fil: Santino, Angelo. Institute of Sciences of Food Production; Italia Fil: De Rosa, Matteo. Università degli Studi di Milano; Italia Fil: Milani, Mario. Università degli Studi di Milano; Italia Fil: Modenutti, Carlos Pablo. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina Fil: Hebert, Daniel N.. Massachusetts Institute of Technology; Estados Unidos Fil: Zitzmann, Nicole. Institute for Nanoscience Discovery; Reino Unido Fil: Roversi, Pietro. University of Leicester; Reino Unido |
| description |
Misfolded glycoprotein recognition and endoplasmic reticulum (ER) retention are mediated by the ER glycoprotein folding quality control (ERQC) checkpoint enzyme, UDP-glucose glycoprotein glucosyltransferase (UGGT). UGGT modulation is a promising strategy for broad-spectrum antivirals, rescue-of-secretion therapy in rare disease caused by responsive mutations in glycoprotein genes, and many cancers, but to date no selective UGGT inhibitors are known. The small molecule 5-[(morpholin-4-yl)methyl]quinolin-8-ol (5M-8OH-Q) binds a CtUGGTGT24 "WY" conserved surface motif conserved across UGGTs but not present in other GT24 family glycosyltransferases. 5M-8OH-Q has a 47 μM binding affinity for CtUGGTGT24in vitro as measured by ligand-enhanced fluorescence. In cellula, 5M-8OH-Q inhibits both human UGGT isoforms at concentrations higher than 750 μM. 5M-8OH-Q binding to CtUGGTGT24 appears to be mutually exclusive to M5-9 glycan binding in an in vitro competition experiment. A medicinal program based on 5M-8OH-Q will yield the next generation of UGGT inhibitors. |
| publishDate |
2023 |
| dc.date.none.fl_str_mv |
2023-10 |
| dc.type.none.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion http://purl.org/coar/resource_type/c_6501 info:ar-repo/semantics/articulo |
| format |
article |
| status_str |
publishedVersion |
| dc.identifier.none.fl_str_mv |
http://hdl.handle.net/11336/261574 Guay, Kevin P.; Ibba, Roberta; Kiappes, J. L.; Vasiljevic, Snezana; Bonì, Francesco; et al.; A quinolin-8-ol sub-millimolar inhibitor of UGGT, the ER glycoprotein folding quality control checkpoint; Cell Press; iScience; 26; 10; 10-2023; 1-19 2589-0042 CONICET Digital CONICET |
| url |
http://hdl.handle.net/11336/261574 |
| identifier_str_mv |
Guay, Kevin P.; Ibba, Roberta; Kiappes, J. L.; Vasiljevic, Snezana; Bonì, Francesco; et al.; A quinolin-8-ol sub-millimolar inhibitor of UGGT, the ER glycoprotein folding quality control checkpoint; Cell Press; iScience; 26; 10; 10-2023; 1-19 2589-0042 CONICET Digital CONICET |
| dc.language.none.fl_str_mv |
eng |
| language |
eng |
| dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/url/https://linkinghub.elsevier.com/retrieve/pii/S258900422301996X info:eu-repo/semantics/altIdentifier/doi/10.1016/j.isci.2023.107919 |
| dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-nd/2.5/ar/ |
| eu_rights_str_mv |
openAccess |
| rights_invalid_str_mv |
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/ |
| dc.format.none.fl_str_mv |
application/pdf application/pdf |
| dc.publisher.none.fl_str_mv |
Cell Press |
| publisher.none.fl_str_mv |
Cell Press |
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reponame:CONICET Digital (CONICET) instname:Consejo Nacional de Investigaciones Científicas y Técnicas |
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Consejo Nacional de Investigaciones Científicas y Técnicas |
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CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas |
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dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar |
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13.070432 |