Zobrazeno 1 - 10
of 32
pro vyhledávání: '"Julián Gómez-Gutiérrez"'
Publikováno v:
Bio-Protocol, Vol 8, Iss 23 (2018)
In order to study the mechanism underlying the Hepatitis C Virus (HCV) fusion process we have performed assays using phospholipid liposomes and a truncated form of E2 protein, E2661 (amino acids 384-661 of the HCV polyprotein) lacking the transmembra
Externí odkaz:
https://doaj.org/article/479134fbc62c48e497008218808478ca
Publikováno v:
Bio-Protocol, Vol 8, Iss 19 (2018)
In this protocol, we describe the production and purification of the ectodomain of the E2661 envelope protein (amino acids 384-661) of the Hepatitis C virus, which plays a fundamental role in the entry of the virus into the host cell. This protein ha
Externí odkaz:
https://doaj.org/article/46abe5573c254d3f98fa1a455b5699c0
Publikováno v:
Bio Protoc
In this protocol, we describe the production and purification of the ectodomain of the E2(661) envelope protein (amino acids 384-661) of the Hepatitis C virus, which plays a fundamental role in the entry of the virus into the host cell. This protein
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c8eef74b09b1a567c855b14a899d173d
https://pubmed.ncbi.nlm.nih.gov/34532509
https://pubmed.ncbi.nlm.nih.gov/34532509
Publikováno v:
Bio Protoc
In order to study the mechanism underlying the Hepatitis C Virus (HCV) fusion process we have performed assays using phospholipid liposomes and a truncated form of E2 protein, E2(661) (amino acids 384-661 of the HCV polyprotein) lacking the transmemb
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::257fd9dbe11d4008aacb027bcf51d8cb
https://doi.org/10.21769/bioprotoc.3108
https://doi.org/10.21769/bioprotoc.3108
Autor:
Daniel Tello, Mar Rodríguez-Rodríguez, Julián Gómez-Gutiérrez, Belén Yélamos, Francisco Gavilanes, Darrell L. Peterson
Publikováno v:
Biochimica et biophysica acta. Biomembranes. 1860(3)
The steps leading from hepatitis C virus (HCV) attachment to the hepatocytes to the fusion of viral and cellular membranes remain uncharacterized. In this regard, we have studied the mechanism underlying the HCV fusion process using liposomes and a t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6ba0ca80fa1816b49e333fc3827adecf
https://pubmed.ncbi.nlm.nih.gov/29273334
https://pubmed.ncbi.nlm.nih.gov/29273334
Autor:
Julián Gómez-Gutiérrez, Sara Ortega-Atienza, Laura Lombana, Belén Yélamos, Darrell L. Peterson, Francisco Gavilanes
Publikováno v:
E-Prints Complutense. Archivo Institucional de la UCM
instname
E-Prints Complutense: Archivo Institucional de la UCM
Universidad Complutense de Madrid
instname
E-Prints Complutense: Archivo Institucional de la UCM
Universidad Complutense de Madrid
We have obtained a chimeric protein containing the ectodomains of hepatitis C virus (HCV) envelope proteins but lacking the region 268-292 of E1. All its structural properties are coincident with those of the corresponding full length chimera. The de
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::996b90c69a540a8f8e67eb4edd0ffef5
http://eprints.ucm.es/36213/
http://eprints.ucm.es/36213/
Autor:
Sylvia Ayora, Mª José Feito, Julián Gómez-Gutiérrez, Darrell L. Peterson, Juan C. Alonso, Francisco Gavilanes
Publikováno v:
Virus Research. 135:166-174
West Nile virus (WNV) is a member of the Flaviviridae family of positive-strand RNA viruses. Its viral RNA is translated to produce a polyprotein precursor that is further processed into three structural and seven non-structural proteins. The non-str
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::84b4d37f0e8d997cdc7bdcec97981dce
https://doi.org/10.1016/j.virusres.2008.03.008
https://doi.org/10.1016/j.virusres.2008.03.008
Autor:
Francisco Gavilanes, Julián Gómez-Gutiérrez, Elena Núñez, Carmen Delgado, Darrell L. Peterson, Belén Yélamos
Publikováno v:
E-Prints Complutense. Archivo Institucional de la UCM
instname
E-Prints Complutense: Archivo Institucional de la UCM
Universidad Complutense de Madrid
instname
E-Prints Complutense: Archivo Institucional de la UCM
Universidad Complutense de Madrid
In a previous study, it was shown that purified preS domains of hepatitis B virus (HBV) could interact with acidic phospholipid vesicles and induce aggregation, lipid mixing and leakage of internal contents which could be indicative of their involvem
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fb21c9e26e75f83d095b94cba12f1446
http://eprints.ucm.es/33640/
http://eprints.ucm.es/33640/
Autor:
Julián Gómez-Gutiérrez, Darrell L. Peterson, Belén Yélamos, Beatriz Pacheco, Juan Pablo Albar, Francisco Gavilanes, Fernando Roncal, Carmen Delgado
Publikováno v:
E-Prints Complutense. Archivo Institucional de la UCM
instname
E-Prints Complutense: Archivo Institucional de la UCM
Universidad Complutense de Madrid
instname
E-Prints Complutense: Archivo Institucional de la UCM
Universidad Complutense de Madrid
Based on the predicted capacity to interact with membranes at the interface, we have found three regions in the ectodomain of the hepatitis C virus envelope glycoprotein E2 (430-449, 543-560 and 603-624) with the ability to destabilize membranes. Thr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d0f351590dbf07abaee7b050951266b3
Autor:
Julián Gómez-Gutiérrez, Belén Yélamos, Francisco Gavilanes, Darrell L. Peterson, Daniel Tello, Mar Rodríguez-Rodríguez
Publikováno v:
E-Prints Complutense: Archivo Institucional de la UCM
Universidad Complutense de Madrid
E-Prints Complutense. Archivo Institucional de la UCM
instname
Universidad Complutense de Madrid
E-Prints Complutense. Archivo Institucional de la UCM
instname
In this report it is described for the first time the expression and purification of large quantities of a soluble and correctly folded chimeric recombinant protein, E2661E1340, containing the permuted Hepatitis C virus (HCV) glycoprotein ectodomains
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::24a8a662222c11cc70865c49a868d997