Research graph
References from In vitro enzymatic synthesis of long-acting therapeutic proteins and peptides. Local targets link to admitted publications; unresolved targets remain external evidence.
Trends in peptide drug discovery
10.1038/s41573-020-00135-8 · 2021 · External reference
Anti-obesity drug discovery: advances and challenges
10.1038/s41573-021-00337-8 · 2022 · External reference
Peptide-based vaccines: current Progress and future challenges
10.1021/acs.chemrev.9b00472 · 2020 · External reference
Protein engineering strategies for improved pharmacokinetics
10.1002/adfm.202101633 · 2021 · External reference
Derivatization with fatty acids in peptide and protein drug discovery
10.1038/s41573-022-00529-w · 2023 · External reference
Adherence to and persistence with antidiabetic medications and associations with clinical and economic outcomes in people with type 2 diabetes mellitus: a systematic literature review
10.1111/dom.14603 · 2022 · External reference
A comprehensive review on current advances in peptide drug development and design
10.3390/ijms20102383 · 2019 · External reference
Recent advances in glycopeptide and glycoprotein synthesis: a refined synthetic probe towards the biological world
10.1002/cjoc.202300035 · 2023 · External reference
Patient perceptions of and preferences between characteristics of injectable diabetes treatments
10.1007/s13300-021-01097-9 · 2021 · External reference
Molecular engineering of insulin Icodec, the first acylated insulin Analog for once-weekly Administration in Humans
10.1021/acs.jmedchem.1c00257 · 2021 · External reference
Approved delivery strategies for biopharmaceuticals
10.1016/j.cclet.2024.110225 · 2025 · External reference
Recent progress in enzymatic protein labelling techniques and their applications
10.1039/c8cs00537k · 2018 · External reference
Post-translational modifications of the protein termini
2021 · External reference
10.1093/abt/tbaf010
10.1093/abt/tbaf010 · External reference
Glycosylation shapes the efficacy and safety of diverse protein, gene and cell therapies
10.1016/j.biotechadv.2023.108206 · 2023 · External reference
Chemical (neo)glycosylation of biological drugs
10.1016/j.addr.2021.01.021 · 2021 · External reference
Glycosylation engineering of therapeutic IgG antibodies: challenges for the safety, functionality and efficacy
10.1007/s13238-017-0433-3 · 2017 · External reference
Sialylation as an important regulator of antibody function
10.3389/fimmu.2022.818736 · 2022 · External reference
Decoding the complex substrate specificities of GalNAc-Ts
10.1093/glycob/cwaf073 · 2025 · External reference
An atlas of O-linked glycosylation on peptide hormones reveals diverse biological roles
10.1038/s41467-020-17473-1 · 2020 · External reference
Integrated chemoenzymatic approach to streamline the assembly of complex glycopeptides in the liquid phase
10.1021/jacs.2c01819 · 2022 · External reference
Single-pot enzymatic synthesis of cancer-associated MUC16 O-glycopeptide libraries and multivalent protein glycoconjugates: a step towards cancer glycovaccines
10.1039/d0nj06021f · 2021 · External reference
N-glycosylation of monoclonal antibody therapeutics: a comprehensive review on significance and characterization
10.1016/j.aca.2022.339828 · 2022 · External reference
Chemoenzymatic synthesis of glycoengineered IgG antibodies and glycosite-specific antibody–drug conjugates
10.1038/nprot.2017.058 · 2017 · External reference
Cell-based glycoengineering for production of homogeneous and specific glycoform-enriched antibodies with improved effector functions
10.1073/pnas.2423853122 · 2025 · External reference
RNA-binding proteins and glycoRNAs form domains on the cell surface for cell-penetrating peptide entry
10.1016/j.cell.2025.01.040 · 2025 · External reference
Albumin-based drug designs for pharmacokinetic modulation
10.1080/17425255.2020.1801633 · 2020 · External reference
Half-life extension of single-domain antibody–drug conjugates by albumin binding moiety enhances antitumor efficacy
10.1002/mco2.557 · 2020 · External reference
Extending the half-life of a protein in vivo by enzymatic Labeling with amphiphilic lipopeptides
10.1021/acs.bioconjchem.1c00027 · 2021 · External reference
Discovery of the once-weekly glucagon-like Peptide-1 (GLP-1) analogue Semaglutide
10.1021/acs.jmedchem.5b00726 · 2015 · External reference
2FA-platform generates dual fatty acid-conjugated GLP-1 receptor agonist TE-8105 with enhanced diabetes, obesity, and NASH efficacy compared to Semaglutide
10.1021/acs.jmedchem.4c02153 · 2025 · External reference
Design, synthesis, and biological evaluation of long-acting glucagon-like peptide-1 (GLP-1) conjugates modified with dual fatty acids and a proline-alanine-serine (PAS) polypeptide
10.1016/j.bmc.2025.118266 · 2025 · External reference
Inhibition of human N myristoyltransferase 1 as a strategy to suppress cancer progression driven by myristoylation
10.1038/s41598-025-13529-8 · 2025 · External reference
Phytochemical profiling and in silico evaluation of Artemisia absinthium compounds targeting leishmania N-myristoyltransferase: molecular docking, drug-likeness, and toxicity analyses
10.3389/fchem.2024.1508603 · 2024 · External reference
GFP Farnesylation as a suitable strategy for selectively tagging exosomes
10.1021/acsabm.4c01112 · 2024 · External reference
Engineering biomimetic Trogocytosis with Farnesylated chemically self-assembled Nanorings
10.1021/acs.biomac.2c00837 · 2022 · External reference
Extracellular carriers control lipid-dependent secretion, delivery, and activity of WNT morphogens
10.1016/j.devcel.2023.11.027 · 2024 · External reference
Unresolved reference
2024 · External reference
Advances in drug delivery systems based on red blood cells and their membrane-derived nanoparticles
10.1021/acsnano.2c11965 · 2023 · External reference
Engineering protein farnesyltransferase for enzymatic protein Labeling applications
10.1021/bc500240p · 2014 · External reference
Engineering protein prenylation: an emerging tool for selective protein modification
10.1042/bst20253076 · 2025 · External reference
PEGylation in pharmaceutical development: current status and emerging trends in macromolecular and immunotherapeutic drugs
2024 · External reference
Polyethylene glycol immunogenicity: theoretical, clinical, and practical aspects of anti-polyethylene glycol antibodies
10.1021/acsnano.1c05922 · 2021 · External reference
Enzyme-mediated ligation technologies for peptides and proteins
10.1016/j.cbpa.2017.01.017 · 2017 · External reference
Enzymatic procedure for site-specific pegylation of proteins
10.1016/s0169-409x(02)00024-8 · 2002 · External reference
Chaperonin co-expression and chemical modification enables production of active microbial transglutaminase from E. Coli cytoplasm
10.1016/j.ijbiomac.2023.127355 · 2023 · External reference
Improving the therapeutic potential of G-CSF through compact circular PEGylation based on orthogonal conjugations
10.1021/acs.biomac.3c00543 · 2023 · External reference
Site-specific PEGylation of proteins: insights into structural and functional changes
10.1016/j.apsb.2025.10.014 · 2025 · External reference
Antibody and antibody fragments site-specific conjugation using new Q-tag substrate of bacterial transglutaminase
10.1038/s41420-024-01845-3 · 2024 · External reference
Design and study of PEG linkers that enable robust characterization of PEGylated proteins
10.1021/acsptsci.1c00112 · 2021 · External reference
Site-specific Glyco-tagging of native proteins for the development of biologicals
10.1021/jacs.4c11091 · 2024 · External reference
PEGylation technology: addressing concerns, moving forward
10.1080/10717544.2025.2494775 · 2025 · External reference
Site-selective enzymatic Labeling of designed ankyrin repeat proteins using protein farnesyltransferase
2019 · External reference
MALDI-MS analysis of peptide libraries expands the scope of substrates for farnesyltransferase
10.3390/ijms222112042 · 2021 · External reference
Protein farnesyltransferase Catalyzes unanticipated Farnesylation and geranylgeranylation of shortened target sequences
10.1021/acs.biochem.0c00081 · 2020 · External reference
Versatile peptide macrocyclization with Diels–Alder cycloadditions
10.1021/jacs.9b07578 · 2019 · External reference
Cyclic peptides: backbone rigidification and capability of mimicking motifs at protein–protein interfaces
10.1039/d0cp04633g · 2021 · External reference
Head-to-tail cyclization after interaction with trypsin: a scorpion venom peptide that resembles plant cyclotides
10.1021/acs.jmedchem.0c00686 · 2020 · External reference
10.2147/ijn.s487303
10.2147/ijn.s487303 · External reference
Characterization and application of natural and recombinant butelase-1 to improve industrial enzymes by end-to-end circularization
10.1039/d1ra03763c · 2021 · External reference
Sortase A-catalyzed peptide cyclization for the synthesis of macrocyclic peptides and glycopeptides
10.1039/c1cc13322e · 2011 · External reference
Enzymatic on-resin peptide cleavage and in situ cyclization one-pot strategy for the synthesis of cyclopeptide and cyclotide
10.1021/acs.joc.8b02032 · 2018 · External reference
Empowering site-specific bioconjugations in vitro and in vivo: advances in Sortase engineering and Sortase-mediated ligation
10.1002/anie.202310910 · 2024 · External reference
Cyclizing disulfide-rich peptides using Sortase a
2019 · External reference
Employing unnatural promiscuity of sortase to construct peptide macrocycle libraries for ligand discovery
10.1039/d4sc01992j · 2024 · External reference
Challenges in the use of sortase and other peptide ligases for site-specific protein modification
10.1039/d0cs01148g · 2022 · External reference
Improving Sortase-A-mediated transpeptidation reactions by electrostatically assisted capture
10.1021/acs.orglett.5c03718 · 2025 · External reference
Combined application of orthogonal Sortases and Depsipeptide substrates for dual protein Labeling
10.1021/acs.bioconjchem.2c00411 · 2022 · External reference
Phage display of Graspeptides via SrtA-mediated peptide ligation and cyclization
10.1021/acs.orglett.5c03982 · 2025 · External reference
Hepta-mutant Staphylococcus aureus Sortase a (SrtA7m) as a tool for in vivo protein Labeling in Caenorhabditis elegans
10.1021/acschembio.6b00998 · 2017 · External reference
Chapter four - AEP-mediated backbone cyclization of cyclotides—A chemoenzymatic method for cyclotide production
2025 · External reference
“Top-down” overexpression optimization of butelase-1 in Escherichia coli and its application in anti-tumor peptides
10.1016/j.ijbiomac.2024.133933 · 2024 · External reference
Characterization and application of natural and recombinant butelase-1 to improve industrial enzymes by end-to-end circularization
10.1039/d1ra03763c · 2021 · External reference
Butelase 1: a versatile ligase for peptide and protein macrocyclization
10.1021/jacs.5b11014 · 2015 · External reference
An efficient and easily obtainable butelase variant for chemoenzymatic ligation and modification of peptides and proteins
10.1186/s12934-024-02598-5 · 2024 · External reference
Consensus design and engineering of an efficient and high-yield peptide asparaginyl ligase for protein cyclization and ligation
10.1016/j.jbc.2023.102997 · 2023 · External reference
Engineering a catalytically efficient recombinant protein ligase
10.1021/jacs.6b12637 · 2017 · External reference
Design of a recombinant asparaginyl ligase for site-specific modification using efficient recognition and nucleophile motifs
10.1038/s42004-024-01173-8 · 2024 · External reference
Chapter fifteen - preparing recombinant “Split AEP” for protein labeling
2023 · External reference
A suite of kinetically superior AEP ligases can cyclise an intrinsically disordered protein
10.1038/s41598-019-47273-7 · 2019 · External reference
Plant asparaginyl endopeptidases and their structural determinants of function
10.1042/bst20200908 · 2021 · External reference
Vypal2: a versatile peptide ligase for precision tailoring of proteins
10.3390/ijms23010458 · 2022 · External reference
Mapping proteolytic neo-N termini at the surface of living cells
10.1073/pnas.2018809118 · 2021 · External reference
Peptiligase, an enzyme for efficient chemoenzymatic peptide synthesis and cyclization in water
10.1002/adsc.201600017 · 2016 · External reference
From thiol-subtilisin to omniligase: design and structure of a broadly applicable peptide ligase
10.1016/j.csbj.2021.02.002 · 2021 · External reference
Employing broad substrate specificity of Omniligase to generate phage-encoded bicyclic peptide libraries for ligand discovery
10.1021/acs.orglett.5c01205 · 2025 · External reference
The inducible Intein-mediated self-cleaving tag (IIST) system: a novel purification and Amidation system for peptides and proteins
10.3390/molecules26195948 · 2021 · External reference
Native chemical ligation and extended methods: mechanisms, catalysis, scope, and limitations
10.1021/acs.chemrev.8b00712 · 2019 · External reference
Enzymatic Macrolactamization of mRNA display libraries for inhibitor selection
10.1021/acschembio.2c00828 · 2023 · External reference
Microbial transglutaminase for biotechnological and biomedical engineering
10.1515/hsz-2018-0335 · 2019 · External reference
Engineering of a biologically active glycosylated glucagon-like Peptide-1 analogue
10.1021/acs.jmedchem.4c00093 · 2024 · External reference
Enzymatic properties of recombinant ligase Butelase-1 and its application in cyclizing food-derived angiotensin I-converting enzyme inhibitory peptides
10.1021/acs.jafc.1c01755 · 2021 · External reference
Protein design using structure-prediction networks: AlphaFold and RoseTTAFold as protein structure foundation models
10.1101/cshperspect.a041472 · 2024 · External reference
Combining machine learning with structure-based protein design to predict and engineer post-translational modifications of proteins
10.1371/journal.pcbi.1011939 · 2024 · External reference
Role of machine and deep learning in predicting protein modification sites: review and future directions
2025 · External reference
De novo design of protein structure and function with RFdiffusion
10.1038/s41586-023-06415-8 · 2023 · External reference
De novo design of luciferases using deep learning
10.1038/s41586-023-05696-3 · 2023 · External reference
Engineering orthogonal polypeptide GalNAc-transferase and UDP-sugar pairs
10.1021/jacs.9b04695 · 2019 · External reference
Genetic code expansion: recent developments and emerging applications
10.1021/acs.chemrev.4c00216 · 2025 · External reference
Systems and methods for continuous evolution of enzymes
2024 · External reference
Artificial lipidation of antifungal proteins and antifungal behavior: a case study with Cholesterylation
10.1002/cbic.202401081 · 2025 · External reference
An overview of turoctocog alfa pegol (N8-GP; ESPEROCT®) assay performance: implications for postadministration monitoring
10.1111/hae.13897 · 2020 · External reference
OaAEP1-mediated ligation of Mirror-image peptides via acyl donor substrate engineering
10.1021/jacs.6c00057 · 2026 · External reference
Protein engineering strategies for improved pharmacokinetics
10.1002/adfm.202101633 · ExternalCitation · doi-reference
Peptiligase, an enzyme for efficient chemoenzymatic peptide synthesis and cyclization in water
10.1002/adsc.201600017 · ExternalCitation · doi-reference
Empowering site-specific bioconjugations in vitro and in vivo: advances in Sortase engineering and Sortase-mediated ligation
10.1002/anie.202310910 · ExternalCitation · doi-reference
Artificial lipidation of antifungal proteins and antifungal behavior: a case study with Cholesterylation
10.1002/cbic.202401081 · ExternalCitation · doi-reference
Recent advances in glycopeptide and glycoprotein synthesis: a refined synthetic probe towards the biological world
10.1002/cjoc.202300035 · ExternalCitation · doi-reference
Half-life extension of single-domain antibody–drug conjugates by albumin binding moiety enhances antitumor efficacy
10.1002/mco2.557 · ExternalCitation · doi-reference
Glycosylation engineering of therapeutic IgG antibodies: challenges for the safety, functionality and efficacy
10.1007/s13238-017-0433-3 · ExternalCitation · doi-reference
Patient perceptions of and preferences between characteristics of injectable diabetes treatments
10.1007/s13300-021-01097-9 · ExternalCitation · doi-reference
N-glycosylation of monoclonal antibody therapeutics: a comprehensive review on significance and characterization
10.1016/j.aca.2022.339828 · ExternalCitation · doi-reference
Chemical (neo)glycosylation of biological drugs
10.1016/j.addr.2021.01.021 · ExternalCitation · doi-reference
Site-specific PEGylation of proteins: insights into structural and functional changes
10.1016/j.apsb.2025.10.014 · ExternalCitation · doi-reference
Glycosylation shapes the efficacy and safety of diverse protein, gene and cell therapies
10.1016/j.biotechadv.2023.108206 · ExternalCitation · doi-reference
Design, synthesis, and biological evaluation of long-acting glucagon-like peptide-1 (GLP-1) conjugates modified with dual fatty acids and a proline-alanine-serine (PAS) polypeptide
10.1016/j.bmc.2025.118266 · ExternalCitation · doi-reference
Enzyme-mediated ligation technologies for peptides and proteins
10.1016/j.cbpa.2017.01.017 · ExternalCitation · doi-reference
Approved delivery strategies for biopharmaceuticals
10.1016/j.cclet.2024.110225 · ExternalCitation · doi-reference
RNA-binding proteins and glycoRNAs form domains on the cell surface for cell-penetrating peptide entry
10.1016/j.cell.2025.01.040 · ExternalCitation · doi-reference
From thiol-subtilisin to omniligase: design and structure of a broadly applicable peptide ligase
10.1016/j.csbj.2021.02.002 · ExternalCitation · doi-reference
Extracellular carriers control lipid-dependent secretion, delivery, and activity of WNT morphogens
10.1016/j.devcel.2023.11.027 · ExternalCitation · doi-reference
Chaperonin co-expression and chemical modification enables production of active microbial transglutaminase from E. Coli cytoplasm
10.1016/j.ijbiomac.2023.127355 · ExternalCitation · doi-reference
“Top-down” overexpression optimization of butelase-1 in Escherichia coli and its application in anti-tumor peptides
10.1016/j.ijbiomac.2024.133933 · ExternalCitation · doi-reference
Consensus design and engineering of an efficient and high-yield peptide asparaginyl ligase for protein cyclization and ligation
10.1016/j.jbc.2023.102997 · ExternalCitation · doi-reference
Enzymatic procedure for site-specific pegylation of proteins
10.1016/s0169-409x(02)00024-8 · ExternalCitation · doi-reference
Protein farnesyltransferase Catalyzes unanticipated Farnesylation and geranylgeranylation of shortened target sequences
10.1021/acs.biochem.0c00081 · ExternalCitation · doi-reference
Extending the half-life of a protein in vivo by enzymatic Labeling with amphiphilic lipopeptides
10.1021/acs.bioconjchem.1c00027 · ExternalCitation · doi-reference
Combined application of orthogonal Sortases and Depsipeptide substrates for dual protein Labeling
10.1021/acs.bioconjchem.2c00411 · ExternalCitation · doi-reference
Engineering biomimetic Trogocytosis with Farnesylated chemically self-assembled Nanorings
10.1021/acs.biomac.2c00837 · ExternalCitation · doi-reference
Improving the therapeutic potential of G-CSF through compact circular PEGylation based on orthogonal conjugations
10.1021/acs.biomac.3c00543 · ExternalCitation · doi-reference
Genetic code expansion: recent developments and emerging applications
10.1021/acs.chemrev.4c00216 · ExternalCitation · doi-reference
Native chemical ligation and extended methods: mechanisms, catalysis, scope, and limitations
10.1021/acs.chemrev.8b00712 · ExternalCitation · doi-reference
Peptide-based vaccines: current Progress and future challenges
10.1021/acs.chemrev.9b00472 · ExternalCitation · doi-reference
Enzymatic properties of recombinant ligase Butelase-1 and its application in cyclizing food-derived angiotensin I-converting enzyme inhibitory peptides
10.1021/acs.jafc.1c01755 · ExternalCitation · doi-reference
Head-to-tail cyclization after interaction with trypsin: a scorpion venom peptide that resembles plant cyclotides
10.1021/acs.jmedchem.0c00686 · ExternalCitation · doi-reference
Molecular engineering of insulin Icodec, the first acylated insulin Analog for once-weekly Administration in Humans
10.1021/acs.jmedchem.1c00257 · ExternalCitation · doi-reference
Engineering of a biologically active glycosylated glucagon-like Peptide-1 analogue
10.1021/acs.jmedchem.4c00093 · ExternalCitation · doi-reference
2FA-platform generates dual fatty acid-conjugated GLP-1 receptor agonist TE-8105 with enhanced diabetes, obesity, and NASH efficacy compared to Semaglutide
10.1021/acs.jmedchem.4c02153 · ExternalCitation · doi-reference
Discovery of the once-weekly glucagon-like Peptide-1 (GLP-1) analogue Semaglutide
10.1021/acs.jmedchem.5b00726 · ExternalCitation · doi-reference
Enzymatic on-resin peptide cleavage and in situ cyclization one-pot strategy for the synthesis of cyclopeptide and cyclotide
10.1021/acs.joc.8b02032 · ExternalCitation · doi-reference
Employing broad substrate specificity of Omniligase to generate phage-encoded bicyclic peptide libraries for ligand discovery
10.1021/acs.orglett.5c01205 · ExternalCitation · doi-reference
Improving Sortase-A-mediated transpeptidation reactions by electrostatically assisted capture
10.1021/acs.orglett.5c03718 · ExternalCitation · doi-reference
Phage display of Graspeptides via SrtA-mediated peptide ligation and cyclization
10.1021/acs.orglett.5c03982 · ExternalCitation · doi-reference
GFP Farnesylation as a suitable strategy for selectively tagging exosomes
10.1021/acsabm.4c01112 · ExternalCitation · doi-reference
Enzymatic Macrolactamization of mRNA display libraries for inhibitor selection
10.1021/acschembio.2c00828 · ExternalCitation · doi-reference
Hepta-mutant Staphylococcus aureus Sortase a (SrtA7m) as a tool for in vivo protein Labeling in Caenorhabditis elegans
10.1021/acschembio.6b00998 · ExternalCitation · doi-reference
Polyethylene glycol immunogenicity: theoretical, clinical, and practical aspects of anti-polyethylene glycol antibodies
10.1021/acsnano.1c05922 · ExternalCitation · doi-reference
Advances in drug delivery systems based on red blood cells and their membrane-derived nanoparticles
10.1021/acsnano.2c11965 · ExternalCitation · doi-reference
Design and study of PEG linkers that enable robust characterization of PEGylated proteins
10.1021/acsptsci.1c00112 · ExternalCitation · doi-reference
Engineering protein farnesyltransferase for enzymatic protein Labeling applications
10.1021/bc500240p · ExternalCitation · doi-reference
Integrated chemoenzymatic approach to streamline the assembly of complex glycopeptides in the liquid phase
10.1021/jacs.2c01819 · ExternalCitation · doi-reference
Site-specific Glyco-tagging of native proteins for the development of biologicals
10.1021/jacs.4c11091 · ExternalCitation · doi-reference
Butelase 1: a versatile ligase for peptide and protein macrocyclization
10.1021/jacs.5b11014 · ExternalCitation · doi-reference
Engineering a catalytically efficient recombinant protein ligase
10.1021/jacs.6b12637 · ExternalCitation · doi-reference
OaAEP1-mediated ligation of Mirror-image peptides via acyl donor substrate engineering
10.1021/jacs.6c00057 · ExternalCitation · doi-reference
Engineering orthogonal polypeptide GalNAc-transferase and UDP-sugar pairs
10.1021/jacs.9b04695 · ExternalCitation · doi-reference
Versatile peptide macrocyclization with Diels–Alder cycloadditions
10.1021/jacs.9b07578 · ExternalCitation · doi-reference
Chemoenzymatic synthesis of glycoengineered IgG antibodies and glycosite-specific antibody–drug conjugates
10.1038/nprot.2017.058 · ExternalCitation · doi-reference
Antibody and antibody fragments site-specific conjugation using new Q-tag substrate of bacterial transglutaminase
10.1038/s41420-024-01845-3 · ExternalCitation · doi-reference
An atlas of O-linked glycosylation on peptide hormones reveals diverse biological roles
10.1038/s41467-020-17473-1 · ExternalCitation · doi-reference
Trends in peptide drug discovery
10.1038/s41573-020-00135-8 · ExternalCitation · doi-reference
Anti-obesity drug discovery: advances and challenges
10.1038/s41573-021-00337-8 · ExternalCitation · doi-reference
Derivatization with fatty acids in peptide and protein drug discovery
10.1038/s41573-022-00529-w · ExternalCitation · doi-reference
De novo design of luciferases using deep learning
10.1038/s41586-023-05696-3 · ExternalCitation · doi-reference
De novo design of protein structure and function with RFdiffusion
10.1038/s41586-023-06415-8 · ExternalCitation · doi-reference
A suite of kinetically superior AEP ligases can cyclise an intrinsically disordered protein
10.1038/s41598-019-47273-7 · ExternalCitation · doi-reference
Inhibition of human N myristoyltransferase 1 as a strategy to suppress cancer progression driven by myristoylation
10.1038/s41598-025-13529-8 · ExternalCitation · doi-reference
Design of a recombinant asparaginyl ligase for site-specific modification using efficient recognition and nucleophile motifs
10.1038/s42004-024-01173-8 · ExternalCitation · doi-reference
Sortase A-catalyzed peptide cyclization for the synthesis of macrocyclic peptides and glycopeptides
10.1039/c1cc13322e · ExternalCitation · doi-reference
Recent progress in enzymatic protein labelling techniques and their applications
10.1039/c8cs00537k · ExternalCitation · doi-reference
Cyclic peptides: backbone rigidification and capability of mimicking motifs at protein–protein interfaces
10.1039/d0cp04633g · ExternalCitation · doi-reference
Challenges in the use of sortase and other peptide ligases for site-specific protein modification
10.1039/d0cs01148g · ExternalCitation · doi-reference
Single-pot enzymatic synthesis of cancer-associated MUC16 O-glycopeptide libraries and multivalent protein glycoconjugates: a step towards cancer glycovaccines
10.1039/d0nj06021f · ExternalCitation · doi-reference
Characterization and application of natural and recombinant butelase-1 to improve industrial enzymes by end-to-end circularization
10.1039/d1ra03763c · ExternalCitation · doi-reference
Employing unnatural promiscuity of sortase to construct peptide macrocycle libraries for ligand discovery
10.1039/d4sc01992j · ExternalCitation · doi-reference
Plant asparaginyl endopeptidases and their structural determinants of function
10.1042/bst20200908 · ExternalCitation · doi-reference
Engineering protein prenylation: an emerging tool for selective protein modification
10.1042/bst20253076 · ExternalCitation · doi-reference
Mapping proteolytic neo-N termini at the surface of living cells
10.1073/pnas.2018809118 · ExternalCitation · doi-reference
Cell-based glycoengineering for production of homogeneous and specific glycoform-enriched antibodies with improved effector functions
10.1073/pnas.2423853122 · ExternalCitation · doi-reference
PEGylation technology: addressing concerns, moving forward
10.1080/10717544.2025.2494775 · ExternalCitation · doi-reference
Albumin-based drug designs for pharmacokinetic modulation
10.1080/17425255.2020.1801633 · ExternalCitation · doi-reference
10.1093/abt/tbaf010
10.1093/abt/tbaf010 · ExternalCitation · doi-reference
Decoding the complex substrate specificities of GalNAc-Ts
10.1093/glycob/cwaf073 · ExternalCitation · doi-reference
Protein design using structure-prediction networks: AlphaFold and RoseTTAFold as protein structure foundation models
10.1101/cshperspect.a041472 · ExternalCitation · doi-reference
Adherence to and persistence with antidiabetic medications and associations with clinical and economic outcomes in people with type 2 diabetes mellitus: a systematic literature review
10.1111/dom.14603 · ExternalCitation · doi-reference
An overview of turoctocog alfa pegol (N8-GP; ESPEROCT®) assay performance: implications for postadministration monitoring
10.1111/hae.13897 · ExternalCitation · doi-reference
An efficient and easily obtainable butelase variant for chemoenzymatic ligation and modification of peptides and proteins
10.1186/s12934-024-02598-5 · ExternalCitation · doi-reference
Combining machine learning with structure-based protein design to predict and engineer post-translational modifications of proteins
10.1371/journal.pcbi.1011939 · ExternalCitation · doi-reference
Microbial transglutaminase for biotechnological and biomedical engineering
10.1515/hsz-2018-0335 · ExternalCitation · doi-reference
10.2147/ijn.s487303
10.2147/ijn.s487303 · ExternalCitation · doi-reference
Phytochemical profiling and in silico evaluation of Artemisia absinthium compounds targeting leishmania N-myristoyltransferase: molecular docking, drug-likeness, and toxicity analyses
10.3389/fchem.2024.1508603 · ExternalCitation · doi-reference
Sialylation as an important regulator of antibody function
10.3389/fimmu.2022.818736 · ExternalCitation · doi-reference
A comprehensive review on current advances in peptide drug development and design
10.3390/ijms20102383 · ExternalCitation · doi-reference
MALDI-MS analysis of peptide libraries expands the scope of substrates for farnesyltransferase
10.3390/ijms222112042 · ExternalCitation · doi-reference
Vypal2: a versatile peptide ligase for precision tailoring of proteins
10.3390/ijms23010458 · ExternalCitation · doi-reference
The inducible Intein-mediated self-cleaving tag (IIST) system: a novel purification and Amidation system for peptides and proteins
10.3390/molecules26195948 · ExternalCitation · doi-reference
