Biocarburants < Biocatalyse < Biochimie

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List of bibliographic references indexed by Biocatalyse

Number of relevant bibliographic references: 20.

Ident.	Authors (with country if any)	Title
000560 (2020)	Pallinti Purushotham [États-Unis] ; Ruoya Ho [États-Unis] ; Jochen Zimmer [États-Unis]	Architecture of a catalytically active homotrimeric plant cellulose synthase complex.
000972 (2019)	Ruiqin Zhong [États-Unis] ; Dongtao Cui [États-Unis] ; Zheng-Hua Ye [États-Unis]	Evolutionary origin of O-acetyltransferases responsible for glucomannan acetylation in land plants.
000C61 (2018)	Xia Zhou [République populaire de Chine] ; Dayong Ding [République populaire de Chine] ; Tingting You [République populaire de Chine] ; Xun Zhang [République populaire de Chine] ; Keiji Takabe [Japon] ; Feng Xu [République populaire de Chine]	Synergetic Dissolution of Branched Xylan and Lignin Opens the Way for Enzymatic Hydrolysis of Poplar Cell Wall.
000F78 (2018)	Kaori Yoneyama [Japon] ; Narumi Mori [Japon] ; Tomoyasu Sato [Japon] ; Akiyoshi Yoda [Japon] ; Xiaonan Xie [Japon] ; Masanori Okamoto [Japon] ; Masashi Iwanaga [Japon] ; Toshiyuki Ohnishi [Japon] ; Hisashi Nishiwaki [Japon] ; Tadao Asami [Japon] ; Takao Yokota [Japon] ; Kohki Akiyama [Japon] ; Koichi Yoneyama [Japon] ; Takahito Nomura [Japon]	Conversion of carlactone to carlactonoic acid is a conserved function of MAX1 homologs in strigolactone biosynthesis.
001187 (2017)	Henri Pégeot [France] ; Sandrine Mathiot [France] ; Thomas Perrot [France] ; Frédéric Gense [France] ; Arnaud Hecker [France] ; Claude Didierjean [France] ; Nicolas Rouhier [France]	Structural plasticity among glutathione transferase Phi members: natural combination of catalytic residues confers dual biochemical activities.
001408 (2017)	Rahul Singh [Canada] ; Jinguang Hu [Canada] ; Matthew R. Regner [États-Unis] ; James W. Round [Canada] ; John Ralph [États-Unis] ; John N. Saddler [Canada] ; Lindsay D. Eltis [Canada]	Enhanced delignification of steam-pretreated poplar by a bacterial laccase.
001542 (2017)	Jianbo Xie [République populaire de Chine] ; Xiaohui Yang [République populaire de Chine] ; Yuepeng Song [République populaire de Chine] ; Qingzhang Du [République populaire de Chine] ; Ying Li [République populaire de Chine] ; Jinhui Chen [République populaire de Chine] ; Deqiang Zhang [République populaire de Chine]	Adaptive evolution and functional innovation of Populus-specific recently evolved microRNAs.
001A22 (2016)	Pallinti Purushotham [États-Unis] ; Sung Hyun Cho [États-Unis] ; Sara M. Díaz-Moreno [Suède] ; Manish Kumar [États-Unis] ; B Tracy Nixon [États-Unis] ; Vincent Bulone [Australie] ; Jochen Zimmer [États-Unis]	A single heterologously expressed plant cellulose synthase isoform is sufficient for cellulose microfibril formation in vitro.
001B46 (2015)	Hongcheng Sun [République populaire de Chine] ; Lu Miao [République populaire de Chine] ; Jiaxi Li [République populaire de Chine] ; Shuang Fu [République populaire de Chine] ; Guo An [République populaire de Chine] ; Chengye Si [République populaire de Chine] ; Zeyuan Dong [République populaire de Chine] ; Quan Luo [République populaire de Chine] ; Shuangjiang Yu [République populaire de Chine] ; Jiayun Xu [République populaire de Chine] ; Junqiu Liu [République populaire de Chine]	Self-assembly of cricoid proteins induced by "soft nanoparticles": an approach to design multienzyme-cooperative antioxidative systems.
001B61 (2015)	Vanessa Castro-Rodríguez [Espagne] ; Angel García-Gutiérrez [Espagne] ; Rafael A. Ca As [Espagne] ; Ma Belén Pascual [Espagne] ; Concepci N Avila [Espagne] ; Francisco M. Cánovas [Espagne]	Redundancy and metabolic function of the glutamine synthetase gene family in poplar.
001C02 (2015)	Jack P. Wang [États-Unis] ; Ling Chuang [États-Unis] ; Philip L. Loziuk [États-Unis] ; Hao Chen [États-Unis] ; Ying-Chung Lin [États-Unis] ; Rui Shi [États-Unis] ; Guan-Zheng Qu [République populaire de Chine] ; David C. Muddiman [États-Unis] ; Ronald R. Sederoff [États-Unis] ; Vincent L. Chiang [États-Unis]	Phosphorylation is an on/off switch for 5-hydroxyconiferaldehyde O-methyltransferase activity in poplar monolignol biosynthesis.
002231 (2014)	L T Mai Pham ; S Jin Kim ; U Suk Ahn ; J Weon Choi ; B Keun Song ; Y Hwan Kim	Extension of polyphenolics by CWPO-C peroxidase mutant containing radical-robust surface active site.
002585 (2013)	Nan Zhao [États-Unis] ; Jianzhuang Yao ; Minta Chaiprasongsuk ; Guanglin Li ; Ju Guan ; Timothy J. Tschaplinski ; Hong Guo ; Feng Chen	Molecular and biochemical characterization of the jasmonic acid methyltransferase gene from black cottonwood (Populus trichocarpa).
002644 (2013)	Sandra Irmisch [Allemagne] ; Sybille B. Unsicker [Allemagne] ; Jonathan Gershenzon [Allemagne] ; Tobias G. Köllner [Allemagne]	Identification and characterization of CYP79D6v4, a cytochrome P450 enzyme producing aldoximes in black poplar (Populus nigra).
002A38 (2012)	Jun Shigeto [Japon] ; Yoshitaka Itoh ; Yuji Tsutsumi ; Ryuichiro Kondo	Identification of Tyr74 and Tyr177 as substrate oxidation sites in cationic cell wall-bound peroxidase from Populus alba L.
002D92 (2011)	Zhen-Zhen Zhang [République populaire de Chine] ; Xiao-Xi Li ; Bao-Qing Zhu ; Ya-Qin Wen ; Chang-Qing Duan ; Qiu-Hong Pan	Molecular characterization and expression analysis on two isogenes encoding 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase in grapes.
002E14 (2011)	Claudia E. Vickers [Royaume-Uni] ; Malcolm Possell [Royaume-Uni] ; Jullada Laothawornkitkul [Royaume-Uni] ; Annette C. Ryan [Royaume-Uni] ; C Nicholas Hewitt [Royaume-Uni] ; Philip M. Mullineaux [Royaume-Uni]	Isoprene synthesis in plants: lessons from a transgenic tobacco model.
003125 (2010)	Navneet Phogat ; Vaibhav Vindal ; Vikash Kumar ; Krishna K. Inampudi ; Nirmal K. Prasad	Sequence analysis, in silico modeling and docking studies of caffeoyl CoA-O-methyltransferase of Populus trichopora.
003195 (2010)	Yun Lee [États-Unis] ; Eberhard O. Voit	Mathematical modeling of monolignol biosynthesis in Populus xylem.
003453 (2009)	Kaisa Marjamaa [Finlande] ; Eija M. Kukkola ; Kurt V. Fagerstedt	The role of xylem class III peroxidases in lignification.

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