Jing-Fang Yang

Dr. Jing-Fang Yang


Research Focus & Metrics

Academic Career Length

4Years (2023-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

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3 May 2024 in Analytica Chimica Acta
Verified
Journal Article
Closed access
Qi SunQi Sun
Qi Sun
TZTing Zhang
Ting Zhang
YRYuchen Ren
Yuchen Ren
YQYuan Qiu
Yuan Qiu
XLXiaogang Luo
Xiaogang Luo
GLGenyan Liu
Genyan Liu

7 June 2025 in Pesticide Biochemistry and Physiology
Verified
Journal Article
Closed access
KZKun Zhang
Kun Zhang
JCJianwen Chen
Jianwen Chen
HHHuixiu Huang
Huixiu Huang
HWHuiqi Wen
Huiqi Wen
JYJing-Fang Yang
Jing-Fang Yang
SWShaoying Wu
Shaoying Wu

Verified
Journal Article
Open access
PDF file
JYJing-Fang Yang
Jing-Fang Yang
LSLe-Rong Shi
Le-Rong Shi
KWKe-Chen Wang
Ke-Chen Wang
LHLi-Long Huang
Li-Long Huang
YDYun-Shuang Deng
Yun-Shuang Deng
Zhongshi ZhouZhongshi Zhou
Zhongshi Zhou
Zn2+-dependent histone deacetylases (HDACs) are enzymes that regulate gene expression by removing acetyl groups from histone proteins. These enzymes are essential in all living systems, playing key roles in cancer treatment and as potential pesticide targets. Previous phylogenetic analyses of HDAC in certain species have been published. However, their classification and evolutionary origins across biological kingdoms remain unclear, which limits our understanding of them. In this study, we collected the HDAC sequences from 1451 organisms and performed analyses. The HDACs are found to diverge into three classes and seven subclasses under divergent selection pressure. Most subclasses show species specificity, indicating that HDACs have evolved with high plasticity and diversification to adapt to different environmental conditions in different species. In contrast, HDAC1 and HDAC3, belonging to the oldest class, are conserved and crucial in major kingdoms of life, especially HDAC1. These findings lay the groundwork for the future application of HDACs.

24 March 2025 in Pesticide Biochemistry and Physiology
Verified
Journal Article
Open access
YYYang Yue
Yang Yue
CMChao Ma
Chao Ma
YZYan Zhang
Yan Zhang
WMWeihua Ma
Weihua Ma
JWJing-Jing Wang
Jing-Jing Wang
Zhongshi ZhouZhongshi Zhou
Zhongshi Zhou
Odorant binding proteins (OBPs) play a critical role in insect survival by facilitating the detection of environmental odors. This study identified and characterized OcomOBP11 in the leaf beetle Ophraella communa Lesage. Sequence and phylogenetic analyses demonstrated that OcomOBP11 belongs to the Minus-C OBP family. Tissue-specific expression analysis revealed that OcomOBP11 showed the highest relative expression in the testis. Functional assays demonstrated that OcomOBP11 has strong binding affinity to 24 of the 26 volatiles from Ambrosia artemisiifolia L., a primary host plant. Molecular docking showed that OcomOBP11 formed hydrophobic interactions with β-caryophyllene, α-pinene, camphene, octanal, and nonanal and hydrogen bonds with octanal and nonanal. RNAi-mediated knockdown of OcomOBP11 significantly reduced the electrophysiological (EAG) response and behavioral preference of O. communa for these ligands. These findings suggest that OcomOBP11 plays an important role in host plant localization, thus providing guidance for future biological invasion control strategies.

10 May 2026 in Insects
Verified
Journal Article
Open access
PDF file
XWXihao Wang
Xihao Wang
MHMengying He
Mengying He
LYLu Yang
Lu Yang
YZYan Zhang
Yan Zhang
JYJing-Fang Yang
Jing-Fang Yang
Zhongshi ZhouZhongshi Zhou
Zhongshi Zhou
External environment shapes the cold adaptation of Ophraella communa, a specialist natural enemy of the invasive common ragweed, and further affects its biological control efficacy. Our study aims to clarify the cold tolerance correlation between ragweed and leaf beetle and explore whether host cold acclimation can enhance the beetle’s low-temperature adaptability. We measured cold-resistant substances, supercooling point (SCP), and chill-coma recovery time (CCRT) of four geographic populations, and conducted indoor low-temperature acclimation of ragweed at 13 °C, 17 °C, 21 °C for 3–9 d, then fed leaf beetle with treated leaves. Results showed that cold-resistant substances in both species varied with latitude and were highly heritable. Cold acclimation can elevate sugars, trehalose, glycerol, and proline in ragweed; the cold tolerance of beetles feeding on these plants was significantly improved. We conclude that cold-resistant substances in ragweed can be trophically transferred to leaf beetle to enhance its cold hardiness, providing a new strategy to improve biocontrol in high-latitude regions.

12 September 2025 in Pesticide Biochemistry and Physiology
Verified
Journal Article
Open access
QWQing-Guo Wu
Qing-Guo Wu
RLRen-Long Liang
Ren-Long Liang
JYJing-Fang Yang
Jing-Fang Yang
4-Hydroxyphenylpyruvate dioxygenase (HPPD, EC 1.13.11.27) is a key target for herbicide development, especially in the management of herbicide-resistant weeds. However, many existing HPPD inhibitors suffer from poor crop selectivity, limiting their widespread application. To address this problem, a series of novel 2,4-dichlorobenzene-3-morpholine derivatives were designed and synthesized. Greenhouse activity tests demonstrated that a large class of molecules obviously inhibited dwarfing in the tested weeds. Notably, compound B2 exhibited superior herbicidal activity against broadleaf weeds, such as Abutilon theophrasti, Zinnia elegans, and Portulaca oleracea, at 9.375 g ai/ha, which is superior to that of the widely used herbicide mesotrione. Moreover, compared with mesotrione, compound B2 showed no obvious injury on the growth of peanuts at 150 g ai/ha and was safer for peanuts, even at the higher dosage of 600 g ai/ha. These results suggest that B2 is a promising new candidate herbicide for use in peanut fields. Molecular simulations of the representative molecule further revealed a binding mode that fit into the active site of HPPD, similar to most known HPPD inhibitors. Met338 in P. oleracea HPPD plays a crucial role in the binding of compound B2, whereas Ile453 and Ile455 in peanut HPPD may contribute to reduced inhibition in peanuts. Additionally, the entry pathways of compounds, along with their polarity and lipophilicity, could increase their selectivity for different plant species. This study provides valuable insights for the future development of highly selective HPPD inhibitors.