Zobrazeno 1 - 10
of 17
pro vyhledávání: '"protein complexe"'
Oxygenic phototrophs use the Calvin–Benson cycle to fix CO2 during photosynthesis. In the dark, glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and phosphoribulokinase (PRK), two enzymes of the Calvin–Benson cycle, form an inactive complex with
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f7adb03f2d8e6252768a3d67894dd258
http://hdl.handle.net/11585/851372
http://hdl.handle.net/11585/851372
Autor:
Noack, Lise
Publikováno v:
Subcellular Processes [q-bio.SC]. Université de Lyon, 2020. English. ⟨NNT : 2020LYSEN066⟩
Eukaryotic cells are composed of several membrane-surrounded compartments. Each compartment has a unique physicochemical environment delimited by a membrane with a specific biochemical and biophysical identity. The membrane identity includes the natu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::ded65c9fa31ac22a3138ff61d673caf4
https://theses.hal.science/tel-03099332/file/NOACK_Lise_2020LYSEN066_These_VD.pdf
https://theses.hal.science/tel-03099332/file/NOACK_Lise_2020LYSEN066_These_VD.pdf
Autophagy is an extremely dynamic process that mediates the rapid degradation of intracellular components in response to different stress conditions. The autophagic response is executed by specific protein complexes, whose function is regulated by po
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ca3e740c358b16d48b7852f2f1836bf1
https://hdl.handle.net/11587/409223
https://hdl.handle.net/11587/409223
Autor:
Emilio Marengo, Jose Alejandro Muñoz Tabares, Marcello Manfredi, Cristina Pagliano, James Barber, Pascal Albanese, Jon Nield, Guido Saracco, Angelica Chiodoni, Fabio Gosetti
In higher plants, photosystem II (PSII) is a multi-subunit pigment-protein complex embedded in the thylakoid membranes of chloroplasts, where it is present mostly in dimeric form within the grana. Its light-harvesting antenna system, LHCII, is compos
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a7be27460f783113d6b7d67ef6b7be71
http://hdl.handle.net/11583/2652216
http://hdl.handle.net/11583/2652216
Autor:
Freeman, Jamie, Smith, David, Latinkic, Branko, Ewan, Ken, Samuel, Lee, Zollo, Massimo, Marino, Natascia, Tyas, Lorraine, Jones, Nick, Dale, Trevor C.
Publikováno v:
Molecular Cancer
Background Wnt/β-catenin signaling is often portrayed as a simple pathway that is initiated by Wnt ligand at the cell surface leading, via linear series of interactions between ‘core pathway’ members, to the induction of nuclear transcription fr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::c65269d7a3876547543bc75eb3eb9ff2
https://orca.cardiff.ac.uk/id/eprint/83967/1/art%3A10.1186%2Fs12943-015-0475-1.pdf
https://orca.cardiff.ac.uk/id/eprint/83967/1/art%3A10.1186%2Fs12943-015-0475-1.pdf
Autor:
Rita Zilhão, Giuseppina Cangiano, Maurilio De Felice, Adriano O. Henriques, Rachele Isticato, Sofia Nolasco, Giovanni Esposito, Ezio Ricca
Publikováno v:
Journal of Bacteriology. 186:1129-1135
We report evidence that the CotC polypeptide, a previously identified component of the Bacillus subtilis spore coat, is assembled into at least four distinct forms. Two of these, having molecular masses of 12 and 21 kDa, appeared 8 h after the onset
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::85aeac3d3bc1ec677d0f73e8e67c87a6
https://doi.org/10.1128/jb.186.4.1129-1135.2004
https://doi.org/10.1128/jb.186.4.1129-1135.2004
Autor:
Kremer, Adrian, Bietlot, Emerance, Zanelli, Alberto, Malicka, Joanna M., Armaroli, Nicola, Bonifazi, Davide
Publikováno v:
Chemistry (Weinh., Print) 21 (2015): 1108–1117. doi:10.1002/chem.201404372
info:cnr-pdr/source/autori:Kremer, Adrian and Bietlot, Emerance and Zanelli, Alberto and Malicka, Joanna M. and Armaroli, Nicola and Bonifazi, Davide/titolo:Versatile Bisethynyl[60]fulleropyrrolidine Scaffolds for Mimicking Artificial Light-Harvesting Photoreaction Centers/doi:10.1002%2Fchem.201404372/rivista:Chemistry (Weinh., Print)/anno:2015/pagina_da:1108/pagina_a:1117/intervallo_pagine:1108–1117/volume:21
info:cnr-pdr/source/autori:Kremer, Adrian and Bietlot, Emerance and Zanelli, Alberto and Malicka, Joanna M. and Armaroli, Nicola and Bonifazi, Davide/titolo:Versatile Bisethynyl[60]fulleropyrrolidine Scaffolds for Mimicking Artificial Light-Harvesting Photoreaction Centers/doi:10.1002%2Fchem.201404372/rivista:Chemistry (Weinh., Print)/anno:2015/pagina_da:1108/pagina_a:1117/intervallo_pagine:1108–1117/volume:21
Fullerene-based tetrads, triads, and dyads are presented in which [60]fulleropyrrolidine synthons are linked to an oligo(p-phenyleneethynylene) antenna at the nitrogen atom and to electron-donor phenothiazine (PTZ) and/or ferrocene (Fc) moieties at t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::67623fab726c63f8c2318cd33a9016a3
http://hdl.handle.net/11368/2869719
http://hdl.handle.net/11368/2869719
Autor:
Halabelian, Levon, Ricagno, Stefano, Giorgetti, Sofia, Santambrogio, Carlo, Barbiroli, Alberto, Pellegrino, Sara, Achour, Adnane, Grandori, Rita, Marchese, Loredana, Raimondi, Sara, Mangione, P. Patrizia, Esposito, Gennaro, Al-Shawi, Raya, Simons, J. Paul, Speck, Ivana, Stoppini, Monica, Bolognesi, Martino, Bellotti, Vittorio
Publikováno v:
'Journal of Biological Chemistry ', vol: 289, pages: 3318-3327 (2014)
The Journal of Biological Chemistry
The Journal of Biological Chemistry
Background: Amyloidogenic D76N β2m variant escapes the intracellular quality control despite its instability. Results: We show tridimensional structure and stability of D76N β2m assembled within MHCI compared with the wild type protein. Conclusion:
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::c897a785395320ef4911f8885cdbe49d
http://hdl.handle.net/10281/95744
http://hdl.handle.net/10281/95744
Autor:
Francesco Trapasso, Alfina Quintiero, Cinzia Raso, Tiziana Palumbo, Ilaria Le Pera, Alfredo Fusco, Giuseppe Viglietto, Dario Palmieri, Carlo M. Croce, Flavia Pichiorri, Tullio Florio, Alessandra Pattarozzi, Rodolfo Iuliano
Publikováno v:
Journal of Biochemistry (Tokyo) (2009).
info:cnr-pdr/source/autori:Iuliano R, Raso C, Quintiero A, Pera IL, Pichiorri F, Palumbo T, Palmieri D, Pattarozzi A, Florio T, Viglietto G, Trapasso F, Croce CM, Fusco A./titolo:The eighth fibronectin type III domain of protein tyrosine phosphatase receptor J influences the formation of protein complexes and cell localization./doi:/rivista:Journal of Biochemistry (Tokyo)/anno:2009/pagina_da:/pagina_a:/intervallo_pagine:/volume
info:cnr-pdr/source/autori:Iuliano R, Raso C, Quintiero A, Pera IL, Pichiorri F, Palumbo T, Palmieri D, Pattarozzi A, Florio T, Viglietto G, Trapasso F, Croce CM, Fusco A./titolo:The eighth fibronectin type III domain of protein tyrosine phosphatase receptor J influences the formation of protein complexes and cell localization./doi:/rivista:Journal of Biochemistry (Tokyo)/anno:2009/pagina_da:/pagina_a:/intervallo_pagine:/volume
Regulation of receptor-type phosphatases can involve the formation of higher-order structures, but the exact role played in this process by protein domains is not well understood. In this study we show the formation of different higher-order structur
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::66871165601073346e19b1ccaa4390c7
https://publications.cnr.it/doc/21179
https://publications.cnr.it/doc/21179
Autor:
Gabriel Waksman, Tina Daviter, Sheena E. Radford, Denis Verger, Alison E. Ashcroft, Han Remaut, Emanuele Paci, R.J. Rose
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 105(35)
P pili are multisubunit fibers essential for the attachment of uropathogenic Escherichia coli to the kidney. These fibers are formed by the noncovalent assembly of six different homologous subunit types in an array that is strictly defined in terms o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6b103a5404ac6fd1d36b35d195a2739a
https://pubmed.ncbi.nlm.nih.gov/18728178
https://pubmed.ncbi.nlm.nih.gov/18728178