Glycobiology最新文献_第2页

GlycoSiteMiner: an ML/AI-assisted literature mining-based pipeline for extracting glycosylation sites from PubMed abstracts. GlycoSiteMiner：一个ML/ ai辅助的基于文献挖掘的管道，用于从PubMed摘要中提取糖基化位点。

IF 3.4 3区生物学

Glycobiology Pub Date : 2025-06-02 DOI: 10.1093/glycob/cwaf030

Robel Kahsay, Urnisha Bhuiyan, Cyrus Chun Hong Au, Nathan Edwards, Luke Johnson, Sujeet Kulkarni, Karina Martinez, Rene Ranzinger, K Vijay-Shanker, Jeet Vora, Kate Warner, Michael Tiemeyer, Raja Mazumder

{"title":"GlycoSiteMiner: an ML/AI-assisted literature mining-based pipeline for extracting glycosylation sites from PubMed abstracts.","authors":"Robel Kahsay, Urnisha Bhuiyan, Cyrus Chun Hong Au, Nathan Edwards, Luke Johnson, Sujeet Kulkarni, Karina Martinez, Rene Ranzinger, K Vijay-Shanker, Jeet Vora, Kate Warner, Michael Tiemeyer, Raja Mazumder","doi":"10.1093/glycob/cwaf030","DOIUrl":"10.1093/glycob/cwaf030","url":null,"abstract":"Over 50% of human proteins are estimated to be glycosylated, making glycosylation one of the most common post-translational modifications (PTMs) of proteins. A glycoinformatics resource such as the GlyGen knowledgebase, consisting of experimentally verified sequence-specific glycosylation sites, is critical for advancing research in glycobiology. Unfortunately, most experimental studies report glycosylation sites in free text format in scientific literature, mentioning gene names and amino acid positions without providing protein sequence identifiers, making it difficult to mine reported sites that can be mapped onto specific protein sequences. We have developed GlycoSiteMiner, which is an automated literature mining-based pipeline that extracts experimentally verified protein sequence-specific glycosylation sites from PubMed abstracts. The pipeline employs ML/AI algorithms to filter out incorrectly identified sites and has been applied to 33 million PubMed abstracts, identifying 1118 new sequence-specific glycosylation sites that were not previously present in the GlyGen resource.","PeriodicalId":12766,"journal":{"name":"Glycobiology","volume":" ","pages":""},"PeriodicalIF":3.4,"publicationDate":"2025-06-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12130968/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144119597","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Systematic and comprehensive analysis of major localizations of alpha-dystroglycan-specific modifying enzymes. 系统、全面地分析α -糖醛酸特异性修饰酶的主要定位。

IF 3.4 3区生物学

Glycobiology Pub Date : 2025-06-02 DOI: 10.1093/glycob/cwaf027

Shinya Aso, Martin Lowe, Kazutoshi Mori, Satoshi Ninagawa

{"title":"Systematic and comprehensive analysis of major localizations of alpha-dystroglycan-specific modifying enzymes.","authors":"Shinya Aso, Martin Lowe, Kazutoshi Mori, Satoshi Ninagawa","doi":"10.1093/glycob/cwaf027","DOIUrl":"10.1093/glycob/cwaf027","url":null,"abstract":"Dystroglycan (DG) binds to extracellular matrix via its O-glycans, which are sequentially modified in a specific order by DG-specific enzymes: POMGNT2, B3GalNT2, and POMK in the endoplasmic reticulum (ER), followed by FKTN, FKRP, TMEM5, B4GAT1 and LARGE1 in the Golgi apparatus. However, there have been no comprehensive and systematic studies on the major localization of these enzymes. Here, we expressed fluorescent fusion proteins of DG-specific modifying enzymes under the control of short CMV promoter and observed their primary localization using the latest microscopy along with localization markers: mEGFP-KDEL for the ER, GM130 and GRASP55 for the cis-/medial-Golgi, and TGN46 and GCC1 for the trans-Golgi network. As a result, POMGNT2 and B3GalNT2 were localized to the ER as expected, but POMK was localized predominantly to the cis-/medial-Golgi showing co-localization with GRASP55. FKTN, FKRP and TMEM5 were partially co-localized with both cis-/medial- and trans-Golgi network markers. Though B4GAT1 did not co-localize with GM130 or TGN46, it co-localized with GCC1 another trans-Golgi network marker, indicating Golgi subcompartmentalization. LARGE1, the final glycosyltransferase involved in the modification of DG's O-glycan, was localized in the cis-/medial-Golgi, but did not overlap with trans-Golgi network markers. An EndoH sensitivity assay demonstrated that DG-specific enzymes interacting with DG were localized in the early secretory pathway. Our results reveal that POMK and B4GAT1 function at locations distinct from their major localization and support the conclusion that the modification of matriglycan on DG is completed at the cis-/medial-Golgi.","PeriodicalId":12766,"journal":{"name":"Glycobiology","volume":" ","pages":""},"PeriodicalIF":3.4,"publicationDate":"2025-06-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143982901","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"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

Tools for investigating host-microbe crosstalk using glycan analysis probes inspired by human lectins. 利用受人凝集素启发的聚糖分析探针研究宿主-微生物串扰的工具。

IF 3.4 3区生物学

Glycobiology Pub Date : 2025-06-02 DOI: 10.1093/glycob/cwaf031

Soumi Ghosh, Rajeev Chorghade, Roger C Diehl, Greg J Dodge, Sunhee Bae, Amanda E Dugan, Melanie Halim, Michael G Wuo, Helen Bartlett, Liam Herndon, Laura L Kiessling, Barbara Imperiali

{"title":"Tools for investigating host-microbe crosstalk using glycan analysis probes inspired by human lectins.","authors":"Soumi Ghosh, Rajeev Chorghade, Roger C Diehl, Greg J Dodge, Sunhee Bae, Amanda E Dugan, Melanie Halim, Michael G Wuo, Helen Bartlett, Liam Herndon, Laura L Kiessling, Barbara Imperiali","doi":"10.1093/glycob/cwaf031","DOIUrl":"10.1093/glycob/cwaf031","url":null,"abstract":"Human lectins are critical carbohydrate-binding proteins that recognize diverse glycoconjugates from microorganisms and can play a key role in host-microbe interactions. Despite their importance in immune recognition and microbe binding, the specific glycan ligands and functions of many human lectins remain poorly understood. Using previous proof-of-concept studies on selected lectins as the foundation for this work, we present ten additional glycan analysis probes (GAPs) from a diverse set of human soluble lectins, offering robust tools to investigate glycan-mediated interactions. We describe a protein engineering platform that enables scalable production of GAPs that maintain native-like conformations and oligomerization states, equipped with functional reporter tags for targeted glycan profiling. We demonstrate that the soluble GAP reagents can be used in various applications, including glycan array analysis, mucin-binding assays, tissue staining, and microbe binding in complex populations. These capabilities make GAPs valuable for dissecting interactions relevant to understanding host responses to microbes. The tools can also be used to probe differential microbial and mammalian glycan interactions, which are crucial for understanding the interactions of lectins in a physiological environment where both glycan types exist. GAPs have potential as diagnostic and prognostic tools for detecting glycan alterations in chronic diseases, microbial dysbiosis, and immune-related conditions.","PeriodicalId":12766,"journal":{"name":"Glycobiology","volume":" ","pages":""},"PeriodicalIF":3.4,"publicationDate":"2025-06-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12167852/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144150308","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

The Multifaceted Roles of Galectins in Host-Virus Interactions: A Comprehensive Overview. 凝集素在宿主-病毒相互作用中的多重作用：全面概述。

IF 3.4 3区生物学

Glycobiology Pub Date : 2025-04-23 DOI: 10.1093/glycob/cwaf026

Ying-Wei Tung, Zih-Syuan Yang, Jie-Yu Huang, Yun-Tzu Hsu, Ching-I Tsui, Mahmoud Salama Hemdan, Sneha Tadikamalla, Albright Dew Baua, Wanchai Assavalapsakul, Arunee Thitithanyanont, Day-Yu Chao, Fu-Tong Liu, Sheng-Fan Wang

{"title":"The Multifaceted Roles of Galectins in Host-Virus Interactions: A Comprehensive Overview.","authors":"Ying-Wei Tung, Zih-Syuan Yang, Jie-Yu Huang, Yun-Tzu Hsu, Ching-I Tsui, Mahmoud Salama Hemdan, Sneha Tadikamalla, Albright Dew Baua, Wanchai Assavalapsakul, Arunee Thitithanyanont, Day-Yu Chao, Fu-Tong Liu, Sheng-Fan Wang","doi":"10.1093/glycob/cwaf026","DOIUrl":"https://doi.org/10.1093/glycob/cwaf026","url":null,"abstract":"Galectins are a family of β-galactosides-binding protein, crucial regulators of host-virus interactions. They achieve this by recognizing specific glycan patterns on viral surfaces or mediating interactions with intracellular viral or host proteins, subsequently influencing the critical phases of the viral life cycle, such as attachment, replication, immune evasion, and reactivation. Furthermore, galectins modulate host immune responses, shaping the progression and outcomes of viral infections. This review comprehensively examines the roles of both endogenous and exogenous galectins in viral infections, noting that only a few galectins, including Galectin-1, -3, -4, -7, -8, and -9, Have been identified as key players in viral infection. Notably, Galectin-1, -3, and -9 play diverse functions in both DNA and RNA viral infection. Emerging evidence highlights the potential of Galectin-4 and -8 as intracellular sensors and modulators of viral pathogenesis. Endogenous galectins, produced by host cells, act through both glycan-dependent and glycan-independent mechanisms, influencing viral processes and immune responses. Exogenous galectins, which are secreted by other cells or administered as recombinant proteins, can either enhance or counteract the actions of endogenous galectins. The functions of galectins are virus-specific and context-dependent, serving as either promoters or inhibitors of viral replication and reactivation. Dysregulation of galectin expression is often linked to disease progression, highlighting their potential as diagnostic and prognostic biomarkers, as well as therapeutic targets. The important and varied roles that galectins play in viral infections are highlighted in this review, which also provides fresh insights into host-pathogen interactions and the development of antiviral tactics.Highlights: ","PeriodicalId":12766,"journal":{"name":"Glycobiology","volume":"35 6","pages":""},"PeriodicalIF":3.4,"publicationDate":"2025-04-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143998539","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"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

Tumor Hemorrhage-inducing polysaccharides secreted by streptococci and Serratia proposed as the active principal ingredients (API's) of Coley's toxin: on PS1, the Serratia marcescens API. 提出由链球菌和沙雷氏菌分泌的肿瘤致出血多糖作为Coley毒素的活性主成分（API’s）：在PS1上，为粘质沙雷氏菌API。

IF 3.4 3区生物学

Glycobiology Pub Date : 2025-04-23 DOI: 10.1093/glycob/cwaf021

Roger A Laine, Henry W Lopez, Hiromu Takematsu

{"title":"Tumor Hemorrhage-inducing polysaccharides secreted by streptococci and Serratia proposed as the active principal ingredients (API's) of Coley's toxin: on PS1, the Serratia marcescens API.","authors":"Roger A Laine, Henry W Lopez, Hiromu Takematsu","doi":"10.1093/glycob/cwaf021","DOIUrl":"https://doi.org/10.1093/glycob/cwaf021","url":null,"abstract":"Coley's Toxin comprised a mixture of cell-free, heat-treated culture media from Streptococcus pyogenes (originally Streptococus erysipelatos) and Serratia marcescens (originally Bacillus prodigiosus). A 250 kDa tumor hemorrhage-inducing polysaccharide \"PS1\" is reported here secreted into culture medium by S. marcescens. Four h after PS1 is injected at 32 μg/kg (10pM) into the tail vein of Balb/C mice bearing C26 subcutaneous colon-derived tumors, tumor-specific capillary hemorrhage is exhibited in 90% of tumors. As a positive control, CM101, a similar tumor hemorrhagic polysaccharide from Streptococcus agalactica caused tumor hemorrhage in 75% of tumors in the Balb/C-C26 model at 7.5 μg/kg(2.5pM). CM101 has previously been safety tested in a Phase I clinical trial. These two polysaccharides have merit to be identified as the active principal ingredients (API's) of Coley'sToxin. Additional approaches to cancer therapy are a global need. No matter the level of wealth of victims, some cancers are still incurable. Recall in recent years the tragic early cancer deaths of Steve Jobs and Paul Allen among other luminaries. Streptococcal and Serratia bacterial extracts have unique tumor specific capillary destructive activity, with observations originating with sarcomas cured by nosocomial erysipelas infections in the 1860's. The active pharmaceutical ingredients (API's) in these extracts and Coley's Toxins are proposed to be polysaccharides.","PeriodicalId":12766,"journal":{"name":"Glycobiology","volume":"35 6","pages":""},"PeriodicalIF":3.4,"publicationDate":"2025-04-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143969573","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"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

Nicotiana tabacum contains two alpha1,3-fucosyltransferase types, one of which is able to catalyze core fucosylation of high-mannose N-glycans. 烟草含有两种α 1,3-聚焦转移酶，其中一种能够催化高甘露糖n -聚糖的核心聚焦。

IF 3.4 3区生物学

Glycobiology Pub Date : 2025-04-23 DOI: 10.1093/glycob/cwaf024

Catherine Navarre, Nicolas Bailly, Juliette Balieu, Olivier Perruchon, Xavier Herman, Antoine Mercier, Adeline Courtoy, Patrice Lerouge, Muriel Bardor, François Chaumont

{"title":"Nicotiana tabacum contains two alpha1,3-fucosyltransferase types, one of which is able to catalyze core fucosylation of high-mannose N-glycans.","authors":"Catherine Navarre, Nicolas Bailly, Juliette Balieu, Olivier Perruchon, Xavier Herman, Antoine Mercier, Adeline Courtoy, Patrice Lerouge, Muriel Bardor, François Chaumont","doi":"10.1093/glycob/cwaf024","DOIUrl":"https://doi.org/10.1093/glycob/cwaf024","url":null,"abstract":"N-glycosylation is a critical quality attribute to consider when expressing recombinant glycoproteins in eukaryotic cells including plant cells. N-acetylglucosaminyltransferase I (GnTI) initiates complex N-glycan maturation in the Golgi apparatus by transferring a single N-acetylglucosamine (GlcNAc) residue on the alpha1,3-arm of a Man5 N-glycan acceptor. This step is required for the processing of high mannose into hybrid and complex N-glycans. Therefore, Arabidopsis mutants lacking GnTI activity display accumulation of Man5 N-glycans instead of complex N-glycans and do not synthesise N-glycans containing core alpha1,3-fucose residue. In contrast, GnTI knockout cell line of Nicotiana tabacum BY-2 still displays a little core alpha1,3-fucose signal on western blotting. Here, we show that N. tabacum contains two alpha1,3-fucosyltransferase types, one of which is able to transfer a core alpha1,3-fucose on a Man5 substrate when no Man5Gn substrate is available such as in BY-2 GnTI knock-out cell lines.","PeriodicalId":12766,"journal":{"name":"Glycobiology","volume":"35 6","pages":""},"PeriodicalIF":3.4,"publicationDate":"2025-04-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143984023","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"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

Myriad mechanisms: factors regulating the synthesis of aberrant mucin-type O-glycosylation found on cancer cells. 多种机制：在癌细胞上发现的调节异常黏液型o糖基化合成的因素。

IF 3.4 3区生物学

Glycobiology Pub Date : 2025-04-23 DOI: 10.1093/glycob/cwaf023

Joanna Cull, Ryan C Pink, Priya Samuel, Susan A Brooks

{"title":"Myriad mechanisms: factors regulating the synthesis of aberrant mucin-type O-glycosylation found on cancer cells.","authors":"Joanna Cull, Ryan C Pink, Priya Samuel, Susan A Brooks","doi":"10.1093/glycob/cwaf023","DOIUrl":"10.1093/glycob/cwaf023","url":null,"abstract":"Mucin-type O-linked glycosylation is initiated by the transfer of a single N-acetyl-D-galactosamine (GalNAc) to the hydroxyl group of either a serine (Ser) or threonine (Thr) residue. This process is catalysed by a portfolio of twenty isoenzymes, the UDP-N-acetyl-α-D-galactosamine:polypeptide N-acetylgalactosaminyltransferases (ppGalNAc-Ts, GalNAc-Ts or GALNTs) to create the Thomsen nouvelle (Tn) antigen (GalNAcα1-O-Ser/Thr ). In healthy adult cells, Tn antigen is further elaborated by the action of specific glycosyltransferases to either form one of eight core structures, which themselves can be extended to form more complex glycans, or into sialyl Tn or sialyl core 1 (sialyl T), where sialylation terminates chain extension. These O-glycans, produced through mucin-type O-linked glycosylation, are a feature of many secreted and membrane-bound proteins, and are fundamental in a wide range of biological functions. Dysregulation of this process, often resulting in the exposure of usually cryptic truncated O-glycans including Tn antigen, is important in a wide range of pathologies and has been implicated in cancer metastasis. The regulation of mucin-type O-linked glycosylation, in health and disease, is highly complex and not fully understood. It is determined by a myriad of mechanisms, from transcriptional control, mutation, posttranslational control, stability of transferases, their relocation within the secretory pathway, and changes in the fundamental structure and environment of the Golgi apparatus. This review presents an overview of the evidence for these potential regulatory steps in the synthesis of truncated mucin-type O-linked glycans in cancer.","PeriodicalId":12766,"journal":{"name":"Glycobiology","volume":" ","pages":""},"PeriodicalIF":3.4,"publicationDate":"2025-04-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143977272","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"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

Glyco you should know. Glyco你应该知道。

IF 3.4 3区生物学

Glycobiology Pub Date : 2025-04-23 DOI: 10.1093/glycob/cwaf029

Lilyanna Massman

引用次数: 0

Ephrin-B1 regulates cell surface residency of heparan sulfate proteoglycans (HSPGs) and complexes with the HSPG CD44V3-10 and fibroblast growth factor receptors. Ephrin-B1调节硫酸肝素蛋白聚糖（HSPGs）及其与HSPG CD44V3-10和成纤维细胞生长因子受体的复合物的细胞表面驻留。

IF 3.4 3区生物学

Glycobiology Pub Date : 2025-04-23 DOI: 10.1093/glycob/cwaf020

Kristian Prydz, Roger Simm, Erna Davydova, Hans-Christian Aasheim

{"title":"Ephrin-B1 regulates cell surface residency of heparan sulfate proteoglycans (HSPGs) and complexes with the HSPG CD44V3-10 and fibroblast growth factor receptors.","authors":"Kristian Prydz, Roger Simm, Erna Davydova, Hans-Christian Aasheim","doi":"10.1093/glycob/cwaf020","DOIUrl":"10.1093/glycob/cwaf020","url":null,"abstract":"The ephrin family of membrane proteins mediate intracellular signalling as ligands of transmembrane Eph tyrosine kinase receptors during cell-cell interactions. Ephrin/Eph signalling regulates processes like cell migration and angiogenesis and is of particular importance during embryonic development. Ephrins-A3 and -B3 can also bind to cell surface-associated and soluble heparan sulfate proteoglycans (HSPGs) that also play important roles during early development. Here we show that ephrins-B1, -B2, and -B3 all can bind in cis to cell surface HSPGs, while only ephrin-B1 interacts with cell surface HSPGs in a way that retards HSPG endocytosis. Expressing ephrin-B1 in HEK293T cells, using polyethyleneimine (PEI) as transfection agent, increased cell surface levels of HSPGs which were detected by an anti-heparan sulfate (HS) antibody or by ephrin-B3-Fc binding. Ephrin-B1 in the plasma membrane seemed to retard PEI-induced HSPG internalisation and degradation. Binding of HSPGs by ephrin-B1 was observed for the human, mouse, xenopus, and zebrafish homologs, and did not require the cytoplasmic tail of ephrin-B1 that contains tyrosines shown to be involved in intracellular signalling. Furthermore, ephrin-B1 could bind the HSPG variant of CD44 (CD44V3-10), a complex that could further associate with fibroblast growth factor receptors (1 and 4) after co-expression with one of these receptors. In summary, our data indicate that ephrin-B1 can regulate cellular HSPG turnover and is able to form complexes of potential biological importance with CD44V3-10 and fibroblast growth factor receptors.","PeriodicalId":12766,"journal":{"name":"Glycobiology","volume":"35 6","pages":""},"PeriodicalIF":3.4,"publicationDate":"2025-04-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12036661/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143988713","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Region-specific quantitation of glycosphingolipids in the elderly human brain with Nanoflow MEA Chip Q/ToF mass spectrometry. Nanoflow MEA芯片Q/ToF质谱法定量老年人大脑中鞘糖脂的区域特异性。

IF 3.4 3区生物学

Glycobiology Pub Date : 2025-04-23 DOI: 10.1093/glycob/cwaf022

Ryan L Schindler, Lee-Way Jin, Angela M Zivkovic, Yiyun Liu, Carlito B Lebrilla

引用次数: 0