Hongyu Zhang

Dr. Hongyu Zhang


Research Focus & Metrics

Academic Career Length

27Years (2000-Present)

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

Representative Publications

View All Publications
6 November 2017 in Oncotarget
Verified
Journal Article
Open access
PDF file
HRHaihua Ruan
Haihua Ruan
SHShuangyan Hu
Shuangyan Hu
HZHongyu Zhang
Hongyu Zhang
GDGang Du
Gang Du
XLXiaoting Li
Xiaoting Li
XLXichuan Li
Xichuan Li
// <![CDATA[ $('.header-date').hide();$('#titleAuthors').hide();$('#abstractHeader').hide(); // ]]> Haihua Ruan1, Shuangyan Hu1, Hongyu Zhang1, Gang Du1, Xiaoting Li2, Xiaobo Li2 and Xichuan Li2 1Tianjin Key Laboratory of Food Science and Biotechnology, College of Biotechnology and Food Science, Tianjin University of Commerce, Tianjin, China 2Department of Immunology, Tianjin Medical University, Tianjin, China Correspondence to: Xichuan Li, email: xichuanli@tmu.edu.cn Hongyu Zhang, email: zhanghongyu@tjcu.edu.cn Keywords: solid tumors, SOX9, prognosis, meta-analysis Received: August 23, 2017 Accepted: October 05, 2017 Published: November 06, 2017 ABSTRACT It was recently reported that increased SOX9 expression drives tumor growth and promotes cancer invasion during human tumorigenicity and metastasis. However, the prognostic value of SOX9 for the survival of patients with solid tumors remains controversial. The present meta-analysis was thus performed to highlight the link between dysregulated SOX9 expression and prognosis in cancer patients. A systematic literature search was conducted using the electronic databases PubMed, Web of Science and Embase to identify eligible studies. A random-effects meta-analytical model was employed to correlate SOX9 expression with overall survival (OS), disease-free survival (DFS) and clinicopathological features. In total, 17 studies with 3307 patients were eligible for the final analysis. Combined hazard ratios (HRs) and 95% confidence intervals (CIs) suggested that high SOX9 expression has an unfavourable impact on OS (HR = 1.66, 95% CI 1.36–2.02, P < 0.001) and DFS (HR = 3.54, 95% CI 2.29–5.47, P = 0.008) in multivariate analysis. Additionally, the pooled odds ratios (ORs) indicated that SOX9 over-expression is associated with large tumor size, lymph node metastasis, distant metastasis and a higher clinical stage. Overall, these results indicated that SOX9 over-expression in patients with solid tumors might be related to poor prognosis and could serve as a potential predictive marker of poor clinicopathological prognosis factor.

28 August 2024 in Molecules
Verified
Journal Article
Open access
PDF file
HZHongyu Zhang
Hongyu Zhang
LZLeting Zhu
Leting Zhu
ZZZixuan Zhou
Zixuan Zhou
DWDanyun Wang
Danyun Wang
JYJinShan Yang
JinShan Yang
TLTingting Lou
Tingting Lou
Sucrose phosphorylase (SPase), a member of the glycoside hydrolase GH13 family, possesses the ability to catalyze the hydrolysis of sucrose to generate α-glucose-1-phosphate and can also glycosylate diverse substrates, showcasing a wide substrate specificity. This enzyme has found extensive utility in the fields of food, medicine, and cosmetics, and has garnered significant attention as a focal point of research in transglycosylation enzymes. Nevertheless, SPase encounters numerous obstacles in industrial settings, including low enzyme yield, inadequate thermal stability, mixed regioselectivity, and limited transglycosylation activity. In-depth exploration of efficient expression strategies and molecular modifications based on the crystal structure and functional information of SPase is now a critical research priority. This paper systematically reviews the source microorganisms, crystal structure, and catalytic mechanism of SPase, summarizes diverse heterologous expression systems based on expression hosts and vectors, and examines the application and molecular modification progress of SPase in synthesizing typical glycosylated products. Additionally, it anticipates the broad application prospects of SPase in industrial production and related research fields, laying the groundwork for its engineering modification and industrial application.

9 September 2011 in Marine Drugs
Verified
Journal Article
Open access
PDF file
HZHongyu Zhang
Hongyu Zhang
HWHong-peng Wang
Hong-peng Wang
HCHongli Cui
Hongli Cui
HZHongyu Zhang
Hongyu Zhang
ZXZeping Xie
Zeping Xie
SQSong Qin
Song Qin
A new anthracene derivative, 3-hydroxy-1-keto-3-methyl-8-methoxy-1,2,3,4-tetrahydro-benz[α]anthracene, was isolated from the marine strain Streptomyces sp. W007, and its structure was established by spectroscopic analysis including mass spectra, 1D- and 2D-NMR (1H–1H COSY, HMBC, HSQC and NOESY) experiments. 3-hydroxy-1-keto-3-methyl-8-methoxy-1,2,3,4-tetrahydro-benz[α]anthracene showed cytotoxicity against human lung adenocarcinoma cell line A549.

27 December 2018 in Journal of Basic Microbiology
Verified
Journal Article
Closed access
PDF file
HZHongyu Zhang
Hongyu Zhang
SDShirui Dong
Shirui Dong
TLTingting Lou
Tingting Lou
SWSu-Ying Wang
Su-Ying Wang

9 November 2024 in Crystals
Verified
Journal Article
Open access
PDF file
SMShuru Ma
Shuru Ma
HZHongyu Zhang
Hongyu Zhang
TLTingting Lou
Tingting Lou
SWSu-Ying Wang
Su-Ying Wang
Sucrose phosphorylase (SPase) is a member of the glycoside hydrolase family 13, catalyzing the reversible phosphorolysis of sucrose to produce α–glucose–1–phosphate and exhibiting transglycosylation activity toward multiple substrates. Its wide substrate specificity enables the synthesis of various glycosides, which are broadly applied in food, cosmetics, and pharmaceuticals. However, the industrial application of SPase is constrained by its poor thermostability and limited transglycosylation activity. Therefore, current research focuses on enhancing the thermostability and transglycosylation activity of SPase through efficient engineering strategies based on its crystal structure and catalytic mechanism. This paper systematically reviews the crystal structure and catalytic mechanism of SPase, outlines the application of protein engineering and immobilization strategies in improving the thermostability of SPase, and analyzes how modifications at key amino acid sites affect the synthesis of typical glycosylation products. It also summarizes the limitations of SPase engineering modification strategies and explores the potential of diversified approaches for SPase modification, highlighting its broad application prospects in industrial production and laying a solid foundation for further advancements in SPase engineering modification and its industrial application.

14 September 2022 in Fermentation
Verified
Journal Article
Open access
PDF file
HZHongyu Zhang
Hongyu Zhang
RLRan Liu
Ran Liu
TLTingting Lou
Tingting Lou
PZPei Zhao
Pei Zhao
SWSu-Ying Wang
Su-Ying Wang
Pentostatin (PNT), a nucleoside antibiotic with a 1,3-diazo ring structure, is distributed in several actinomycetes and fungi species. Its special structure makes PNT possess a wide spectrum of biological and pharmacological properties, such as antibacterial, antitrypanosomal, anticancer, antiviral, herbicidal, insecticidal, and immunomodulatory effects. Because of the promising adenosine deaminase inhibitory activity of PNT, its extensive application in the clinical treatment of malignant tumors has been extensively studied. However, the fermentation level of microbial-derived PNT is low and cannot meet medical needs. Because the biosynthesis pathway of PNT is obscure, only high-yield mutant screening and optimization of medium components and fermentation processes have been conducted for enhancing its production. Recently, the biosynthesis pathways of PNT in actinomycetes and fungi hosts have been revealed successively, and the large-scale production of PNT by systematic metabolic engineering will become an inevitable trend. Therefore, this review covers all aspects of PNT research, in which major advances in understanding the resource microorganisms, mechanism of action, and biosynthesis pathway of PNT were achieved and diverse clinical applications of PNT were emphasized, and it will lay the foundation for commercial transformation and industrial technology of PNT based on systematic metabolic engineering.