Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Tânia Filipa Custódio"'
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-8 (2019)
Nature Communications
Paulsen, P A, Custódio, T F & Pedersen, B P 2019, ' Crystal structure of the plant symporter STP10 illuminates sugar uptake mechanism in monosaccharide transporter superfamily ', Nature Communications, vol. 10, no. 1, 407 . https://doi.org/10.1038/s41467-018-08176-9
Nature Communications 10(1), 407 (1-8) (2019). doi:10.1038/s41467-018-08176-9
Nature Communications
Paulsen, P A, Custódio, T F & Pedersen, B P 2019, ' Crystal structure of the plant symporter STP10 illuminates sugar uptake mechanism in monosaccharide transporter superfamily ', Nature Communications, vol. 10, no. 1, 407 . https://doi.org/10.1038/s41467-018-08176-9
Nature Communications 10(1), 407 (1-8) (2019). doi:10.1038/s41467-018-08176-9
Plants are dependent on controlled sugar uptake for correct organ development and sugar storage, and apoplastic sugar depletion is a defense strategy against microbial infections like rust and mildew. Uptake of glucose and other monosaccharides is me
Autor:
Maria Garcia-Alai, Leonardo G. Alonso, Lisandro H. Otero, Lucas A. Defelipe, Patricio O. Craig, Lucio Aliperti, Ramiro Lorenzo, Sebastián Klinke, Kim Remans, Stephan Niebling, Ignacio E. Sánchez, Tânia Filipa Custódio, Jennifer J. Schwarz, Christian Löw
The spike is the main protein component of the SARS-CoV-2 virion surface. The spike receptor binding motif mediates recognition of the hACE2 receptor, a critical infection step, and is the preferential target for spike-neutralizing antibodies. Post-t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2edea2099ed926c56d4017707ae29159
https://doi.org/10.1101/2021.05.20.445042
https://doi.org/10.1101/2021.05.20.445042
Structural comparison of GLUT1 to GLUT3 reveal transport regulation mechanism in sugar porter family
Publikováno v:
Custódio, T F, Paulsen, P A, Frain, K M & Pedersen, B P 2021, ' Structural comparison of GLUT1 to GLUT3 reveal transport regulation mechanism in sugar porter family ', Life science alliance, vol. 4, no. 4, e202000858 . https://doi.org/10.26508/LSA.202000858
Life Science Alliance
Custódio, T F, Paulsen, P A, Frain, K M & Pedersen, B P 2021, ' Structural comparison of GLUT1 to GLUT3 reveal transport regulation mechanism in sugar porter family ', Life science alliance, vol. 4, no. 4, e202000858 . https://doi.org/10.26508/lsa.202000858
Life science alliance 4(4), e202000858-(2021). doi:10.26508/lsa.202000858
Life Science Alliance
Custódio, T F, Paulsen, P A, Frain, K M & Pedersen, B P 2021, ' Structural comparison of GLUT1 to GLUT3 reveal transport regulation mechanism in sugar porter family ', Life science alliance, vol. 4, no. 4, e202000858 . https://doi.org/10.26508/lsa.202000858
Life science alliance 4(4), e202000858-(2021). doi:10.26508/lsa.202000858
Life science alliance 4(4), e202000858 - (2021). doi:10.26508/lsa.202000858
The human glucose transporters GLUT1 and GLUT3 have a central role in glucose uptake as canonical members of the Sugar Porter (SP) family. GLUT1 and GLUT3 share a fully
The human glucose transporters GLUT1 and GLUT3 have a central role in glucose uptake as canonical members of the Sugar Porter (SP) family. GLUT1 and GLUT3 share a fully
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f53753762c3c9712d626f126119100ad
Autor:
Cy M. Jeffries, Martin A. Schroer, Markus A. Seeger, Nikolay Dobrev, Melissa A. Graewert, Ben Murrell, Christian Löw, Joanna Pieprzyk, Tânia Filipa Custódio, B. M. Hällberg, Samuel Pazicky, Kim Remans, Daniel J. Sheward, Andrey Yu. Gruzinov, Leo Hanke, M. Sorgenfrei, Hrishikesh Das, Gerald M. McInerney, Dmitri I. Svergun
Publikováno v:
Nature Communications
Nature Communications 11(1), 5588 (2020). doi:10.1038/s41467-020-19204-y
Nature Communications, Vol 11, Iss 1, Pp 1-11 (2020)
Nature Communications 11(1), 5588 (2020). doi:10.1038/s41467-020-19204-y
Nature Communications, Vol 11, Iss 1, Pp 1-11 (2020)
The coronavirus SARS-CoV-2 is the cause of the ongoing COVID-19 pandemic. Therapeutic neutralizing antibodies constitute a key short-to-medium term approach to tackle COVID-19. However, traditional antibody production is hampered by long development
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2d70a414e35750147a9c3655b7be1d6f
https://doi.org/10.5167/uzh-196534
https://doi.org/10.5167/uzh-196534
Autor:
Tânia Filipa Custódio, Ramiro Lorenzo, Sebastián Klinke, Ignacio E. Sánchez, Kim Remans, Lisandro H. Otero, Maria Garcia-Alai, Jennifer J. Schwarz, Stephan Niebling, Leonardo G. Alonso, Lucas A. Defelipe, Lucio Aliperti, Christian Löw, Patricio O. Craig
Publikováno v:
CONICET Digital (CONICET)
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
The Journal of Biological Chemistry
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
The Journal of Biological Chemistry
The spike protein is the main protein component of the SARS-CoV-2 virion surface. The spike receptor-binding motif mediates recognition of the human angiotensin-converting enzyme 2 (hACE2) receptor, a critical step in infection, and is the preferenti