标题
Mechanism of high-affinity abscisic acid binding to PYL9/RCAR1
作者
关键词
-
出版物
GENES TO CELLS
Volume 19, Issue 5, Pages 386-404
出版商
Wiley
发表日期
2014-03-20
DOI
10.1111/gtc.12140
参考文献
相关参考文献
注意:仅列出部分参考文献,下载原文获取全部文献信息。- Structural Insights into the Abscisic Acid Stereospecificity by the ABA Receptors PYR/PYL/RCAR
- (2013) Xingliang Zhang et al. PLoS One
- Complex Structures of the Abscisic Acid Receptor PYL3/RCAR13 Reveal a Unique Regulatory Mechanism
- (2012) Xingliang Zhang et al. STRUCTURE
- A thermodynamic switch modulates abscisic acid receptor sensitivity
- (2011) Florine Dupeux et al. EMBO JOURNAL
- The Molecular Basis of ABA-Independent Inhibition of PP2Cs by a Subclass of PYL Proteins
- (2011) Qi Hao et al. MOLECULAR CELL
- Structural insight into brassinosteroid perception by BRI1
- (2011) Ji She et al. NATURE
- Structural basis of steroid hormone perception by the receptor kinase BRI1
- (2011) Michael Hothorn et al. NATURE
- Structural basis for cytokinin recognition by Arabidopsis thaliana histidine kinase 4
- (2011) Michael Hothorn et al. Nature Chemical Biology
- Crystallization of the plant hormone receptors PYL9/RCAR1, PYL5/RCAR8 and PYR1/RCAR11 in the presence of (+)-abscisic acid
- (2010) Nobuyuki Shibata et al. Acta Crystallographica Section F-Structural Biology and Crystallization Communications
- Plant Nuclear Hormone Receptors: A Role for Small Molecules in Protein-Protein Interactions
- (2010) Shelley Lumba et al. Annual Review of Cell and Developmental Biology
- Single Amino Acid Alteration between Valine and Isoleucine Determines the Distinct Pyrabactin Selectivity by PYL1 and PYL2
- (2010) Xiaoqiu Yuan et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Jasmonate perception by inositol-phosphate-potentiated COI1–JAZ co-receptor
- (2010) Laura B. Sheard et al. NATURE
- Structural basis for selective activation of ABA receptors
- (2010) Francis C Peterson et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Identification and mechanism of ABA receptor antagonism
- (2010) Karsten Melcher et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Molecular replacement withMOLREP
- (2009) Alexei Vagin et al. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
- Structural basis of abscisic acid signalling
- (2009) Ken-ichi Miyazono et al. NATURE
- The abscisic acid receptor PYR1 in complex with abscisic acid
- (2009) Julia Santiago et al. NATURE
- A gate–latch–lock mechanism for hormone signalling by abscisic acid receptors
- (2009) Karsten Melcher et al. NATURE
- Recent advances and emerging trends in plant hormone signalling
- (2009) Aaron Santner et al. NATURE
- Structural insights into the mechanism of abscisic acid signaling by PYL proteins
- (2009) Ping Yin et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Modulation of drought resistance by the abscisic acid receptor PYL5 through inhibition of clade A PP2Cs
- (2009) Julia Santiago et al. PLANT JOURNAL
- Closely related receptor complexes differ in their ABA selectivity and sensitivity
- (2009) Izabela Szostkiewicz et al. PLANT JOURNAL
- Triple Loss of Function of Protein Phosphatases Type 2C Leads to Partial Constitutive Response to Endogenous Abscisic Acid
- (2009) S. Rubio et al. PLANT PHYSIOLOGY
- Stressed Out Over a Stress Hormone
- (2009) E. Pennisi SCIENCE
- Structural Mechanism of Abscisic Acid Binding and Signaling by Dimeric PYR1
- (2009) N. Nishimura et al. SCIENCE
- Jasmonate Passes Muster: A Receptor and Targets for the Defense Hormone
- (2008) John Browse Annual Review of Plant Biology
- The Bet v 1 fold: an ancient, versatile scaffold for binding of large, hydrophobic ligands
- (2008) Christian Radauer et al. BMC EVOLUTIONARY BIOLOGY
- The ABA receptors – we report you decide
- (2008) Peter McCourt et al. CURRENT OPINION IN PLANT BIOLOGY
- Gibberellin-induced DELLA recognition by the gibberellin receptor GID1
- (2008) Kohji Murase et al. NATURE
Add your recorded webinar
Do you already have a recorded webinar? Grow your audience and get more views by easily listing your recording on Peeref.
Upload NowAsk a Question. Answer a Question.
Quickly pose questions to the entire community. Debate answers and get clarity on the most important issues facing researchers.
Get Started