The role of RGGA RNA binding protein in plant response to osmotic stress

Autor: Ambrosone A., Batelli G., Nurcato R., Aurilia V., Punzo P., BangarusamyK.D., Ruberti I., Sassi M., Leone A., Costa A., Grillo S.

Publikováno v: The 3rd Spot-ITN Conference, Stress Biology and Crop Fertility, pp. 48–48, Sorrento, Italy, March, 18-22 2015
info:cnr-pdr/source/autori:Ambrosone A., Batelli G., Nurcato R., Aurilia V., Punzo P., BangarusamyK.D., Ruberti I., Sassi M., Leone A., Costa A., Grillo S./congresso_nome:The 3rd Spot-ITN Conference, Stress Biology and Crop Fertility/congresso_luogo:Sorrento, Italy/congresso_data:March, 18-22 2015/anno:2015/pagina_da:48/pagina_a:48/intervallo_pagine:48–48

Osmotic stress critically limits plant growth and crop productivity. The identification of genes underlying the mechanisms of stress response is the subject of intense research in plant biology. Through microarray analyses we previously identified an

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=cnr_________::c562e96a6bf14ac9ecff780d103db3a5
http://3rdconference.spot-itn.eu/wp-content/uploads/2015/10/bookabstract.pdf

The Arabidopsis AtRGGA protein is involved in post-transcriptional regulation of gene expression during salt stress

Autor: Punzo P., Nurcato R., Costa A., Aurilia V., Batelli G., Bailey-Serres J., Grillo S.

Publikováno v: Proceedings of the Joint Congress SIBV-SIGA, pp. 2.15, Milano, 8/11 September, 2015
info:cnr-pdr/source/autori:Punzo P., Nurcato R., Costa A., Aurilia V., Batelli G., Bailey-Serres J., Grillo S./congresso_nome:Proceedings of the Joint Congress SIBV-SIGA/congresso_luogo:Milano/congresso_data:8%2F11 September, 2015/anno:2015/pagina_da:2.15/pagina_a:/intervallo_pagine:2.15

Soil salinity reduces crop yields and limits available land for agriculture. Understanding the molecular mechanisms of plant salt stress response is becoming increasingly important. RNA regulatory mechanisms such as synthesis, transport, translation,

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=cnr_________::25d96b20632f9a0f534159f023971353
http://www.cnr.it/prodotto/i/347802

Enzymes and proteins from extremophiles as hyperstable probes in nanotechnology: the use of D-trehalose/D-maltose-binding protein from the hyperthermophilic archaeon Thermococcus litoralis for sugars monitoring

Autor: De Stefano L, Vitale A, Rea I, Staiano M, Rotiroti L, Labella T, Rendina I, Aurilia V, Rossi M, D’Auria S

Publikováno v: Extremophiles (Tokyo, Print) 12 (2008): 69–73.
info:cnr-pdr/source/autori:De Stefano L, Vitale A, Rea I, Staiano M, Rotiroti L, Labella T, Rendina I, Aurilia V, Rossi M, D’Auria S/titolo:Enzymes and proteins from extremophiles as hyperstable probes in nanotechnology: the use of D-trehalose%2FD-maltose-binding protein from the hyperthermophilic archaeon Thermococcus litoralis for sugars monitoring./doi:/rivista:Extremophiles (Tokyo, Print)/anno:2008/pagina_da:69/pagina_a:73/intervallo_pagine:69–73/volume:12

The D-trehalose/D-maltose-binding protein (TMBP), a monomeric protein of 48 kDa, is one component of the trehalose and maltose (Mal) uptake system. In the hyperthermophilic archaeon Thermococcus litoralis, this is mediated by a protein-dependent ATP-

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::26234e7494757c01ea50ba2a81e0e7d1
http://hdl.handle.net/11588/326480

A new archaeal beta-glycosidase from Sulfolobus solfataricus: Seeding a novel retaining beta-glycan-specific glycoside hydrolase family along with the human non-lysosomal glucosylceramidase GBA2

Autor: Cobucci-Ponzano B, Aurilia V, Gennaro Riccio, Henrissat B, Pm, Coutinho, Strazzulli A, Padula A, Mm, Corsaro, Pieretti G, Pocsfalvi G, Fiume I, Cannio R, Rossi M, Moracci M

Publikováno v: The Journal of biological chemistry
285 (2010): 20691–20703. doi:10.1074/jbc.M109.086470
info:cnr-pdr/source/autori:Cobucci-Ponzano B.; Aurilia V.; Riccio G.; Henrissat B.; Coutinho P.M.; Strazzulli A.; Padula A.; Corsaro M.M.; Pieretti G.; Pocsfalvi G.; Fiume I.; Cannio R.; Rossi M.; Moracci M./titolo:A new archaeal beta-glycosidase from Sulfolobus solfataricus: Seeding a novel retaining beta-glycan-specific glycoside hydrolase family along with the human non-lysosomal glucosylceramidase GBA2/doi:10.1074%2Fjbc.M109.086470/rivista:The Journal of biological chemistry (Print)/anno:2010/pagina_da:20691/pagina_a:20703/intervallo_pagine:20691–20703/volume:285
Europe PubMed Central

Carbohydrate active enzymes (CAZymes) are a large class of enzymes, which build and breakdown the complex carbohydrates of the cell. On the basis of their amino acid sequences they are classified in families and clans that show conserved catalytic me

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::06dc79b66440c5cad2ffe3ae5bb1ee5d
http://www.cnr.it/prodotto/i/9069

Cold-adapted enzymes: structure, stability and function investigated by computational methods

Autor: Marabotti, Anna, Facchiano, A, Aurilia, V, Rioux Dubé JF, Pézolet, M, D’Auria, S.

Publikováno v: BITS2009, Genova, 2009
info:cnr-pdr/source/autori:Marabotti A, Facchiano A, Aurilia V, Rioux-Dubé JF, Pézolet M, D’Auria S/congresso_nome:BITS2009/congresso_luogo:Genova/congresso_data:2009/anno:2009/pagina_da:/pagina_a:/intervallo_pagine

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::db36f7db9fa71233ca7d646d36e11eb2
http://www.cnr.it/prodotto/i/93016