H
Heqiao Zhang
Researcher at Tsinghua University
Publications - 21
Citations - 1333
Heqiao Zhang is an academic researcher from Tsinghua University. The author has contributed to research in topics: Biology & Gene. The author has an hindex of 13, co-authored 17 publications receiving 1004 citations. Previous affiliations of Heqiao Zhang include ShanghaiTech University & Chinese Academy of Sciences.
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Journal ArticleDOI
An RLP23–SOBIR1–BAK1 complex mediates NLP-triggered immunity
Isabell Albert,Hannah Böhm,Markus Albert,Christina E. Feiler,Julia Imkampe,Niklas Wallmeroth,Caterina Brancato,Tom M. Raaymakers,Stan Oome,Heqiao Zhang,Elzbieta Krol,Christopher Grefen,Andrea A. Gust,Jijie Chai,Rainer Hedrich,Guido Van den Ackerveken,Thorsten Nürnberger +16 more
TL;DR: It is shown that the leucine-rich repeat receptor protein (LRR-RP) RLP23 binds in vivo to a conserved 20-amino-acid fragment found in most NLPs, thereby mediating immune activation in Arabidopsis thaliana and inducing immunity to destructive oomycete and fungal plant pathogens.
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Allosteric receptor activation by the plant peptide hormone phytosulfokine
Jizong Wang,Hongjun Li,Zhifu Han,Heqiao Zhang,Tong Wang,Guangzhong Lin,Junbiao Chang,Wei-Cai Yang,Jijie Chai +8 more
TL;DR: The crystal structures of the extracellular LRR domain of PSKR in free, PSK- and co-receptor-bound forms are reported, revealing the structural basis for PSKR recognition of PSK and allosteric activation ofPSKR by PSK, opening up new avenues for the design of PS KR-specific small molecules.
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Signature motif-guided identification of receptors for peptide hormones essential for root meristem growth.
Wen Song,Li Liu,Jizong Wang,Zhen Wu,Heqiao Zhang,Jiao Tang,Guangzhong Lin,Yichuan Wang,Yichuan Wang,Xing Wen,Wenyang Li,Zhifu Han,Hongwei Guo,Hongwei Guo,Jijie Chai +14 more
TL;DR: This study identifies RGF receptors and co-receptors that can link RGF signals with their downstream components and provides a proof of principle for structure-based matching of LRR-RKs with their peptide ligands.
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Structural basis for recognition of an endogenous peptide by the plant receptor kinase PEPR1
TL;DR: A crystal structure of the extracellular LRR domain of PEPR1 (PEPR1LRR) in complex with AtPep1 is reported, providing significant insight into prediction of recognition of other peptides by their cognate LRR-RKs.
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Crystal structure of PXY-TDIF complex reveals a conserved recognition mechanism among CLE peptide-receptor pairs
TL;DR: The crystal structure of TDIF in complex with its receptor PXY, a leucine-rich repeat receptor kinase (LRR-RK), reveals that TDIF mainly adopts an “Ω”-like conformation binding to the inner surface of the LRR domain of PXY.