Glycoconjugate Journal最新文献_第2页

Review on macrophage polarization during visceral leishmaniasis and impact of glycoprotein. 内脏利什曼病巨噬细胞极化及糖蛋白影响的研究进展。

IF 3.1 4区生物学

Glycoconjugate Journal Pub Date : 2026-01-09 DOI: 10.1007/s10719-025-10206-w

Nayanika Datta, Sajal Dasmahapatra, Madhusri Pramanik, Santanu Kar Mahapatra

引用次数: 0

Integrating plasma protein-centric multi-omics to evaluate the causal effect of glycosylation on the risk of cancer. 整合以血浆蛋白为中心的多组学来评估糖基化对癌症风险的因果影响。

IF 3.1 4区生物学

Glycoconjugate Journal Pub Date : 2026-01-06 DOI: 10.1007/s10719-025-10207-9

Zhi Geng, Kangwei Qi, Long Yu, Yuanyuan Ruan, Jianxin Gu, Shushu Song

{"title":"Integrating plasma protein-centric multi-omics to evaluate the causal effect of glycosylation on the risk of cancer.","authors":"Zhi Geng, Kangwei Qi, Long Yu, Yuanyuan Ruan, Jianxin Gu, Shushu Song","doi":"10.1007/s10719-025-10207-9","DOIUrl":"https://doi.org/10.1007/s10719-025-10207-9","url":null,"abstract":"Glycosylation is a crucial post-translational modification, and numerous studies have reported its significant role in cancer progression. Nevertheless, no study has comprehensively analyzed the causal effect of glycosylation on the risk of cancer till now. Herein, we identified 32 SNPs of glycosylation-related genes (GRGs) that correlated with the risk of 8 kinds of cancer by summary-statistics-based mendelian randomization (SMR) analysis for genome-wide association study (GWAS) data. Next, the heterogeneity in dependent instrument (HEIDI) test and colocalisation analysis were utilized to verify the heterogeneity and consistency of SMR results. Further fine-mapping of causal gene set (FOCUS) analysis based on transcriptome-wide association study (TWAS) data showed that rs9810189 of ST6GAL1 and rs223489 of MANBA were negatively correlated with the risk of breast cancer and squamous cell carcinoma, respectively. Moreover, the MANBA protein in blood plasma also exhibited a probably negative causal effect on squamous cell carcinoma according to two-sample MR analyses for protein quantitative trait locus (pQTLs). In addition, single-cell RNA sequencing analysis and Kaplan-Meier plot analysis were performed to evaluate the potential role of GRGs in corresponding cancer prioritized by the above MR analysis. Finally, we attempted to illustrate the function of glycosyltransferases and investigate the druggable status of GRGs. Together, our study comprehensively analyzed the causal effect of glycosylation on cancer risk and identified potential strategies for cancer treatment.","PeriodicalId":12762,"journal":{"name":"Glycoconjugate Journal","volume":"43 1","pages":"6"},"PeriodicalIF":3.1,"publicationDate":"2026-01-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145911201","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

SPR interaction analysis of GM3 glycan with the integrin α5β1 head domain. GM3聚糖与整合素α5β1头部结构域的SPR相互作用分析。

IF 3.1 4区生物学

Glycoconjugate Journal Pub Date : 2026-01-06 DOI: 10.1007/s10719-025-10205-x

Shinya Hanashima, Migiwa Kishi, Katsuaki Sasaki, Yusuke Sato, Michio Murata

{"title":"SPR interaction analysis of GM3 glycan with the integrin α5β1 head domain.","authors":"Shinya Hanashima, Migiwa Kishi, Katsuaki Sasaki, Yusuke Sato, Michio Murata","doi":"10.1007/s10719-025-10205-x","DOIUrl":"https://doi.org/10.1007/s10719-025-10205-x","url":null,"abstract":"Integrins are heterodimeric receptors involved in cell adhesion and bidirectional signaling. Ganglioside GM3 in the outer leaflet of cell membranes possibly regulates integrin activity via direct interactions; however, its specific binding mode with integrins remains unclear. Therefore, in this study, we focused on the GM3 glycan moiety, which encounters the integrin ectodomain on the cell surface, and synthesized a soluble GM3 probe without hydrocarbon chains using a chemoenzymatic approach. Binding analysis using surface plasmon resonance (SPR) indicated that the synthetic GM3 probe interacts with the integrin α5β1 ectodomain with a significantly higher affinity than the lactosylceramide probe. Saturation transfer difference (STD) NMR spectra suggested that the integrin α5β1 ectodomain interacts with N-acetylneuraminic acid (Neu5Ac) at the GM3 terminal and α2-3Gal linkage. Notably, RGD peptide, an integrin ligand interacting with the heterodimer interface, competed with GM3 to bind to integrin α5β1 on the SPR sensor chip. Consistent with these results, the GM3-binding site predicted by Chai-1 partially overlapped with the RGD peptide-binding groove on integrin α5β1; however, the binding mode was different. RGD peptide bridged the α and β subunits of the integrin head moiety, whereas the GM3 probe found at the cleft between the subunits. The Neu5Ac-Gal moiety primarily interacts with the metal ion-dependent adhesion site and nearby residues in the β1 subunit. Overall, our findings suggest that gangliosides directly interact with integrin α5β1 at a previously unknown binding site, revealing a novel regulatory mechanism for the integrin activity.","PeriodicalId":12762,"journal":{"name":"Glycoconjugate Journal","volume":"43 1","pages":"5"},"PeriodicalIF":3.1,"publicationDate":"2026-01-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145911181","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Assessment of IgG N-Glycan patterns in adult patients with immune thrombocytopenia and healthy individuals. 成年免疫性血小板减少症患者和健康人IgG n -聚糖模式的评估。

IF 3.1 4区生物学

Glycoconjugate Journal Pub Date : 2026-01-04 DOI: 10.1007/s10719-025-10199-6

Ena Ranković, Natali Nakić Bedeković, Frano Vučković, Irena Trbojević-Akmačić, Maja Pučić-Baković, Gordan Lauc, Dražen Pulanić

引用次数: 0

Mass spectrometric profiling reveals alterations in N-Glycans and O-Glycans in Tay-Sachs disease under Autophagy-Induced conditions. 质谱分析揭示了自噬诱导条件下Tay-Sachs病n -聚糖和o -聚糖的变化。

IF 3.1 4区生物学

Glycoconjugate Journal Pub Date : 2025-12-29 DOI: 10.1007/s10719-025-10203-z

Melike Can, Hande Basirli, Chunsheng Jin, Niclas G Karlsson, Daniel Bojar, Volkan Seyrantepe

{"title":"Mass spectrometric profiling reveals alterations in N-Glycans and O-Glycans in Tay-Sachs disease under Autophagy-Induced conditions.","authors":"Melike Can, Hande Basirli, Chunsheng Jin, Niclas G Karlsson, Daniel Bojar, Volkan Seyrantepe","doi":"10.1007/s10719-025-10203-z","DOIUrl":"https://doi.org/10.1007/s10719-025-10203-z","url":null,"abstract":"Tay-Sachs disease is a rare neurodegenerative disorder caused by mutations in the HEXA gene. The HEXA gene encodes the α-subunit of the enzyme β-hexosaminidase A, which degrades GM2 ganglioside. Previously, we identified impaired autophagy in the brains of a mouse model of Tay-Sachs disease, which exhibited neuropathological and clinical abnormalities. Moreover, we demonstrated autophagosome clearance in Tay-Sachs cells under lithium-induced conditions. Here, we further aimed to evaluate N- and O-glycan changes in these cells and examine whether glycan alterations are linked to ER stress. The profiles of N- and O-glycans were analyzed using LC-MS/MS in fibroblasts and neuroglial cells from 5-month-old Hexa-/-Neu3-/- mice and neuroglial cells from Tay-Sachs patients under lithium induction and nutrient deprivation. The expression levels of ER stress-related markers were assessed using qRT-PCR and Western blot analyses. We demonstrated higher levels of high mannose and lower levels of complex types of N-glycans, along with increased O-glycan levels in Tay-Sachs cells. Compared to control groups, we observed upregulated expression of endoplasmic reticulum (ER) stress-related markers, CHOP and ATF-6, in Tay-Sachs cells. Our study demonstrated that autophagy induction causes the degradation of accumulated high-mannose N-glycans and O-glycans, which is associated with the downregulation of ER stress-related genes in Tay-Sachs cells. Our study is the first to show this phenomenon in Tay-Sachs cells and suggests the presence of ER stress-mediated autophagy. Therefore, targeting glycans through autophagy induction could offer therapeutic benefits to patients with Tay-Sachs disease in future studies.","PeriodicalId":12762,"journal":{"name":"Glycoconjugate Journal","volume":"43 1","pages":"3"},"PeriodicalIF":3.1,"publicationDate":"2025-12-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145849412","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

High molecular weight fucosylated glycosaminoglycan promotes the binding of antithrombin and thrombin: a template mechanism and structure-activity relationship study. 高分子量聚焦糖胺聚糖促进抗凝血酶和凝血酶结合：模板机制及构效关系研究。

IF 3.1 4区生物学

Glycoconjugate Journal Pub Date : 2025-12-23 DOI: 10.1007/s10719-025-10200-2

Chuang Xiao, Li Xu, Ying Cai, Zhenhua Liu, Yingnian Li, Na Gao, Jinhua Zhao

{"title":"High molecular weight fucosylated glycosaminoglycan promotes the binding of antithrombin and thrombin: a template mechanism and structure-activity relationship study.","authors":"Chuang Xiao, Li Xu, Ying Cai, Zhenhua Liu, Yingnian Li, Na Gao, Jinhua Zhao","doi":"10.1007/s10719-025-10200-2","DOIUrl":"10.1007/s10719-025-10200-2","url":null,"abstract":"Native fucosylated glycosaminoglycan (FG), a structurally unique polysaccharide with chondroitin sulfate like backbone and sulfated fucose side chains, has multiple anticoagulant mechanisms. Analyzing the interaction between FG and coagulation proteins will help to further understand its pharmacological mechanisms. Previously, we have reported that high molecular weight depolymerized FG (dFG) and unfractionated heparin (UFH) exhibit different binding models for antithrombin (AT), which is a primary natural anticoagulant in plasma by inhibiting coagulation proteases including thrombin (FIIa). In this study, the effect of dFG or UFH on the interaction between AT and FIIa was detected by biolayer interferometry. The relative AT binding affinity and AT-dependent anti-FIIa activity of dFG derivatives were measured to elucidate the structure-activity relationship. The results demonstrate that high molecular weight dFG significantly promotes the irreversible binding of FIIa and AT by a template mechanism. As the molecular weight decreases, the relative AT binding affinity of dFG decreases and molecular weight above 8.55 kDa is required for their interaction in this study. Both the fucose side chains and carboxyl groups are indispensable for dFG to bind with AT and inhibit FIIa activity. This study clarifies the mechanism and structure-activity relationship of dFG inhibiting FIIa by AT, providing references for the development of novel anticoagulant drugs based on FG and its derivatives.","PeriodicalId":12762,"journal":{"name":"Glycoconjugate Journal","volume":"43 1","pages":"2"},"PeriodicalIF":3.1,"publicationDate":"2025-12-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145809708","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Identification of a distinct sialic acid (KDN) and a KDN-specific aldolase in Pacific oyster. 太平洋牡蛎中独特唾液酸（KDN）及其特异性醛缩酶的鉴定。

IF 3.1 4区生物学

Glycoconjugate Journal Pub Date : 2025-12-19 DOI: 10.1007/s10719-025-10202-0

Zi-Xuan Hu, Jia-Yu Zhang, Jitske van Ede, Yao-Yao Zhang, Yu-Quan Li, Mattia Ghirardello, M Carmen Galan, Martin Pabst, Li Liu, Josef Voglmeir

{"title":"Identification of a distinct sialic acid (KDN) and a KDN-specific aldolase in Pacific oyster.","authors":"Zi-Xuan Hu, Jia-Yu Zhang, Jitske van Ede, Yao-Yao Zhang, Yu-Quan Li, Mattia Ghirardello, M Carmen Galan, Martin Pabst, Li Liu, Josef Voglmeir","doi":"10.1007/s10719-025-10202-0","DOIUrl":"https://doi.org/10.1007/s10719-025-10202-0","url":null,"abstract":"Sialic acids are a diverse family of acidic sugars typically found at the terminal positions of glycan chains, mediating key physiological and pathological processes across animals - particularly vertebrates - including cell signaling and host-pathogen interactions. The distribution of sialic acids in lower animals such as mollusks, however, remains largely unresolved. Here, we report the discovery of unconjugated 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid (KDN), a deaminated analogue of N-acetylneuraminic acid, in the muscle tissue of Pacific oysters (Magallana gigas). Using UPLC-ESI-MS/MS fingerprinting, we identified naturally occurring free KDN at a concentration of 1.2 ± 0.1 nmol/100 mg of oyster muscle tissue. To investigate the biosynthetic pathway, four candidate genes were identified in the M. gigas genome, and the corresponding recombinant proteins were expressed and characterized. Enzymatic assays revealed that one putative sialic acid aldolase (MgNPL) specifically catalyzes the cleavage of KDN into mannose and pyruvate. To our knowledge, this represents the first molecular evidence of KDN metabolism in mollusks and highlights both the unexpected conservation of substrate-specific aldolase activity and distinct sialic acid utilization mechanisms compared to vertebrates.","PeriodicalId":12762,"journal":{"name":"Glycoconjugate Journal","volume":"43 1","pages":"1"},"PeriodicalIF":3.1,"publicationDate":"2025-12-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145794172","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Advanced glycation end products (AGEs) and their role in diabetes mellitus and related complications: mechanisms and therapeutic insights. 晚期糖基化终产物（AGEs）及其在糖尿病和相关并发症中的作用：机制和治疗见解。

IF 3.1 4区生物学

Glycoconjugate Journal Pub Date : 2025-12-01 Epub Date: 2025-09-22 DOI: 10.1007/s10719-025-10194-x

Eskandar Qaed, Waleed Aldahmash, Mueataz A Mahyoub

{"title":"Advanced glycation end products (AGEs) and their role in diabetes mellitus and related complications: mechanisms and therapeutic insights.","authors":"Eskandar Qaed, Waleed Aldahmash, Mueataz A Mahyoub","doi":"10.1007/s10719-025-10194-x","DOIUrl":"10.1007/s10719-025-10194-x","url":null,"abstract":"Diabetes mellitus (DM) is marked by prolonged elevated blood glucose levels, which lead to the formation of covalent adducts between glucose and plasma proteins through a non-enzymatic reaction called glycation. This biochemical process plays a crucial role in the development of DM complications, including retinopathy, nephropathy, neuropathy, and cardiomyopathy, while also impacting conditions such as rheumatoid arthritis, osteoporosis, and aging. Glycation alters the molecular structure, enzymatic activity, and receptor interactions of proteins, affecting their normal functions. Advanced glycation end products (AGEs) arise from these modifications, forming cross-links within and between cells, which affect proteins and other vital biomolecules, such as lipids and nucleic acids. This contributes significantly to the complex complications associated with DM. Recent studies highlight the interaction between AGEs and their specific receptors, receptor for advanced glycation end products (RAGE), located on the plasma membrane. This involvement initiates changes in intracellular signaling, alters gene expression, and stimulates the release of pro-inflammatory cytokines and reactive oxygen species. This review examines the glycation of key plasma proteins albumin, fibrinogen, globulins, and collagen and discusses the various AGEs formed. Furthermore, it elucidates the role of AGEs in the exacerbation of DM complications, providing a comprehensive overview of the molecular pathways involved and the systemic impact of these glycation products.","PeriodicalId":12762,"journal":{"name":"Glycoconjugate Journal","volume":" ","pages":"209-223"},"PeriodicalIF":3.1,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145112885","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Eukaryotic expression and characterization of two α1,2-fucosyltransferase genes in the histo-blood group antigens synthesis pathway of the Pacific oyster (Crassostrea gigas). 两个α1,2-聚焦转移酶基因在太平洋牡蛎（长牡蛎）组织血型抗原合成途径中的真核表达及特性研究。

IF 3.1 4区生物学

Glycoconjugate Journal Pub Date : 2025-12-01 Epub Date: 2025-10-01 DOI: 10.1007/s10719-025-10195-w

Junxia Hu, Meng Qu, Weiran Zhang, Binbin Gui, Yanhua Jiang, Lin Yao, Shixin Wang, Dapeng Wang

{"title":"Eukaryotic expression and characterization of two α1,2-fucosyltransferase genes in the histo-blood group antigens synthesis pathway of the Pacific oyster (Crassostrea gigas).","authors":"Junxia Hu, Meng Qu, Weiran Zhang, Binbin Gui, Yanhua Jiang, Lin Yao, Shixin Wang, Dapeng Wang","doi":"10.1007/s10719-025-10195-w","DOIUrl":"10.1007/s10719-025-10195-w","url":null,"abstract":"Norovirus (NoV), an important cause of human viral gastroenteritis worldwide, recognizes human histo-blood group antigens (HBGAs) as receptors. Oysters are a vector of foodborne transmission of NoV, and HBGAs have been found in oyster tissues. In this study, CgFUT1 and CgFUT2, the key genes involved in the synthesis of HBGAs in Crassostrea gigas, were successfully expressed in Pichia pastoris, and 32.6 kDa target proteins were obtained after purification, concentration, and dialysis treatments. Western blot analysis using FUT1 and FUT2 antibodies showed that CgFUT1 and CgFUT2 have antigenic similarity as human FUT1 and FUT2. Enzyme catalysis assays using Galβ1-3GlcNAc and Galβ1-4GlcNAc as substrates showed that these substrates react with GDP-Fuc to generate Fucα1-2GalβGlcNAc under the action of CgFUT1 and CgFUT2. High-resolution mass spectrometry analysis revealed that CgFUT1 and CgFUT2 have the same substrate specificity, both reacting with Galβ1-3GlcNAc and Galβ1-4GlcNAc. The results of this study demonstrate the probable role of CgFUT1 and CgFUT2 in regulating substrates for H antigen synthesis in oysters and provide a reference for future studies into the functions of these genes. The study also lays a foundation for further exploration of the molecular mechanisms underlying NoV accumulation in oysters.","PeriodicalId":12762,"journal":{"name":"Glycoconjugate Journal","volume":" ","pages":"283-293"},"PeriodicalIF":3.1,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145199079","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Asparagine-linked glycosylation protein 1 (ALG1) promotes aggressive phenotypes of lung adenocarcinoma cells, A549, via modulating N-linked glycosylation and ER-Stress. 天冬酰胺连接糖基化蛋白1 （ALG1）通过调节n -连接糖基化和内质网应激促进肺腺癌细胞A549的侵袭性表型。

IF 3.1 4区生物学

Glycoconjugate Journal Pub Date : 2025-12-01 Epub Date: 2025-10-09 DOI: 10.1007/s10719-025-10198-7

Kanadit Piriyapairoje, Marta Baro, Aanchal Katoch, Bryce De Muth, Ludovica Villanti, Charupong Saengboonmee, Sopit Wongkham, Joseph N Contessa, Chatchai Phoomak

{"title":"Asparagine-linked glycosylation protein 1 (ALG1) promotes aggressive phenotypes of lung adenocarcinoma cells, A549, via modulating N-linked glycosylation and ER-Stress.","authors":"Kanadit Piriyapairoje, Marta Baro, Aanchal Katoch, Bryce De Muth, Ludovica Villanti, Charupong Saengboonmee, Sopit Wongkham, Joseph N Contessa, Chatchai Phoomak","doi":"10.1007/s10719-025-10198-7","DOIUrl":"10.1007/s10719-025-10198-7","url":null,"abstract":"Glycosylation plays a critical role in various biological processes and is essential for cell survival. Aberrant glycosylation has been implicated in numerous diseases, including cancer. Lung cancer remains the leading cause of cancer-related mortality worldwide. The correlation between lung cancer progression and abnormal glycosylation has been demonstrated previously. Asparagine-linked glycosylation protein 1 (ALG1) is a key enzyme involved in the N-linked glycosylation process; however, its role in cancer progression remains unclear. In this study, we investigated the function of ALG1 in lung cancer progression. Analysis of the Cancer Genome Atlas (TCGA) dataset revealed that ALG1 expression was significantly upregulated in lung tumor tissues and was associated with poor patient prognosis. To explore its functional relevance, ALG1 expression was depleted in A549 lung adenocarcinoma cells using CRISPR-Cas9-mediated knockout. Loss of ALG1 led to reduced levels of protein N-linked glycosylation and induced an endoplasmic reticulum (ER)-stress response. Functionally, ALG1 knockout significantly impaired A549 cell proliferation, migration, and invasion, as evidenced by phenotypic assays and molecular markers. Moreover, the extent of glycosylation deficiency was positively correlated with ER-stress activation and inversely associated with cancer cell aggressiveness. These findings suggest that ALG1 promotes lung cancer aggressiveness through the regulation of protein glycosylation and modulation of ER-stress pathways. Overall, this study highlights the potential of ALG1 as a therapeutic target and a prognostic biomarker for lung adenocarcinoma patients.","PeriodicalId":12762,"journal":{"name":"Glycoconjugate Journal","volume":" ","pages":"267-281"},"PeriodicalIF":3.1,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145250824","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0