UAB Digital Repository of Documents 7 records found  Search took 0.01 seconds. 
1.
20 p, 10.5 MB Binding site profiles and N-terminal minor groove interactions of the master quorum-sensing regulator LuxR enable flexible control of gene activation and repression / Zhang, Jun (East China University of Science and Technology. State Key Laboratory of Bioreactor Engineering (China)) ; Liu, Bing (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Gu, Dan (Yangzhou University. Jiangsu Co-Innovation Center for Prevention and Control of Important Animal Infectious Diseases and Zoonoses (China)) ; Hao, Yuan (East China University of Science and Technology. State Key Laboratory of Bioreactor Engineering (China)) ; Chen, Mo (East China University of Science and Technology. State Key Laboratory of Bioreactor Engineering (China)) ; Ma, Yue (East China University of Science and Technology. State Key Laboratory of Bioreactor Engineering (China)) ; Zhou, Xiaohui (University of Connecticut. Department of Pathobiology and Veterinary Science (USA)) ; Reverter i Cendrós, David (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Zhang, Yuanxing (Southern Marine Science and Engineering Guangdong Laboratory (China)) ; Wang, Qiyao (East China University of Science and Technology. State Key Laboratory of Bioreactor Engineering (China)) ; Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular
LuxR is a TetR family master quorum sensing (QS) regulator activating or repressing expression of hundreds of genes that control collective behaviors in Vibrios with underlying mechanism unknown. To illuminate how this regulator controls expression of various target genes, we applied ChIP-seq and DNase I-seq technologies. [...]
2021 - 10.1093/nar/gkab150
Nucleic acids research, Vol. 49, Issue 6 (April 2021) , p. 3274-3293  
2.
28 p, 7.6 MB Critical role for a promoter discriminator in RpoS control of virulence in Edwardsiella piscicida / Yin, Kaiyu (East China University of Science and Technology. State Key Laboratory of Bioreactor Engineering) ; Guan, Yunpeng (East China University of Science and Technology. State Key Laboratory of Bioreactor Engineering) ; Ma, Ruiqing (East China University of Science and Technology. State Key Laboratory of Bioreactor Engineering) ; Wei, Lifan (East China University of Science and Technology. State Key Laboratory of Bioreactor Engineering) ; Liu, Bing (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Liu, Xiaohong (East China University of Science and Technology. State Key Laboratory of Bioreactor Engineering) ; Zhou, Xiangshan (East China University of Science and Technology. State Key Laboratory of Bioreactor Engineering) ; Ma, Yue (East China University of Science and Technology. State Key Laboratory of Bioreactor Engineering) ; Zhang, Yuanxing (East China University of Science and Technology. State Key Laboratory of Bioreactor Engineering) ; Waldor, M. K. (Harvard Medical School) ; Wang, Qiyao (East China University of Science and Technology. State Key Laboratory of Bioreactor Engineering) ; Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular
Edwardsiella piscicida is a leading fish pathogen that causes significant economic loses in the aquaculture industry. The pathogen depends on type III and type VI secretion systems (T3/T6SS) for growth and virulence in fish and the expression of both systems is controlled by the EsrB transcription activator. [...]
2018 - 10.1371/journal.ppat.1007272
PLOS pathogens, Vol. 14 issue 8 (2018) , art. e1007272  
3.
13 p, 2.3 MB A quaternary tetramer assembly inhibits the deubiquitinating activity of USP25 / Liu, Bing (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Sureda-Gómez, Marta (Institut d'Investigacions Biomèdiques August Pi i Sunyer) ; Zhen, Yang (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Amador, Virginia (Institut d'Investigacions Biomèdiques August Pi i Sunyer) ; Reverter i Cendrós, David (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
USP25 deubiquitinating enzyme is a key member of the ubiquitin system, which acts as a positive regulator of the Wnt/β-catenin signaling by promoting the deubiquitination and stabilization of tankyrases. [...]
2018 - 10.1038/s41467-018-07510-5
Nature communications, Vol. 9 (2018) , art. 4973  
4.
10 p, 6.7 MB Structural analysis and evolution of specificity of the SUMO UFD E1-E2 interactions / Liu, Bing (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Lois, L. Maria (Centre de Recerca en Agrigenòmica) ; Reverter i Cendrós, David (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular
SUMO belongs to the ubiquitin-like family (UbL) of protein modifiers. SUMO is conserved among eukaryotes and is essential for the regulation of processes such as DNA damage repair, transcription, DNA replication and mitosis. [...]
2017 - 10.1038/srep41998
Scientific reports, Vol. 7 (February 2017) , art. 41998  
5.
30 p, 3.1 MB Structural insights into SUMO E1-E2 interactions in Arabidopsis uncovers a distinctive platform for securing SUMO conjugation specificity across evolution / Liu, Bing (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Lois, L. Maria (Centre de Recerca en Agrigenòmica) ; Reverter i Cendrós, David (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
SUMOylation of proteins involves the concerted action of the E1-activating enzyme, E2-conjugating enzyme and E3-ligases. An essential discrimination step in the SUMOylation pathway corresponds to the initial interaction between E1 ubiquitin-fold domain (UFD) and E2 enzymes. [...]
2019 - 10.1042/BCJ20190232
Biochemical Journal, Vol. 476, Issue 14 (July 2019) , p. 2127-2139  
6.
213 p, 14.7 MB Structure insights into the autoinhibitory mechanism of the deubiquitinating enzyme USP25 and into the SUMO E1-E2 protein-protein recognition / Liu, Bing ; Reverter Cendrós, David, dir. ; Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular
La ubiquitinació i la SUMOilació són dos de les modificacions post-traduccionals més estudiades (PTM). En aquesta tesi, ens hem centrat en estudiar USP25, USP28 i en el reconeixement proteïna-proteïna dels enzims SUMO E1-E2 d'aquestes dues vies PTM. [...]
Ubiquitination and SUMOylation are of the most studied post-translational modifications (PTMs). Here, we focus on USP25, USP28, and the SUMO E1-E2 protein-protein recognition in these two PTM pathways. [...]

[Barcelona] : Universitat Autònoma de Barcelona, 2019.  
7.
28 p, 1.0 MB Temperature increase reduces global yields of major crops in four independent estimates / Zhao, Chuang (Sino-French Institute for Earth System Science) ; Liu, Bing (Nanjing nong ye da xue. National Engineering and Technology Center for Information Agriculture) ; Piao, Shilong (Zhongguo ke xue yuan. Institute of Tibetan Plateau Research) ; Wang, Xuhui (Sino-French Institute for Earth System Science) ; Lobelli, David B. (Stanford University. Department of Earth System Science Center on Food Security and the Environment) ; Huang, Yao (Zhongguo ke xue yuan. State Key Laboratory of Vegetation and Environmental Change) ; Huanga, Mengtian (Sino-French Institute for Earth System Science) ; Yao, Yitong (Sino-French Institute for Earth System Science) ; Bassuk, Simona (Università degli Studi di Sassari. Nucleo Ricerca Desertificazione) ; Ciais, Philippe (Laboratoire des Sciences du Climat et de l'Environnement) ; Durand, Jean-Louis (Institut National de la Recherche Agronomique (França)) ; Elliott, Joshua (University of Chicago Computation Institute) ; Ewert, Frank (Universität Bonn. Institut für Nutzpflanzenwissenschaften und Ressourcenschutz) ; Janssens, Ivan (University of Antwerp (Bèlgica)) ; Li, Tao (International Rice Research Institute) ; Lint, Erda (Zhongguo nong ye ke xue yuan. Agro-Environment and Sustainable Development Institute) ; Liu, Qiang (Sino-French Institute for Earth System Science) ; Martre, Pierre (Institut national de la recherche agronomique (France). Laboratoire d'Écophysiologie des Plantes sous Stress Environnementaux) ; Müller, Christoph (Potsdam-Institut für Klimafolgenforschung) ; Peng, Shushi (Sino-French Institute for Earth System Science) ; Peñuelas, Josep (Centre de Recerca Ecològica i d'Aplicacions Forestals) ; Ruaney, Alex C. (Columbia University. Center for Climate Systems Research) ; Wallachz, Daniel (Institut national de la recherche agronomique (France). UMR AGIR) ; Wang, Tao (Zhongguo ke xue yuan. Institute of Tibetan Plateau Research) ; Wua, Donghai (Sino-French Institute for Earth System Science) ; Liu, Zhuo (Sino-French Institute for Earth System Science) ; Zhu, Yan (Nanjing nong ye da xue. National Engineering and Technology Center for Information Agriculture) ; Zhua, Zaichun (Sino-French Institute for Earth System Science) ; Assengf, Senthold (University of Florida. Agricultural and Biological Engineering Department)
Wheat, rice, maize, and soybean provide two-thirds of human caloric intake. Assessing the impact of global temperature increase on production of these crops is therefore critical to maintaining global food supply, but different studies have yielded different results. [...]
2017 - 10.1073/pnas.1701762114
Proceedings of the National Academy of Sciences of the United States of America, Vol. 114, no. 35 (Aug. 2017) , p. 9326-9331  

Interested in being notified about new results for this query?
Set up a personal email alert or subscribe to the RSS feed.