Serveur d'exploration sur la glutarédoxine - Exploration (Accueil)

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List of bibliographic references indexed by like

Number of relevant bibliographic references: 38.
[0-20] [0 - 20][0 - 38][20-37][20-40]
Ident.Authors (with country if any)Title
000015 (2020) Ryosuke Ota [Japon] ; Yuri Ohkubo [Japon] ; Yasuko Yamashita [Japon] ; Mari Ogawa-Ohnishi [Japon] ; Yoshikatsu Matsubayashi [Japon]Shoot-to-root mobile CEPD-like 2 integrates shoot nitrogen status to systemically regulate nitrate uptake in Arabidopsis.
000065 (2020) Carla Peres De Paula [Brésil] ; Melina Cardoso Dos Santos [Brésil] ; Carlos A. Tairum [Brésil] ; Carlos Alexandre Breyer [Brésil] ; Guilherme Toledo-Silva [Brésil] ; Marcos Hikari Toyama [Brésil] ; Gustavo Maruyama Mori [Brésil] ; Marcos Antonio De Oliveira [Brésil]Glutaredoxin-like protein (GLP)-a novel bacteria sulfurtransferase that protects cells against cyanide and oxidative stresses.
000082 (2020) Tao Su ; Chengchuan Che ; Ping Sun ; Xiaona Li ; Zhijin Gong ; Jinfeng Liu ; Ge YangCorynebacterium glutamicum Mycoredoxin 3 protects against multiple oxidative stresses and displays thioredoxin-like activity.
000121 (2019) Sérgio F. Sousa [Portugal] ; Rui P P. Neves [Portugal] ; Sodiq O. Waheed [Portugal] ; Pedro A. Fernandes [Portugal] ; Maria João Ramos [Portugal]Structural and mechanistic aspects of S-S bonds in the thioredoxin-like family of proteins.
000151 (2019) Chuanli Yang [République populaire de Chine] ; Peiyu Han [République populaire de Chine] ; Fengkai Ruan [République populaire de Chine] ; Tengjian Zhou [République populaire de Chine] ; Bing Luo [République populaire de Chine] ; Yang Qiu [République populaire de Chine] ; Yuchun Lin [République populaire de Chine] ; Zhongning Lin [République populaire de Chine] ; Chengyong He [République populaire de Chine]Lactational exposure to environmentally relevant benzo(a)pyrene causes astrocytic activation and anxiety-like behavior in male mice.
000415 (2016) Deepa Yenugudhati [États-Unis] ; Divya Prakash [États-Unis] ; Adepu K. Kumar [États-Unis] ; R Siva Sai Kumar [États-Unis] ; Neela H. Yennawar [États-Unis] ; Hemant P. Yennawar [États-Unis] ; James G. Ferry [États-Unis]Structural and Biochemical Characterizations of Methanoredoxin from Methanosarcina acetivorans, a Glutaredoxin-Like Enzyme with Coenzyme M-Dependent Protein Disulfide Reductase Activity.
000424 (2016) Li Yang ; Xiaoling Qian ; Mingjiao Chen ; Qili Fei ; Blake C. Meyers ; Wanqi Liang ; Dabing Zhang [République populaire de Chine]Regulatory Role of a Receptor-Like Kinase in Specifying Anther Cell Identity.
000535 (2015) Heba Al Khamici [Australie] ; Louise J. Brown [Australie] ; Khondker R. Hossain [Australie] ; Amanda L. Hudson [Australie] ; Alxcia A. Sinclair-Burton [Australie] ; Jane Phui Mun Ng [Australie] ; Elizabeth L. Daniel [Australie] ; Joanna E. Hare [Australie] ; Bruce A. Cornell [Australie] ; Paul M G. Curmi [Australie] ; Mary W. Davey [Australie] ; Stella M. Valenzuela [Australie]Members of the chloride intracellular ion channel protein family demonstrate glutaredoxin-like enzymatic activity.
000549 (2015) Kyle W. Bender [États-Unis] ; Xuejun Wang [États-Unis] ; George B. Cheng [États-Unis] ; Hyoung Seok Kim [États-Unis] ; Raymond E. Zielinski [États-Unis] ; Steven C. Huber [États-Unis]Glutaredoxin AtGRXC2 catalyses inhibitory glutathionylation of Arabidopsis BRI1-associated receptor-like kinase 1 (BAK1) in vitro.
000664 (2014) Lalida Rojanathammanee [États-Unis] ; Sharlene Rakoczy ; John Kopchick ; Holly M. Brown-BorgEffects of insulin-like growth factor 1 on glutathione S-transferases and thioredoxin in growth hormone receptor knockout mice.
000668 (2014) Ulrich Schweizer [Allemagne] ; Christine Schlicker [Allemagne] ; Doreen Braun [Allemagne] ; Josef Köhrle ; Clemens Steegborn [Allemagne]Crystal structure of mammalian selenocysteine-dependent iodothyronine deiodinase suggests a peroxiredoxin-like catalytic mechanism.
000707 (2013) Benoit Marteyn [France] ; Samer Sakr ; Sandrine Farci ; Mariette Bedhomme ; Solenne Chardonnet ; Paulette Decottignies ; Stéphane D. Lemaire ; Corinne Cassier-Chauvat ; Franck ChauvatThe Synechocystis PCC6803 MerA-like enzyme operates in the reduction of both mercury and uranium under the control of the glutaredoxin 1 enzyme.
000712 (2013) Robert J. Hondal [États-Unis] ; Stefano M. Marino ; Vadim N. GladyshevSelenocysteine in thiol/disulfide-like exchange reactions.
000790 (2013) Dolly K. Khona [Inde] ; Shounak S. Dongre ; Cecilia M. Arraiano ; Jacinta S. D'SouzaA BolA-like morphogene from the alga Chlamydomonas reinhardtii changes morphology and induces biofilm formation in Escherichia coli.
000841 (2012) Haoran Li [États-Unis] ; Caryn E. OuttenMonothiol CGFS glutaredoxins and BolA-like proteins: [2Fe-2S] binding partners in iron homeostasis.
000887 (2012) Kamel Chibani [France] ; Lionel Tarrago ; José Manuel Gualberto ; Gunnar Wingsle ; Pascal Rey ; Jean-Pierre Jacquot ; Nicolas RouhierAtypical thioredoxins in poplar: the glutathione-dependent thioredoxin-like 2.1 supports the activity of target enzymes possessing a single redox active cysteine.
000A40 (2010) Tobias H. Elgán [Suède] ; Anne-Gaëlle Planson ; Jon Beckwith ; Peter Güntert ; Kurt D. BerndtDeterminants of activity in glutaredoxins: an in vitro evolved Grx1-like variant of Escherichia coli Grx3.
000B02 (2009) Zai-Rong Zhang [République populaire de Chine] ; Sarah PerrettNovel glutaredoxin activity of the yeast prion protein Ure2 reveals a native-like dimer within fibrils.
000B65 (2008) Lydia M. Gibson [États-Unis] ; Nin N. Dingra ; Caryn E. Outten ; Lukasz LebiodaStructure of the thioredoxin-like domain of yeast glutaredoxin 3.
000B66 (2008) Timir Tripathi [Inde] ; Stefan Rahlfs ; Katja Becker ; Vinod BhakuniStructural and stability characteristics of a monothiol glutaredoxin: glutaredoxin-like protein 1 from Plasmodium falciparum.
000C48 (2007) Clara Camaschella [Italie] ; Alessandro Campanella ; Luigia De Falco ; Loredana Boschetto ; Roberta Merlini ; Laura Silvestri ; Sonia Levi ; Achille IolasconThe human counterpart of zebrafish shiraz shows sideroblastic-like microcytic anemia and iron overload.

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