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Showing 1–11 of 11 results

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Research | 14 September 2020 | Open
Overexpression of ATP sulfurylase improves the sulfur amino acid content, enhances the accumulation of Bowman–Birk protease inhibitor and suppresses the accumulation of the β-subunit of β-conglycinin in soybean seeds
Scientific Reports 10 , 1–13

Rights & permissionsfor article Overexpression of ATP sulfurylase improves the sulfur amino acid content, enhances the accumulation of Bowman–Birk protease inhibitor and suppresses the accumulation of the β-subunit of β-conglycinin in soybean seeds . Opens in a new window.
News and Views | 1 August 2000
A kaleidoscope of carotenoids
- Joseph M. Jez
- & Joseph P. Noel
Nature Biotechnology 18 , 825–826

Rights & permissionsfor article A kaleidoscope of carotenoids . Opens in a new window.
Correspondence | 10 September 2012
To be or not to be transgenic
Nature Biotechnology 30 , 825–826

Rights & permissionsfor article To be or not to be transgenic . Opens in a new window.
News and Views | 1 May 2009
The devil (and an active jasmonate hormone) is in the details
Nature Chemical Biology 5 , 273–274

Rights & permissionsfor article The devil (and an active jasmonate hormone) is in the details . Opens in a new window.
Research | 1 September 2000
Structure and mechanism of the evolutionarily unique plant enzyme chalcone isomerase
Nature Structural & Molecular Biology 7 , 786–791

Rights & permissionsfor article Structure and mechanism of the evolutionarily unique plant enzyme chalcone isomerase . Opens in a new window.
Research | 4 October 2018 | Open
A multisubstrate reductase from Plantago major: structure-function in the short chain reductase superfamily
- Rachel Fellows
- , Christopher M. Russo
- , Catarina S. Silva
- , Soon Goo Lee
- , Joseph M. Jez
- , John D. Chisholm
- , Chloe Zubieta
- & Max H. Nanao
Scientific Reports 8 , 1–13

Rights & permissionsfor article A multisubstrate reductase from <i>Plantago major</i>: structure-function in the short chain reductase superfamily . Opens in a new window.
Research | 5 February 2018 | Open
Impact of overexpression of cytosolic isoform of O-acetylserine sulfhydrylase on soybean nodulation and nodule metabolome
Scientific Reports 8 , 1–14

Rights & permissionsfor article Impact of overexpression of cytosolic isoform of <i>O</i>-acetylserine sulfhydrylase on soybean nodulation and nodule metabolome . Opens in a new window.
Research | 26 June 2017
Molecular basis of the evolution of alternative tyrosine biosynthetic routes in plants
- Craig A Schenck
- , Cynthia K Holland
- , Matthew R Schneider
- , Yusen Men
- , Soon Goo Lee
- , Joseph M Jez
- & Hiroshi A Maeda
Nature Chemical Biology 13 , 1029–1035

Rights & permissionsfor article Molecular basis of the evolution of alternative tyrosine biosynthetic routes in plants . Opens in a new window.
Research | 24 October 2017 | Open
Functional classification of protein toxins as a basis for bioinformatic screening
- Surendra S. Negi
- , Catherine H. Schein
- , Gregory S. Ladics
- , Henry Mirsky
- , Peter Chang
- , Jean-Baptiste Rascle
- , John Kough
- , Lieven Sterck
- , Sabitha Papineni
- , Joseph M. Jez
- , Lucilia Pereira Mouriès
- & Werner Braun
Scientific Reports 7 , 1–11

Rights & permissionsfor article Functional classification of protein toxins as a basis for bioinformatic screening . Opens in a new window.
Research | 17 August 2014
A chemical inhibitor of jasmonate signaling targets JAR1 in Arabidopsis thaliana
- Christian Meesters
- , Timon Mönig
- , Julian Oeljeklaus
- , Daniel Krahn
- , Corey S Westfall
- , Bettina Hause
- , Joseph M Jez
- , Markus Kaiser
- & Erich Kombrink
Nature Chemical Biology 10 , 830–836

Rights & permissionsfor article A chemical inhibitor of jasmonate signaling targets JAR1 in <i>Arabidopsis thaliana</i> . Opens in a new window.
Research | 1 August 1999
Structure of chalcone synthase and the molecular basis of plant polyketide biosynthesis
Nature Structural & Molecular Biology 6 , 775–784

Rights & permissionsfor article Structure of chalcone synthase and the molecular basis of plant polyketide biosynthesis . Opens in a new window.

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