References

Click chemistry: diverse chemical function from a few good reactions

10.1002/1521-3773(20010601)40:11<2004::aid-anie2004>3.0.co;2-5 · ExternalCitation · doi-reference

A stepwise Huisgen cycloaddition process: copper(I)-catalyzed regioselective “ligation” of azides and terminal alkynes

10.1002/1521-3773(20020715)41:14<2596::aid-anie2596>3.0.co;2-4 · ExternalCitation · doi-reference

Identifying direct protein targets of poly-ADP-ribose polymerases (PARPs) using engineered PARP variants-orthogonal nicotinamide adenine dinucleotide (NAD+) analog pairs

10.1002/9780470559277.ch140259 · ExternalCitation · doi-reference

Rational design of orthogonal receptor-ligand combinations

10.1002/anie.199521291 · ExternalCitation · doi-reference

Chemistry in living cells: detection of active proteasomes by a two-step labeling strategy

10.1002/anie.200351314 · ExternalCitation · doi-reference

The Staudinger ligation—a gift to chemical biology

10.1002/anie.200401744 · ExternalCitation · doi-reference

Increasing the efficacy of bioorthogonal click reactions for bioconjugation: a comparative study

10.1002/anie.201101817 · ExternalCitation · doi-reference

A bioorthogonal reaction of N-oxide and boron reagents

10.1002/anie.201508861 · ExternalCitation · doi-reference

Artificial cysteine S-Glycosylation induced by Per-O-Acetylated unnatural monosaccharides during metabolic glycan labeling

10.1002/anie.201711710 · ExternalCitation · doi-reference

Enzymatic or in vivo installation of propargyl groups in combination with click chemistry for the enrichment and detection of methyltransferase target sites in RNA

10.1002/anie.201800188 · ExternalCitation · doi-reference

Next-generation metabolic glycosylation reporters enable detection of protein O−GlcNAcylation in living cells without S-Glyco modification

10.1002/anie.202320247 · ExternalCitation · doi-reference

Metabolic chemical reporters of glycans exhibit cell-type-selective metabolism and glycoprotein labeling

10.1002/cbic.201700020 · ExternalCitation · doi-reference

Highly efficient synthesis of UDP-GalNAc/GlcNAc analogues with promiscuous recombinant human UDP-GalNAc pyrophosphorylase AGX1

10.1002/chem.201002315 · ExternalCitation · doi-reference

Photocrosslinking O-GlcNAcylated proteins to neighboring biomolecules

10.1002/cpz1.201 · ExternalCitation · doi-reference

Chemoenzymatic synthesis and purification of bioorthogonally tagged UDP-GlcNAc and UDP-GalNAc analogues

10.1002/cpz1.70277 · ExternalCitation · doi-reference

Synthesis of N-Acyl-2-amino-2-deoxy-[1-14C]-glucoses as precursors for the biosynthesis of novel N-acylneuraminic acids

10.1002/jlcr.2580310910 · ExternalCitation · doi-reference

The never-ending story of peptide O-xylosyltransferase

10.1007/s00018-003-3278-2 · ExternalCitation · doi-reference

Aberrant N-glycosylation in cancer: MGAT5 and β1,6-GlcNAc branched N-glycans as critical regulators of tumor development and progression

10.1007/s13402-023-00770-4 · ExternalCitation · doi-reference

Click-triggered bioorthogonal bond-cleavage reactions

10.1007/s41061-025-00492-1 · ExternalCitation · doi-reference

Incorporation of N-acyl-2-amino-2-deoxy-hexoses into glycosphingolipids of the pheochromocytoma cell line PC 12

10.1016/0014-5793(92)81233-c · ExternalCitation · doi-reference

In vivo modulated N-acyl side chain of N-acetylneuraminic acid modulates the cell contact-dependent inhibition of growth

10.1016/0014-5793(96)01029-0 · ExternalCitation · doi-reference

In vivo and in vitro function of human UDP-galactose 4′-epimerase variants

10.1016/j.biochi.2011.06.009 · ExternalCitation · doi-reference

Substrate specificity of N-acetylhexosamine kinase towards N-acetylgalactosamine derivatives

10.1016/j.bmcl.2009.07.104 · ExternalCitation · doi-reference

Strain-promoted cycloadditions involving nitrones and alkynes-rapid tunable reactions for bioorthogonal labeling

10.1016/j.cbpa.2014.05.023 · ExternalCitation · doi-reference

Recent advances in photoaffinity labeling strategies to capture glycan-protein interactions

10.1016/j.cbpa.2024.102456 · ExternalCitation · doi-reference

Click chemistry in proteomic investigations

10.1016/j.cell.2020.01.025 · ExternalCitation · doi-reference

Deconvoluting the functions of polypeptide N-alpha-acetylgalactosaminyltransferase family members by glycopeptide substrate profiling

10.1016/j.chembiol.2004.05.009 · ExternalCitation · doi-reference

A photo-cross-linking GlcNAc analog enables covalent capture of N-linked glycoprotein-binding partners on the cell surface

10.1016/j.chembiol.2021.07.007 · ExternalCitation · doi-reference

Cell-selective bioorthogonal labeling

10.1016/j.chembiol.2023.09.010 · ExternalCitation · doi-reference

Loss of function of GALNT2 lowers high-density lipoproteins in humans, nonhuman primates, and rodents

10.1016/j.cmet.2016.07.012 · ExternalCitation · doi-reference

Genetic glycoengineering in mammalian cells

10.1016/j.jbc.2021.100448 · ExternalCitation · doi-reference

In vivo mapping of the mouse Galnt3-specific O-glycoproteome

10.1016/j.jbc.2024.107628 · ExternalCitation · doi-reference

Structural basis of carbohydrate transfer activity by human UDP-GalNAc: polypeptide α-N-acetylgalactosaminyltransferase (pp-GalNAc-T10)

10.1016/j.jmb.2006.03.061 · ExternalCitation · doi-reference

Bump-and-hole engineering identifies specific substrates of glycosyltransferases in living cells

10.1016/j.molcel.2020.03.030 · ExternalCitation · doi-reference

Co-purification and characterization of UDP-glucose 4-epimerase and UDP-N-acetylglucosamine 4-epimerase from porcine submaxillary glands

10.1016/s0021-9258(17)44524-8 · ExternalCitation · doi-reference

Human UDP-galactose-epimerase (GALE) is required for cell-surface glycome structure and function

10.1016/s0021-9258(17)49882-6 · ExternalCitation · doi-reference

Biosynthesis of a nonphysiological sialic acid in different rat organs, using N-propanoyl-D-hexosamines as precursors

10.1016/s0021-9258(18)41874-1 · ExternalCitation · doi-reference

Control of glycoprotein synthesis. Purification and characterization of rabbit liver UDP-N-acetylglucosamine:alpha-3-D-mannoside beta-1,2-N-acetylglucosaminyltransferase I

10.1016/s0021-9258(18)68473-x · ExternalCitation · doi-reference

Constructing azide-labeled cell surfaces using polysaccharide biosynthetic pathways

10.1016/s0076-6879(03)01018-8 · ExternalCitation · doi-reference

Chapter 2 protein engineering with the traceless Staudinger ligation

10.1016/s0076-6879(09)62002-4 · ExternalCitation · doi-reference

Brain-specific expression of a novel human UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase (GalNAc-T9)1

10.1016/s0167-4781(00)00180-9 · ExternalCitation · doi-reference

Cloning and characterization of complementary DNA encoding human N-acetylglucosamine-phosphate mutase protein

10.1016/s0378-1119(99)00543-0 · ExternalCitation · doi-reference

Design of allele-specific inhibitors to probe protein kinase signaling

10.1016/s0960-9822(98)70198-8 · ExternalCitation · doi-reference

Photoclick chemistry: a bright idea

10.1021/acs.chemrev.0c01212 · ExternalCitation · doi-reference

Azido groups hamper glycan acceptance by carbohydrate processing enzymes

10.1021/acscentsci.1c01172 · ExternalCitation · doi-reference

Mass spectrometric method for the unambiguous profiling of cellular dynamic glycosylation

10.1021/acschembio.0c00453 · ExternalCitation · doi-reference

Optimization of metabolic oligosaccharide engineering with Ac4GalNAlk and Ac4GlcNAlk by an engineered pyrophosphorylase

10.1021/acschembio.1c00034 · ExternalCitation · doi-reference

Mucinomics as the next frontier of mass spectrometry

10.1021/acschembio.1c00384 · ExternalCitation · doi-reference

4-Deoxy-4-fluoro-GalNAz (4FGalNAz) is a metabolic chemical reporter of O-GlcNAc modifications, highlighting the notable substrate flexibility of O-GlcNAc transferase

10.1021/acschembio.1c00818 · ExternalCitation · doi-reference

Substrate specificity of the sialic acid biosynthetic pathway

10.1021/bi010862s · ExternalCitation · doi-reference

Metabolic functionalization of recombinant glycoproteins

10.1021/bi049274f · ExternalCitation · doi-reference

Evaluation of analogues of GalNAc as substrates for enzymes of the mammalian GalNAc salvage pathway

10.1021/cb200511t · ExternalCitation · doi-reference

A chemoenzymatic approach toward the rapid and sensitive detection of O-GlcNAc posttranslational modifications

10.1021/ja038545r · ExternalCitation · doi-reference

A strain-promoted [3 + 2] azide−alkyne cycloaddition for covalent modification of biomolecules in living systems

10.1021/ja044996f · ExternalCitation · doi-reference

Biocompatible copper(I) catalysts for in vivo imaging of glycans

10.1021/ja106553e · ExternalCitation · doi-reference

Second-generation difluorinated cyclooctynes for copper-free click chemistry

10.1021/ja803086r · ExternalCitation · doi-reference

Tetrazine ligation: fast bioconjugation based on inverse-electron-demand Diels–Alder reactivity

10.1021/ja8053805 · ExternalCitation · doi-reference

Protein S-Glyco-modification through an elimination-addition mechanism

10.1021/jacs.0c02110 · ExternalCitation · doi-reference

A bioorthogonal precision tool for human N-acetylglucosaminyltransferase V

10.1021/jacs.4c05955 · ExternalCitation · doi-reference

Not so bioorthogonal chemistry

10.1021/jacs.4c15986 · ExternalCitation · doi-reference

Iterative bump-and-hole engineering creates a bioorthogonal reporter for N -acetylglucosaminyltransferase I

10.1021/jacs.6c01114 · ExternalCitation · doi-reference

Engineering orthogonal polypeptide GalNAc-transferase and UDP-sugar pairs

10.1021/jacs.9b04695 · ExternalCitation · doi-reference

Glycosaminoglycans: what remains to be deciphered?

10.1021/jacsau.2c00569 · ExternalCitation · doi-reference

Benefits of chemical sugar modifications introduced by click chemistry for glycoproteomic analyses

10.1021/jasms.1c00084 · ExternalCitation · doi-reference

Peptidotriazoles on solid phase: [1,2,3]-triazoles by regiospecific copper(I)-catalyzed 1,3-dipolar cycloadditions of terminal alkynes to azides

10.1021/jo011148j · ExternalCitation · doi-reference

A chemical switch for inhibitor-sensitive alleles of any protein kinase

10.1038/35030148 · ExternalCitation · doi-reference

Chemical remodelling of cell surfaces in living animals

10.1038/nature02791 · ExternalCitation · doi-reference

Mining the O-glycoproteome using zinc-finger nuclease-glycoengineered SimpleCell lines

10.1038/nmeth.1731 · ExternalCitation · doi-reference

Isotope-targeted glycoproteomics (IsoTaG): a mass-independent platform for intact N- and O-glycopeptide discovery and analysis

10.1038/nmeth.3366 · ExternalCitation · doi-reference

Cell-specific bioorthogonal tagging of glycoproteins

10.1038/s41467-022-33854-0 · ExternalCitation · doi-reference

Developing bioorthogonal probes to span a spectrum of reactivities

10.1038/s41570-020-0205-0 · ExternalCitation · doi-reference

N-glycan-dependent protein maturation and quality control in the ER

10.1038/s41580-025-00855-y · ExternalCitation · doi-reference

A palmitoyl transferase chemical-genetic system to map ZDHHC-specific S-acylation

10.1038/s41587-023-02030-0 · ExternalCitation · doi-reference

Targeted delivery of nitric oxide via a ‘bump-and-hole’-based enzyme-prodrug pair

10.1038/s41589-018-0190-5 · ExternalCitation · doi-reference

Molecular basis for fibroblast growth factor 23 O-glycosylation by GalNAc-T3

10.1038/s41589-019-0444-x · ExternalCitation · doi-reference

Cell-type-specific labeling and profiling of glycans in living mice

10.1038/s41589-022-01016-4 · ExternalCitation · doi-reference

Selective bioorthogonal probe for N-glycan hybrid structures

10.1038/s41589-024-01756-5 · ExternalCitation · doi-reference

Xylosyltransferase engineering to manipulate proteoglycans in mammalian cells

10.1038/s41589-025-02113-w · ExternalCitation · doi-reference

A chemoenzymatic route to N-acetylglucosamine-1-phosphate analogues: substrate specificity investigations of N-acetylhexosamine 1-kinase

10.1039/b904853g · ExternalCitation · doi-reference

Bioconjugation via azide-Staudinger ligation: An overview

10.1039/c0cs00123f · ExternalCitation · doi-reference

Inverse electron demand Diels–Alder reactions in chemical biology

10.1039/c7cs00184c · ExternalCitation · doi-reference

Nucleoside-modified AdoMet analogues for differential methyltransferase targeting

10.1039/c9cc07807j · ExternalCitation · doi-reference

The reaction mechanism of the azide-alkyne Huisgen cycloaddition

10.1039/c9cp02386k · ExternalCitation · doi-reference

Exploration of human xylosyltransferase for chemoenzymatic synthesis of proteoglycan linkage region

10.1039/d1ob00317h · ExternalCitation · doi-reference

Metabolic glycoengineering—exploring glycosylation with bioorthogonal chemistry

10.1039/d2cs00764a · ExternalCitation · doi-reference

Expanding the repertoire of GalNAc analogues for cell-specific bioorthogonal tagging of glycoproteins

10.1039/d4cb00093e · ExternalCitation · doi-reference

O-linked mucin-type glycosylation in breast cancer

10.1042/bst20170483 · ExternalCitation · doi-reference

Molecular cloning and characterization of murine and human N-acetylglucosamine kinase

10.1046/j.1432-1327.2000.01360.x · ExternalCitation · doi-reference

The beginnings of mucin biosynthesis: the crystal structure of UDP-GalNAc:polypeptide-N-acetylgalactosaminyltransferase-T1

10.1073/pnas.0405657101 · ExternalCitation · doi-reference

Alkynyl sugar analogs for the labeling and visualization of glycoconjugates in cells

10.1073/pnas.0611307104 · ExternalCitation · doi-reference

Copper-free click chemistry for dynamic in vivo imaging

10.1073/pnas.0707090104 · ExternalCitation · doi-reference

Copper-free click chemistry in living animals

10.1073/pnas.0911116107 · ExternalCitation · doi-reference

Metabolic cross-talk allows labeling of O-linked beta-N-acetylglucosamine-modified proteins via the N-acetylgalactosamine salvage pathway

10.1073/pnas.1010045108 · ExternalCitation · doi-reference

Chemical reporters for fluorescent detection and identification of O-GlcNAc-modified proteins reveal glycosylation of the ubiquitin ligase NEDD4-1

10.1073/pnas.1102458108 · ExternalCitation · doi-reference

Metabolic labeling enables selective photocrosslinking of O-GlcNAc-modified proteins to their binding partners

10.1073/pnas.1114356109 · ExternalCitation · doi-reference

A chemical approach for identifying O-GlcNAc-modified proteins in cells

10.1073/pnas.1632821100 · ExternalCitation · doi-reference

The mucin-selective protease StcE enables molecular and functional analysis of human cancer-associated mucins

10.1073/pnas.1813020116 · ExternalCitation · doi-reference

Metabolic precision labeling enables selective probing of O-linked N-acetylgalactosamine glycosylation

10.1073/pnas.2007297117 · ExternalCitation · doi-reference

An enzymatic toolkit for selective proteolysis, detection, and visualization of mucin-domain glycoproteins

10.1073/pnas.2012196117 · ExternalCitation · doi-reference

Quantitative mapping of the in vivo O-GalNAc glycoproteome in mouse tissues identifies GalNAc-T2 O-glycosites in metabolic disorder

10.1073/pnas.2303703120 · ExternalCitation · doi-reference

A metabolic labeling approach toward proteomic analysis of mucin-type O-linked glycosylation

10.1073/pnas.2335201100 · ExternalCitation · doi-reference

A unique molecular chaperone Cosmc required for activity of the mammalian core 1 3-galactosyltransferase

10.1073/pnas.262438199 · ExternalCitation · doi-reference

Disaccharide uptake and priming in animal cells: inhibition of sialyl Lewis X by acetylated Gal beta 1-GlcNAc beta-O-naphthalenemethanol

10.1073/pnas.92.8.3323 · ExternalCitation · doi-reference

Biosynthetic modulation of sialic acid-dependent virus-receptor interactions of two primate polyoma viruses (∗)

10.1074/jbc.270.3.1308 · ExternalCitation · doi-reference

The eukaryotic UDP-N-acetylglucosamine pyrophosphorylases: GENE CLONING, PROTEIN EXPRESSION, AND CATALYTIC MECHANISM*

10.1074/jbc.273.23.14392 · ExternalCitation · doi-reference

A 17-amino acid insert changes UDP-N-acetylhexosamine pyrophosphorylase specificity from UDP-GalNAc to UDP-GlcNAc

10.1074/jbc.273.42.27055 · ExternalCitation · doi-reference

Metabolic delivery of ketone groups to sialic acid residues. Application to cell surface glycoform engineering

10.1074/jbc.273.47.31168 · ExternalCitation · doi-reference

Identification and characterization of the human xylosyltransferase I gene promoter region

10.1074/jbc.m109.016592 · ExternalCitation · doi-reference

Dynamic association between the catalytic and lectin domains of human UDP-GalNAc:Polypeptide α-N-acetylgalactosaminyltransferase-2*

10.1074/jbc.m513590200 · ExternalCitation · doi-reference

Identification of common and unique peptide substrate preferences for the UDP-GalNAc:polypeptide α-N-acetylgalactosaminyltransferases T1 and T2 derived from oriented random peptide substrates

10.1074/jbc.m605149200 · ExternalCitation · doi-reference

Probing the contribution of individual polypeptide GalNAc-transferase isoforms to the O-glycoproteome by inducible expression in isogenic cell lines

10.1074/jbc.ra118.004516 · ExternalCitation · doi-reference

Exploring regulation of protein O-glycosylation in isogenic human HEK293 cells by differential O-glycoproteomics

10.1074/mcp.ra118.001121 · ExternalCitation · doi-reference

Biosynthetic incorporation of unnatural sialic acids into polysialic acid on neural cells

10.1093/glycob/10.10.1049 · ExternalCitation · doi-reference

Biochemical engineering of the N-acyl side chain of sialic acid: biological implications

10.1093/glycob/11.2.11r · ExternalCitation · doi-reference

Dynamic expression of mucins and the genes controlling mucin-type O-glycosylation within the mouse respiratory system

10.1093/glycob/cwad031 · ExternalCitation · doi-reference

Decoding the complex substrate specificities of GalNAc-Ts

10.1093/glycob/cwaf073 · ExternalCitation · doi-reference

All in the family: the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases

10.1093/glycob/cwg007 · ExternalCitation · doi-reference

Control of mucin-type O-glycosylation: a classification of the polypeptide GalNAc-transferase gene family

10.1093/glycob/cwr182 · ExternalCitation · doi-reference

UDP-N-acetyl α-d-galactosamine: polypeptide N-acetylgalactosaminyltransferases: completion of the family tree

10.1093/glycob/cwr183 · ExternalCitation · doi-reference

Regulation of N-glycosylation efficiency by eukaryotic oligosaccharyltransferase

10.1101/2025.09.06.674603 · ExternalCitation · doi-reference

Time-resolved tracking and secretome mapping of intracellular, cell surface, and extracellular glycoconjugates with a mini-tetrazine N-acetylglucosamine

10.1101/2025.10.16.682811 · ExternalCitation · doi-reference

Metabolic glycoengineering through the mammalian GalNAc salvage pathway

10.1111/j.1742-4658.2011.08448.x · ExternalCitation · doi-reference

In vivo imaging of membrane-associated glycans in developing zebrafish

10.1126/science.1155106 · ExternalCitation · doi-reference

Engineering chemical reactivity on cell surfaces through oligosaccharide biosynthesis

10.1126/science.276.5315.1125 · ExternalCitation · doi-reference

Cell surface engineering by a modified Staudinger reaction

10.1126/science.287.5460.2007 · ExternalCitation · doi-reference

Chinese hamster ovary cell mutants with multiple glycosylation defects for production of glycoproteins with minimal carbohydrate heterogeneity

10.1128/mcb.9.2.377-383.1989 · ExternalCitation · doi-reference

Glycan labeling and analysis in cells and in vivo

10.1146/annurev-anchem-091620-091314 · ExternalCitation · doi-reference

UDP-galactose 4′ epimerase (GALE) is essential for development of Drosophila melanogaster

10.1242/dmm.005058 · ExternalCitation · doi-reference

HEK293T cell lines defective for O-linked glycosylation

10.1371/journal.pone.0179949 · ExternalCitation · doi-reference

Deconstruction of O-glycosylation-GalNAc-T isoforms direct distinct subsets of the O-glycoproteome

10.15252/embr.201540796 · ExternalCitation · doi-reference

Understanding bio-orthogonal strain-driven sydnone cycloadditions: data-assisted profiles and the search for linear relationships

10.3390/molecules30132770 · ExternalCitation · doi-reference

Expanding the scope of cyclopropene reporters for the detection of metabolically engineered glycoproteins by Diels–Alder reactions

10.3762/bjoc.10.232 · ExternalCitation · doi-reference