- Home
- Publications
- Publication Search
- Publication Details
Title
Plant proteases and programmed cell death
Authors
Keywords
-
Journal
JOURNAL OF EXPERIMENTAL BOTANY
Volume 70, Issue 7, Pages 1991-1995
Publisher
Oxford University Press (OUP)
Online
2019-03-16
DOI
10.1093/jxb/erz126
References
Ask authors/readers for more resources
Related references
Note: Only part of the references are listed.- Do proteolytic cascades exist in plants?
- (2019) Judith K Paulus et al. JOURNAL OF EXPERIMENTAL BOTANY
- Discovery of AAA+ Protease Substrates through Trapping Approaches
- (2019) Jui-Yun Rei Liao et al. TRENDS IN BIOCHEMICAL SCIENCES
- The macrocyclizing protease butelase 1 remains autocatalytic and reveals the structural basis for ligase activity
- (2019) Amy M. James et al. PLANT JOURNAL
- The Scope, Functions, and Dynamics of Posttranslational Protein Modifications
- (2019) A. Harvey Millar et al. Annual Review of Plant Biology
- Structural analyses ofArabidopsis thalianalegumain γ reveal differential recognition and processing of proteolysis and ligation substrates
- (2018) Florian B. Zauner et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Increases in activity of proteasome and papain-like cysteine protease in Arabidopsis autophagy mutants: back-up compensatory effect or cell-death promoting effect?
- (2018) Marien Havé et al. JOURNAL OF EXPERIMENTAL BOTANY
- Unravelling the mode of action of plant proteases
- (2018) Renier A. L. van der Hoorn et al. NEW PHYTOLOGIST
- Trapping biosynthetic acyl-enzyme intermediates with encoded 2,3-diaminopropionic acid
- (2018) Nicolas Huguenin-Dezot et al. NATURE
- Iron- and Reactive Oxygen Species-Dependent Ferroptotic Cell Death in Rice-Magnaporthe oryzae Interactions
- (2018) Sarmina Dangol et al. PLANT CELL
- N-terminal Proteomics Assisted Profiling of the Unexplored Translation Initiation Landscape in Arabidopsis thaliana
- (2017) Patrick Willems et al. MOLECULAR & CELLULAR PROTEOMICS
- Quantitative proteomics in plant protease substrate identification
- (2017) Fatih Demir et al. NEW PHYTOLOGIST
- Life and death of proteins after protease cleavage: protein degradation by the N-end rule pathway
- (2017) Nico Dissmeyer et al. NEW PHYTOLOGIST
- Limited and digestive proteolysis: crosstalk between evolutionary conserved pathways
- (2017) Elena A. Minina et al. NEW PHYTOLOGIST
- From structure to function - a family portrait of plant subtilases
- (2017) Andreas Schaller et al. NEW PHYTOLOGIST
- The MEROPS database of proteolytic enzymes, their substrates and inhibitors in 2017 and a comparison with peptidases in the PANTHER database
- (2017) Neil D Rawlings et al. NUCLEIC ACIDS RESEARCH
- Juggling jobs: roles and mechanisms of multifunctional protease inhibitors in plants
- (2016) Friederike M. Grosse-Holz et al. NEW PHYTOLOGIST
- The Increasing Impact of Activity-Based Protein Profiling in Plant Science
- (2016) Kyoko Morimoto et al. PLANT AND CELL PHYSIOLOGY
- Loss of function atRAE2, a previously unidentified EPFL, is required for awnlessness in cultivated Asian rice
- (2016) Kanako Bessho-Uehara et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Precursor processing for plant peptide hormone maturation by subtilisin-like serine proteinases
- (2016) Katharina Schardon et al. SCIENCE
- Extracellular peptidase hunting for improvement of protein production in plant cells and roots
- (2015) Jérôme Lallemand et al. Frontiers in Plant Science
- GRIM REAPER peptide binds to receptor kinase PRK5 to trigger cell death in Arabidopsis
- (2014) M. Wrzaczek et al. EMBO JOURNAL
- Set-point control of RD21 protease activity by AtSerpin1 controls cell death in Arabidopsis
- (2013) Nardy Lampl et al. PLANT JOURNAL
- Phytaspase, a relocalisable cell death promoting plant protease with caspase specificity
- (2010) Nina V Chichkova et al. EMBO JOURNAL
Discover Peeref hubs
Discuss science. Find collaborators. Network.
Join a conversationPublish scientific posters with Peeref
Peeref publishes scientific posters from all research disciplines. Our Diamond Open Access policy means free access to content and no publication fees for authors.
Learn More