Site-specific modification of proteins by chemical/enzymatic strategies
Paper Details
Site-specific modification of proteins by chemical/enzymatic strategies
Abstract
Functionalization of proteins is a particular domain for the generation of modified proteins constructs which exhibit stimulating and diverse biological properties. The area has enormous potential for chemists and biologists to tune the proteins functions. The site-specific modification of proteins by installing new moieties or subunits provides an excellent opportunity to expand proteins functional abilities. In this review, we highlighted the most significant studies in protein functionalization which include chemical and enzymatic strategies. Exploration of novel methodologies is still on-going and deserves significant attention for future research in protein functionalization.
Abbas A, Xing B, Loh TP. 2014. Allenamides as orthogonal handles for selective modification of cysteine in peptides and proteins. Angewandte Chemie International Edition (English) 53, 7491-7494.
Agard NJ, Baskin JM, Prescher JA, Lo A, Bertozzi CR. 2006. A Comparative Study of Bioorthogonal Reactions with Azides. ACS Chemical Biology 1, 644-648. http://dx.doi.org/10.1021/cb6003228.
Agarwal P, Bertozzi CR. 2015. Site-specific antibody-drug conjugates: the nexus of bioorthogonal chemistry, protein engineering, and drug development. Bioconjugate chemistry 26, 176-92. http://dx.doi.org/10.1021/bc5004982.
Agarwal P, Van der Weijden J, Sletten EM, Rabuka D, Bertozzi CR. 2013. A Pictet-Spengler ligation for protein chemical modification. Proceedings of the National Academy of Sciences of the United States of America 110, 46-51.
Ai HW, Lee JW, Schultz PG. 2010. A method to site-specifically introduce methyllysine into proteins in E. coli. Chemical communications 46, 5506-8. http://dx.doi.org/10.1039/c0cc00108b.
Albayrak C, Swartz JR. 2013. Using E. coli-based cell-free protein synthesis to evaluate the kinetic performance of an orthogonal tRNA and aminoacyl-tRNA synthetase pair. Biochemical and Biophysical Research Communications 431, 291-5. http://dx.doi.org/10.1016/j.bbrc.2012.12.108.
Anderl J, Müller C, Heckl-Östreicher B, Wehr R. 2014. Abstract 3616: Highly potent antibody-amanitin conjugates cause tumor-selective apoptosis. Cancer Research 71, 3616-3616. http://dx.doi.org/10.1158/1538-7445.am2011-3616.
Antos JM, Francis MB. 2004. Selective tryptophan modification with rhodium carbenoids in aqueous solution. Journal of the American Chemical Society 126, 10256-10257.
Axup JY, Bajjuri KM, Ritland M, Hutchins BM, Kim CH, Kazane SA, Halder R, Forsyth JS, Santidrian AF, Stafin K, Lu Y, Tran H, Seller AJ, Biroc SL, Szydlik A, Pinkstaff JK, Tian F, Sinha SC, Felding-Habermann B, Smider VV, Schultz PG. 2012. Synthesis of site-specific antibody-drug conjugates using unnatural amino acids. Proceedings of the National Academy of Sciences of the United States of America 109, 16101-6. http://dx.doi.org/10.1073/pnas.1211023109.
Bailey JJ, Bundle DR. 2014. Synthesis of high-mannose 1-thio glycans and their conjugation to protein. Organic and Biomolecular Chemistry 12, 2193-2213.
Ban H, Gavrilyuk J, Barbas III CF. 2010. Tyrosine bioconjugation through aqueous ene-type reactions: a click-like reaction for tyrosine. Journal of the American Chemical Society 132, 1523-1525.
Banci L, Benvenuti M, Bertini I, Cabelli DE, Calderone V, Fantoni A, Mangani S, Migliardi M, Viezzoli MS. 2005. From an inactive prokaryotic SOD homologue to an active protein through site-directed mutagenesis. Journal of the American Chemical Society 127, 13287-92. http://dx.doi.org/10.1021/ja052790o.
Bannwarth M, Correa IR, Sztretye M, Pouvreau S, Fellay C, Aebischer A, Royer, L, Rois E, Johnsson K. 2009. Indo-1 derivatives for local calcium sensing. ACS Chemical Biology 4, 179-190. http://dx.doi.org/10.1021/cb800258g.
Becker CF, Liu X, Olschewski D, Castelli R, Seidel R, Seeberger PH. 2008. Semisynthesis of a glycosylphosphatidylinositol-anchored prion protein. Angewandte Chemie International Edition 47, 8215-9.
Bennett EJ, Bjerregaard J, Knapp JE, Chavous DA, Friedman AM, Royer WE, Jr, O’Connor CM. 2003. Catalytic implications from the Drosophila protein L-isoaspartyl methyltransferase structure and site-directed mutagenesis. Biochemistry 42, 12844-53. http://dx.doi.org/10.1021/bi034891+.
Bernardes GJ, Chalker JM, Errey JC, Davis BG. 2008. Facile conversion of cysteine and alkyl cysteines to dehydroalanine on protein surfaces: versatile and switchable access to functionalized proteins. Journal of the American Chemical Society 130, 5052-3. http://dx.doi.org/10.1021/ja800800p.
Bernardes GJ, Steiner M, Hartmann I, Neri D, Casi G. 2013. Site-specific chemical modification of antibody fragments using traceless cleavable linkers. Nature Protocole 8, 2079-89. http://dx.doi.org/10.1038/nprot.2013.121.
Bertozzi CR. 2001. Chemical Glycobiology. Science, 291, 2357-2364. http://dx.doi.org/10.1126/science.1059820.
Boutureira O, Bernardes GAJ. 2015a. Advances in chemical protein modification. Chemical Reviews 115, 2174-2195.
Boutureira O, Bernardes GJ, Fernández‐González M, Anthony DC, Davis BG. 2012. Selenenylsulfide‐Linked Homogeneous Glycopeptides and Glycoproteins: Synthesis of Human “Hepatic Se Metabolite A”. Angewandte Chemie International Edition (English) 51, 1432-1436.
Boutureira O, Bernardes GJL. 2015b. Advances in Chemical Protein Modification. Chemical Reviews 115, 2174-2195.
Brik A, Jbara M. 2017. Palladium in Chemical Protein Synthesis and Modifications. Angewandte Chemie International Edition English.
Brunner AM, Marquardt H, Malacko AR, Lioubin MN, Purchio A. 1989. Site-directed mutagenesis of cysteine residues in the pro region of the transforming growth factor beta 1 precursor. Expression and characterization of mutant proteins. The Journal of Biological Chemistry 264, 13660-13664.
Brustad E, Bushey ML, Lee JW, Groff D, Liu W, Schultz PG. 2008a. A genetically encoded boronate-containing amino acid. Angewandte Chemie International Edition English 47, 8220-3. http://dx.doi.org/10.1021/ja807430h.
Brustad EM, Lemke EA, Schultz PG, Deniz AA. 2008b. A general and efficient method for the site-specific dual-labeling of proteins for single molecule fluorescence resonance energy transfer Journal of the American Chemical Society 130, 17664-5. http://dx.doi.org/10.1002/anie.200803240.
Buskas T, Li Y, Boons GJ. 2004. The immunogenicity of the tumor-associated antigen Lewis(y) may be suppressed by a bifunctional cross-linker required for coupling to a carrier protein. Chemistry 10, 3517-24. http://dx.doi.org/10.1002/chem.200400074.
Cal PM, Vicente JoB, Pires E, Coelho AV, Veiros LSF Cordeiro C, Gois PM. 2012. Iminoboronates: a new strategy for reversible protein modification. Journal of the American Chemical Society 134, 10299-10305.
Carrico ZM, Farkas ME, Zhou Y, Hsiao SC, Marks JD, Chokhawala H, Clark DS, Francis MB. 2012. N-Terminal labeling of filamentous phage to create cancer marker imaging agents. ACS Nano 6, 6675-80.
Casi G, Huguenin-Dezot N, Zuberbühler K, Scheuermann Jr, Neri D. 2012. Site-specific traceless coupling of potent cytotoxic drugs to recombinant antibodies for pharmacodelivery. Journal of the American Chemical Society 134, 5887-5892.
Casi G, Neri D. 2015. Antibody-Drug Conjugates and Small Molecule-Drug Conjugates: Opportunities and Challenges for the Development of Selective Anticancer Cytotoxic Agents. Journal of Medicinal Chemistry 58, 8751-61. http://dx.doi.org/10.1021/acs.jmedchem.5b00457.
Cellitti SE, Jones DH, Lagpacan L, Hao X, Zhang Q, Hu H, Brittain SM, Brinker A, Caldwell J, Bursulaya B, Spraggon G, Brock, A, Ryu Y, Uno T, Schultz PG, Geierstanger BH. 2008. In vivo incorporation of unnatural amino acids to probe structure, dynamics, and ligand binding in a large protein by nuclear magnetic resonance spectroscopy. Journal of the American Chemical Society 130, 9268-81. http://dx.doi.org/10.1021/ja801602q.
Chalker JM, Bernardes GJ, Lin YA, Davis BG. 2009a. Chemical modification of proteins at cysteine: opportunities in chemistry and biology. Chemistry -An Asian Journal 4, 630-40. http://dx.doi.org/10.1002/asia.200800427.
Chalker JM, Gunnoo SB, Boutureira O, Gerstberger SC, Fernández-González M, Bernardes GJL, Griffin L, Hailu H, Schofield CJ, Davis BG. 2011. Methods for converting cysteine to dehydroalanine on peptides and proteins. Chemical Sciences 2, 1666. http://dx.doi.org/10.1039/c1sc00185j.
Chalker JM, Wood CS, Davis BG. 2009b. A convenient catalyst for aqueous and protein Suzuki-Miyaura cross-coupling. Journal of the American Chemical Society 131, 16346-7. http://dx.doi.org/10.1021/ja907150m.
Chames P, Baty D. 2014. Bispecific antibodies for cancer therapy. mAbs, 1, 539-547. http://dx.doi.org/10.4161/mabs.1.6.10015.
Chan AO Y, Ho CM, Chong HC, Leung YC, Huang JS, Wong MK, Che CM. 2012. Modification of N-terminal α-amino groups of peptides and proteins using ketenes. Journal of the American Chemical Society 134, 2589-2598.
Chan AOY, Tsai JLL, Lo VKY, Li L, Wong MK, Che CM. 2013. Gold-mediated selective cysteine modification of peptides using allenes. Chemical communication 49, 1428-1430.
Chatterjee A, Sun SB, Furman JL, Xiao H, Schultz PG. 2013a. A versatile platform for single- and multiple-unnatural amino acid mutagenesis in Escherichia coli. Biochemistry 52, 1828-37. http://dx.doi.org/10.1021/bi4000244.
Chatterjee A, Xiao H, Bollong M, Ai HW, Schultz PG. 2013b. Efficient viral delivery system for unnatural amino acid mutagenesis in mammalian cells. Proceedings of the National Academy of Sciences of the United States of America 110, 11803-8. http://dx.doi.org/10.1073/pnas.1309584110.
Chen, S., Chen, S, Duan Q, Xu G. 2017. Site-Specific Acetyl Lysine Antibodies Reveal Differential Regulation of Histone Acetylation upon Kinase Inhibition. Cell Biochemistry and Biophysics 75, 119-129. http://dx.doi.org/10.1007/s12013-016-0777-y.
Chin JW, Cropp TA, Anderson JC, Mukherji M, Zhang Z, Schultz PG. 2003. An expanded eukaryotic genetic code. Science 301, 964-7. http://dx.doi.org/10.1126/science.1084772.
Choi SR, Seo JS, Bohaty RF, Poulter CD. 2014. Regio- and chemoselective immobilization of proteins on gold surfaces. Bioconjugate chemistry 25, 269-75. http://dx.doi.org/10.1021/bc400413d.
Clark PI, Lowe G. 1978. Conversion of the Active-Site Cysteine Residue of Papain into a Dehydro-serine, a Serine and a Glycine Residue. European Journal of Biochemistry 84, 293-299. http://dx.doi.org/10.1111/j.14321033.1978.tb12168.x.
Cohen R, Vugts DJ, Visser GW, Stigter-van Walsum M, Bolijn M, Spiga M, Lazzari P, Shankar S, Sani M, Zanda M, Van Dongen GA. 2014. Development of novel ADCs: conjugation of tubulysin analogues to trastuzumab monitored by dual radiolabeling. Cancer Research 74, 5700-10. http://dx.doi.org/10.1158/0008-5472.CAN-14-1141.
Cuculis L, Abil Z, Zhao H, Schroeder CM. 2016. TALE proteins search DNA using a rotationally decoupled mechanism.Nature Chemical Biology 12, 831-7. http://dx.doi.org/10.1038/nchembio.2152.
Cui Z, Mureev S, Polinkovsky ME, Tnimov Z, Guo Z, Durek T, Jones A, Alexandrov K. 2017. Combining Sense and Nonsense Codon Reassignment for Site-Selective Protein Modification with Unnatural Amino Acids. ACS Synthetic Biology 6, 535-544. http://dx.doi.org/10.1021/acssynbio.6b00245.
De Graaf AJ, Kooijman M, Hennink WE, Mastrobattista E. 2009. Nonnatural amino acids for site-specific protein conjugation. Bioconjate Chemistry 20, 1281-1295.
Debets MF, Van Berkel SS, Dommerholt J, Dirks AJ, Rutjes FP, Van Delft FL. 2011. Bioconjugation with strained alkenes and alkynes. Accounts of Chemical Research 44, 805-815.
Devaraj NK, Weissleder R, Hilderbrand SA. 2008. Tetrazine-based cycloadditions: application to pretargeted live cell imaging. Bioconjate Chemistry 19, 2297-9. http://dx.doi.org/10.1021/bc8004446.
Diethelm S, Schafroth MA, Carreira EM. 2014. Amine-selective bioconjugation using arene diazonium salts. Organic Letters 16, 3908-3911.
Dirksen A, Dawson PE. 2008. Rapid oxime and hydrazone ligations with aromatic aldehydes for biomolecular labeling. Bioconjugate Chemistry 19, 2543-8. http://dx.doi.org/10.1021/bc800310p.
Doronina SO, Toki BE, Torgov MY, Mendelsohn BA, Cerveny CG, Chace DF, DeBlanc RL, Gearing RP, Bovee TD, Siegall, CB, Francisco JA, Wahl AF, Meyer DL, Senter PD. 2003. Development of potent monoclonal antibody auristatin conjugates for cancer therapy. Nature Biotechnology 21, 778-84. http://dx.doi.org/10.1038/nbt832.
Duan W, Zhang YGX. 2016. Optimization and application of protein C-terminal labeling by carboxypeptidase Y. Sheng Wu Gong Cheng Xue Bao, 32, 135-148.
Dubinsky L, Krom BP, Meijler MM. 2012. Diazirine based photoaffinity labeling. Bioorganic & Medicinal Chemistry 20, 554-570.
Dumas A, Spicer CD, Gao Z, Takehana T, Lin YA, Yasukohchi T, Davis BG. 2013. Self-liganded Suzuki-Miyaura coupling for site-selective protein PEGylation. Angewandte Chemie International Edition English 52, 3916-21. http://dx.doi.org/10.1002/anie.201208626.
Edelheit O, Hanukoglu A, Hanukoglu I. 2009. Simple and efficient site-directed mutagenesis using two single-primer reactions in parallel to generate mutants for protein structure-function studies. BMC Biotechnology 9, 61. http://dx.doi.org/10.1186/1472-6750-9-61.
Eeftens JM, Van der Torre J, Burnham DR, Dekker C. 2015. Copper-free click chemistry for attachment of biomolecules in magnetic tweezers. BMC Biophysics 8, 9.
Ercolani L, Scire A, Galeazzi R, Massaccesi L, Cianfruglia L, Amici A, Piva F, Urbanelli L, Emiliani C, Principato G, Armeni T. 2016. A possible S-glutathionylation of specific proteins by glyoxalase II: An in vitro and in silico study. Cell Biochemistry and Function 34, 620-627. http://dx.doi.org/10.1002/cbf.3236.
Erickson HK, Park PU, Widdison WC, Kovtun, YV, Garrett LM, Hoffman K, Lutz RJ, Goldmacher VS, Blattler WA. 2006. Antibody-maytansinoid conjugates are activated in targeted cancer cells by lysosomal degradation and linker-dependent intracellular processing. Cancer Research 66, 4426-33. http://dx.doi.org/10.1158/0008-5472.CAN-05-4489.
Erickson HK, Widdison WC, Mayo MF, Whiteman K, Audette C, Wilhelm SD, Singh R. 2010. Tumor delivery and in vivo processing of disulfide-linked and thioether-linked antibody-maytansinoid conjugates. Bioconjugate Chemistry 21, 84-92. http://dx.doi.org/10.1021/bc900315y.
Ferguson MA. 1999. The structure, biosynthesis and functions of glycosylphosphatidylinositol anchors, and the contributions of trypanosome research. Journal of Cell Science 112, 2799-809.
Galian C, Bjorkholm P, Bulleid N, Von Heijne G. 2012. Efficient glycosylphosphatidylinositol (GPI) modification of membrane proteins requires a C-terminal anchoring signal of marginal hydrophobicity. Journal of Biological Chemistry 287, 16399-409. http://dx.doi.org/10.1074/jbc.M112.350009.
Gavrilyuk J, Ban H, Nagano M, Hakamata W, Barbas III CF. 2012. Formylbenzene diazonium hexafluorophosphate reagent for tyrosine-selective modification of proteins and the introduction of a bioorthogonal aldehyde. Bioconjugate Chemistry 23, 2321-2328.
Gebleux R, Casi G. 2016. Antibody-drug conjugates: Current status and future perspectives. Pharmacology & Therapeutics 167, 48-59. http://dx.doi.org/10.1016/j.pharmthera.2016.07.012.
Geoghegan KF, Stroh JG. 2002. Site-directed conjugation of nonpeptide groups to peptides and proteins via periodate oxidation of a 2-amino alcohol. Application to modification at N-terminal serine. Bioconjate Chemistry 3, 138-146. http://dx.doi.org/10.1021/bc00014a008.
Gerber HP, Sapra P, Loganzo F, May C. 2016. Combining antibody–drug conjugates and immune-mediated cancer therapy: What to expect? Biochemical Pharmacology 102, 1-6. http://dx.doi.org/10.1016/j.bcp.2015.12.008.
Gilchrist TL. 1969. Carbenes nitrenes and arynes.
Gronemeyer T, Chidley C, Juillerat A, Heinis C, Johnsson K. 2006. Directed evolution of O6-alkylguanine-DNA alkyltransferase for applications in protein labeling. Protein Engineering, Design and Selection 19, 309-16. http://dx.doi.org/10.1093/protein/gzl014.
Gruber R, Rogerson C, Windpassinger C, Banushi B, Straatman-Iwanowska A, Hanley, J, Forneris F, Strohal R, Ulz P, Crumrine D, Menon GK, Blunder S, Schmuth M, Muller T, Smith H, Mills K, Kroisel P, Janecke, AR, Gissen, P. 2017. Autosomal Recessive Keratoderma-Ichthyosis-Deafness (ARKID) Syndrome Is Caused by VPS33B Mutations Affecting Rab Protein Interaction and Collagen Modification. Journal of Investigative Dermatology 137, 845-854. http://dx.doi.org/10.1016/j.jid.2016.12.010.
Guimaraes CP, Witte MD, Theile CS, Bozkurt G, Kundrat L, Blom AE, Ploegh HL. 2013. Site-specific C-terminal and internal loop labeling of proteins using sortase-mediated reactions. Nature Protocal 8, 1787-99. http://dx.doi.org/10.1038/nprot.2013.101.
Guo HM, Minakawa M, Ueno L, Tanaka F. 2009. Synthesis and evaluation of a cyclic imine derivative conjugated to a fluorescent molecule for labeling of proteins. Bioorganic & Medicinal Chemistry Letters 19, 1210-1213.
Haruki H, Gonzalez MR, Johnsson K. 2012. Exploiting ligand-protein conjugates to monitor ligand-receptor interactions. PLoS One 7, e37598. http://dx.doi.org/10.1371/journal.pone.0037598.
Hemantha HP, Bavikar SN, Herman-Bachinsky Y, Haj-Yahya N, Bondalapati S, Ciechanover A, Brik A. 2014. Nonenzymatic polyubiquitination of expressed proteins. Journal of the American Chemical Society 136, 2665-2673.
Hemmerle T, Probst P, Giovannoni L, Green, AJ., Meyer T, Neri D. 2013. The antibody-based targeted delivery of TNF in combination with doxorubicin eradicates sarcomas in mice and confers protective immunity. British Journal of Cancer 109, 1206-13. http://dx.doi.org/10.1038/bjc.2013.421.
Huang H, Huang N, Wang Z, Xia G, Chen M, He L, Tong Z, Ren C. 2017. Room-temperature synthesis of carnation-like ZnO@ AgI hierarchical nanostructures assembled by AgI nanoparticles-decorated ZnO nanosheets with enhanced visible light photocatalytic activity. Journal of Colloid and Interface Science 502, 77-88.
Hudis CA. 2007. Trastuzumab–mechanism of action and use in clinical practice. The New England Journal of Medicine 357, 39-51. http://dx.doi.org/10.1056/NEJMra043186.
Hutchins BM, Kazane SA, Staflin K, Forsyth JS, Felding-Habermann B, Schultz PG, Smider VV. 2011. Site-specific coupling and sterically controlled formation of multimeric antibody fab fragments with unnatural amino acids. Journal of Molecular Biology 406, 595-603. http://dx.doi.org/10.1016/j.jmb.2011.01.011.
Jeremy M, Berg John L, Tymoczko Stryer L. 2002. Biochemistry. 5 ed.
Johnson DB, Xu J, Shen Z, Takimoto JK, Schultz MD, Schmitz RJ, Xiang Z, Ecker JR, Briggs SP, Wang L. 2011. RF1 knockout allows ribosomal incorporation of unnatural amino acids at multiple sites. Nature Chemical Biology 7, 779-86. http://dx.doi.org/10.1038/nchembio.657.
Judes A, Bruch A, Klassen R, Helm M, Schaffrath R. 2016. Sulfur transfer and activation by ubiquitin-like modifier system Uba4*Urm1 link protein urmylation and tRNA thiolation in yeast. Microbial Cell 3, 554-564. http://dx.doi.org/10.15698/mic2016.11.539.
Karve TM, Cheema AK. 2011. Small changes huge impact: the role of protein posttranslational modifications in cellular homeostasis and disease. Journal of Amino Acids 2011, 1-13. http://dx.doi.org/10.4061/2011/207691.
Kaur H, Kamalov M, Brimble MA. 2016. Chemical Synthesis of Peptides Containing Site-Specific Advanced Glycation Endproducts. Accounts of Chemical Research 49, 2199-2208. http://dx.doi.org/10.1021/acs.accounts.6b00366.
Kemppainen K, Rommi K, Holopainen U, Kruus K. 2016. Steam explosion of Brewer’s spent grain improves enzymatic digestibility of carbohydrates and affects solubility and stability of proteins. Applied Biochemistry and Biotechnology 180, 94-108. http://dx.doi.org/10.1007/s12010-016-2085-9.
Kiick KL, Saxon E, Tirrell DA, Bertozzi CR. 2002. Incorporation of azides into recombinant proteins for chemoselective modification by the Staudinger ligation. Proceedings of the National Academy of Sciences of the United States of America 99, 19-24.
Kim CH, Axup JY, Dubrovska A, Kazane SA, Hutchins BA, Wold ED, Smider VV, Schultz PG. 2012. Synthesis of bispecific antibodies using genetically encoded unnatural amino acids. Journal of the American Chemical Society 134, 9918-21. http://dx.doi.org/10.1021/ja303904e.
Kim CH, Axup JY, Schultz PG. 2013. Protein conjugation with genetically encoded unnatural amino acids. Current Opinion in Chemical Biology 17, 412-9.
Knop K, Hoogenboom R, Fischer D, Schubert US. 2010. Poly(ethylene glycol) in drug delivery: pros and cons as well as potential alternatives. Angewandte Chemie International Edition in English 49, 6288-308. http://dx.doi.org/10.1002/anie.200902672.
Koniev O, Leriche G, Nothisen M, Remy JS, Strub JM, Schaeffer-Reiss C, Van Dorsselaer A, Baati R, Wagner A. 2014. Selective irreversible chemical tagging of cysteine with 3-arylpropiolonitriles. Bioconjugate Chemistry 25, 202-206.
Kovtun YV, Audette CA, Mayo MF, Jones GE, Doherty H, Maloney EK, Erickson HK, Sun X, Wilhelm S, Ab O, Lai KC, Widdison WC, Kellogg B, Johnson H, Pinkas J, Lutz RJ, Singh R, Goldmacher VS, Chari RVJ. 2010. Antibody-Maytansinoid Conjugates Designed to Bypass Multidrug Resistance. Cancer Research 70, 2528-2537. http://dx.doi.org/10.1158/0008-5472.can-09-3546.
Krop I, Winer EP. 2014. Trastuzumab emtansine: a novel antibody-drug conjugate for HER2-positive breast cancer. Clinical Cancer Research 20, 15-20. http://dx.doi.org/10.1158/1078-0432.CCR-13-0541.
Kundu R, Ball ZT. 2013. Rhodium-catalyzed cysteine modification with diazo reagents. Chemical Communications 49, 4166-4168.
Lambert JM, Chari RV. 2014. Ado-trastuzumab Emtansine (T-DM1): an antibody-drug conjugate (ADC) for HER2-positive breast cancer. Journal of Medicinal Chemistry 57, 6949-64. http://dx.doi.org/10.1021/jm500766w.
Lane KT, Beese LS. 2006. Thematic review series: lipid posttranslational modifications. Structural biology of protein farnesyltransferase and geranylgeranyltransferase type I. The Journal of Lipid Research 47, 681-99. http://dx.doi.org/10.1194/jlr.R600002-JLR200.
Lang K, Chin JW. 2014a. Cellular incorporation of unnatural amino acids and bioorthogonal labeling of proteins. Chemical Reviews 114, 4764-806. http://dx.doi.org/10.1021/cr400355w.
Lang K, Chin JW. 2014b. Cellular incorporation of unnatural amino acids and bioorthogonal labeling of proteins. Chemical Reviews 114, 4764-4806.
Lang K, Davis L, Torres-Kolbus J, Chou C, Deiters A, Chin JW. 2012a. Genetically encoded norbornene directs site-specific cellular protein labelling via a rapid bioorthogonal reaction. Nature Chemistry 4, 298-304. http://dx.doi.org/10.1038/nchem.1250
Lang K, Davis L, Wallace S, Mahesh M, Cox DJ, Blackman ML, Fox JM, Chin JW. 2012b. Genetic Encoding of bicyclononynes and trans-cyclooctenes for site-specific protein labeling in vitro and in live mammalian cells via rapid fluorogenic Diels-Alder reactions. Journal of the American Chemical Society 134, 10317-20. http://dx.doi.org/10.1021/ja302832g.
Larson SM, Carrasquillo JA, Cheung NK, Press OW. 2015. Radioimmunotherapy of human tumours. Nature Reviews Cancer 15, 347-60. http://dx.doi.org/10.1038/nrc3925.
Laughlin ST, Baskin JM, Amacher SL, Bertozzi CR. 2008. In vivo imaging of membrane-associated glycans in developing zebrafish. Science 320,664-7. http://dx.doi.org/10.1126/science.1155106.
Lee HS, Guo J, Lemke EA, Dimla RD, Schultz PG. 2009. Genetic incorporation of a small, environmentally sensitive, fluorescent probe into proteins in Saccharomyces cerevisiae. Journal of the American Chemical Society 131, 12921-3. http://dx.doi.org/10.1021/ja904896s.
Levengood MR, Zhang X, Hunter JH, Emmerton KK, Miyamoto JB, Lewis TS, Senter PD. 2017. Orthogonal Cysteine Protection Enables Homogeneous Multi-Drug Antibody-Drug Conjugates. Angewandte Chemie International Edition 56, 733-737. http://dx.doi.org/10.1002/anie.201608292.
Li Q, Sun B, Jia H, Hou J, Yang R, Xiong K, Xu Y, Li X. 2017. Engineering a xylanase from Streptomyce rochei L10904 by mutation to improve its catalytic characteristics. International Journal of Biological Macromolecules 101, 366-372. http://dx.doi.org/10.1016/j.ijbiomac.2017.03.135.
Lin YA, Chalker JM, Davis BG. 2010. Olefin cross-metathesis on proteins: investigation of allylic chalcogen effects and guiding principles in metathesis partner selection. Journal of the American Chemical Society 132, 16805-11. http://dx.doi.org/10.1021/ja104994d.
Lin YA, Davis BG. 2010. The allylic chalcogen effect in olefin metathesis. Beilstein. The Journal of Organic Chemistry 6, 1219-1228. http://dx.doi.org/10.3762/bjoc.6.140.
List T, Casi G, Neri D. 2014. A chemically defined trifunctional antibody-cytokine-drug conjugate with potent antitumor activity. Molecular Cancer Therapeutics 13, 2641-52. http://dx.doi.org/10.1158/1535-7163.MCT-14-0599.
Litovchick A, Dumelin CE, Habeshian S, Gikunju D, Guie MA, Centrella P, Zhang Y, Sigel EA, Cuozzo JW, Keefe AD, Clark MA. 2015. Encoded Library Synthesis Using Chemical Ligation and the Discovery of sEH Inhibitors from a 334-Million Member Library. Scientific Reports 5, 10916. http://dx.doi.org/10.1038/srep10916.
Liu CC, Mack AV, Brustad EM, Mills JH, Groff, D, Smider VV, Schultz PG. 2009. Evolution of proteins with genetically encoded “chemical warheads”. Journal of the American Chemical Society 131, 9616-7. http://dx.doi.org/10.1021/ja902985e.
Liu CC, Schultz PG. 2006. Recombinant expression of selectively sulfated proteins in Escherichia coli. Nature Biotechnology 24, 1436-40.
Liu Z, Cheng S, Gallie DR, Julian RR. 2008. Exploring the mechanism of selective noncovalent adduct protein probing mass spectrometry utilizing site-directed mutagenesis to examine ubiquitin. Analytical Chemistry 80, 3846-52. http://dx.doi.org/10.1021/ac800176u.
Lodish H. 2008. Molecular cell biology. Macmillan.
Lorenzi M, Puppo C, Lebrun R, Lignon S, Roubaud V, Martinho M, Mileo E, Tordo P, Marque SR, Gontero B. 2011. Tyrosine‐Targeted Spin Labeling and EPR Spectroscopy: An Alternative Strategy for Studying Structural Transitions in Proteins. Angewandte Chemie International Edition 50, 9108-9111.
Lyon RP, Bovee TD, Doronina SO, Burke PJ, Hunter JH, Neff-LaFord HD, Jonas M., Anderson ME, Setter JR, Senter PD. 2015. Reducing hydrophobicity of homogeneous antibody-drug conjugates improves pharmacokinetics and therapeutic index. Nature Biotechnology 33, 733-5.
Marshall CJ, Agarwal N, Kalia J, Grosskopf VA, McGrath NA, Abbott NL, Raines RT, Shusta EV. 2013. Facile chemical functionalization of proteins through intein-linked yeast display. Bioconjugate Chemistry 24(9), 1634-44. http://dx.doi.org/10.1021/bc4002618.
Martinelli E, De Palma R, Orditura M, De Vita F, Ciardiello F. 2009. Anti-epidermal growth factor receptor monoclonal antibodies in cancer therapy. Clinical & Experimental Immunology 158, 1-9. http://dx.doi.org/10.1111/j.1365-2249.2009.03992.x.
Massa S, Xavier C, De Vos J, Caveliers V, Lahoutte T, Muyldermans S, Devoogdt N. 2014. Site-specific labeling of cysteine-tagged camelid single-domain antibody-fragments for use in molecular imaging. Bioconjate Chemisrty 25, 979-988.
Maynard H. 2015. Chemical biology: Protein modification in a trice. Nature 526, 646-7.
Minnihan EC, Young DD, Schultz PG, Stubbe 2011. Incorporation of fluorotyrosines into ribonucleotide reductase using an evolved, polyspecific aminoacyl-tRNA synthetase. Journal of the American Chemical Society 133, 15942-5.
Mühlberg M, Böhrsch V, Hackenberger CPR. 2009. Chemical Biology. Learning through Case Studies. Edited by Herbert Waldmann and Petra Janning. Angewandte Chemie International Edition english 48, 8175-8175. http://dx.doi.org/10.1002/anie.200904323.
Munier R, Cohen GN. 1959. Incorporation d’analogues structuraux d’aminoacides dans les protéines bactériennes au cours de leur synthèse in vivo. Biochimica et Biophysica Acta 31, 378-391.
Muraki M, Harata K, Sugita N, Sato KI. 2000. Protein−Carbohydrate Interactions in Human Lysozyme Probed by Combining Site-Directed Mutagenesis and Affinity Labeling†. Biochemistry 39, 292-299.
Neri D, Sondel PM. 2016. Immunocytokines for cancer treatment: past, present and future. Current Opinion in Immunology 40, 96-102. http://dx.doi.org/10.1016/j.coi.2016.03.006.
Ngo JT, Tirrell DA. 2011. Noncanonical amino acids in the interrogation of cellular protein synthesis. Accounts of Chemical Research 44, 677-85.
Nilles Matthew L, Condry DJ, Danielle. 2017. Type 3 Secretion Systems: methods and protocols.
Nolting B. 2013. Linker technologies for antibody-drug conjugates. Methods in Molecular Biology 1045, 71-100. http://dx.doi.org/10.1007/978-1-62703-541-5_5.
Orlean P, Menon AK. 2007. Thematic review series: Lipid Posttranslational Modifications.GPI anchoring of protein in yeast and mammalian cells, or: how we learned to stop worrying and love glycophospholipids. The Journal of Lipid Research 48, 993-1011. http://dx.doi.org/10.1194/jlr.R700002-JLR200.
Palomo JM. 2017. Semisynthetic Enzymes by Protein-Peptide Site-Directed Covalent Conjugation: Methods and Applications. Methods in Enzymology 590, 305-316. http://dx.doi.org/10.1016/bs.mie.2017.01.001.
Palsuledesai CC, Distefano MD. 2015. Protein prenylation: enzymes, therapeutics, and biotechnology applications. ACS Chemical Biology 10, 51-62. http://dx.doi.org/10.1021/cb500791f.
Palumbo A, Hauler F, Dziunycz P, Schwager K, Soltermann A, Pretto F, Alonso C, Hofbauer GF, Boyle RW, Neri D. 2011. A chemically modified antibody mediates complete eradication of tumours by selective disruption of tumour blood vessels. British Journal of Cancer 104, 1106-15. http://dx.doi.org/10.1038/bjc.2011.78.
Pan Y, Yan C, Hu Y, Fan Y, Pan Q, Wan Q, Torcivia-Rodriguez J, Mazumder R. 2017. Distribution bias analysis of germline and somatic single-nucleotide variations that impact protein functional site and neighboring amino acids. Scientific Reports 7, 42169. http://dx.doi.org/10.1038/srep42169.
Panowski S, Bhakta S, Raab H, Polakis P, Junutula JR. 2014. Site-specific antibody drug conjugates for cancer therapy. MAbs 6, 34-45.
Pedley RB, Boden JA, Boden R, Begent RHJ, Turner A, Haines AMR, King DJ. 1994. The potential for enhanced tumour localisation by poly(ethylene glycol) modification of anti-CEA antibody. British Journal of Cancer 70, 1126-1130. http://dx.doi.org/10.1038/bjc.1994.459.
Pei XL, Wang QY, Li CL, Qiu XF, Xie KL, Huang LF, Wang AM, Zeng ZW, Xie T. 2011. Efficient production of a thermophilic 2-deoxyribose-5-phosphate aldolase in glucose-limited fed-batch cultivations of Escherichia coli by continuous lactose induction strategy. Applied Biochemistry and Biotechnology 165, 416-25. http://dx.doi.org/10.1007/s12010-011-9261-8.
Platisa J, Vasan G, Yang A, Pieribone VA. 2017. Directed Evolution of Key Residues in Fluorescent Protein Inverses the Polarity of Voltage Sensitivity in the Genetically Encoded Indicator ArcLight. ACS Chemical Neuroscience 8, 513-523. http://dx.doi.org/10.1021/acschemneuro.6b00234.
Platz MS. 2002. Comparison of Phenylcarbene and Phenylnitrene. Accounts of Chemical Research 28, 487-492. http://dx.doi.org/10.1021/ar00060a004.
Polgar L, Bender ML. 1966. A New Enzyme Containing a Synthetically Formed Active Site. Thiol-Subtilisin1. Journal of the American Chemical Society 88, 3153-3154.
Ponsin G, Qu SJ, Fan HZ, Pownall HJ. 2003. Structural and functional determinants of human plasma phospholipid transfer protein activity as revealed by site-directed mutagenesis of charged amino acids. Biochemistry 42, 4444-51. http://dx.doi.org/10.1021/bi027006g.
Popp BV, Ball ZT. 2010. Structure-selective modification of aromatic side chains with dirhodium metallopeptide catalysts. Journal of the American Chemical Society 132, 6660-2.
Prestwich GD, Dormán G, Elliott JT., Marecak DM, Chaudhary A. 1997. Benzophenone Photoprobes for Phosphoinositides, Peptides and Drugs. Photochemistry and Photobiology 65, 222-234. http://dx.doi.org/10.1111/j.17511097.1997.tb08548.x.
Rashidian M, Dozier JK, Distefano MD. 2013. Enzymatic labeling of proteins: techniques and approaches. Bioconjate Chemistry 24, 1277-1294.
Richter AW, Åkerblom E. 1983. Antibodies against Polyethylene Glycol Produced in Animals by Immunization with Monomethoxy Polyethylene Glycol Modified Proteins. International Archives of Allergy and Immunology 70, 124-131.
Robinson MA, Charlton ST, Garnier P, Wang XT, Davis SS, Perkins AC, Frier M, Duncan R, Savage TJ, Wyatt DA. 2004. LEAPT: lectin-directed enzyme-activated prodrug therapy. Proceedings of the National Academy of Sciences of the United States of America 101, 14527-14532.
Rodriguez EA, Lester HA, Dougherty DA. 2006. In vivo incorporation of multiple unnatural amino acids through nonsense and frameshift suppression. Proceedings of the National Academy of Sciences of the United States of America 103, 8650-5. http://dx.doi.org/10.1073/pnas.0510817103.
Roopenian DC, Akilesh S. 2007. FcRn: the neonatal Fc receptor comes of age. Nature Reviews Immunology 7, 715-25. http://dx.doi.org/10.1038/nri2155.
Rosen CB, Kwant RL, MacDonald JI, Rao M, Francis MB. 2016. Capture and Recycling of Sortase A through Site-Specific Labeling with Lithocholic Acid. Angewandte Chemie International Edition English 55, 8585-9. http://dx.doi.org/10.1002/anie.201602353.
Rostovtsev VV, Green LG, Fokin VV, Sharpless KB. 2002. A stepwise huisgen cycloaddition process: copper (I)‐catalyzed regioselective “ligation” of azides and terminal alkynes. Angewandte Chemie International Edition English 114, 2708-2711.
Rowan F, Richards M, Widya M, Bayliss R, Blagg J. 2014. Diverse functionalization of Aurora-A kinase at specified surface and buried sites by native
chemical modification. PLoS One 9, e103935.
Santoro SW, Wang L, Herberich B, King DS, Schultz PG. 2002. An efficient system for the evolution of aminoacyl-tRNA synthetase specificity. Nature Biotechnology 20, 1044-8. http://dx.doi.org/10.1038/nbt742.
Sarpong K, Bose R. 2017. Efficient sortase-mediated N-terminal labeling of TEV protease cleaved recombinant proteins. Analytical Biochemistry 521, 55-58. http://dx.doi.org/10.1016/j.ab.2017.01.008.
Schardon CL, Tuley A, Er JAV, Swartzel JC, Fast W. 2017. Selective Covalent Protein Modification by 4-Halopyridines through Catalysis. ChemBioChem, 18, 1551-1556.
Schmidt MM, Wittrup KD. 2009. A modeling analysis of the effects of molecular size and binding affinity on tumor targeting. Molecular Cancer Therapeutics 8, 2861-71. http://dx.doi.org/10.1158/1535-7163.MCT-09-0195.
Senter PD, Sievers EL. 2012. The discovery and development of brentuximab vedotin for use in relapsed Hodgkin lymphoma and systemic anaplastic large cell lymphoma. Nature Biotechnology 30, 631-7.
Shaunak S, Godwin A, Choi JW, Balan S, Pedone E, Vijayarangam D, Heidelberger S, Teo I, Zloh M, Brocchini S. 2006. Site-specific PEGylation of native disulfide bonds in therapeutic proteins. Nature Chemical Biology 2, 312-3. http://dx.doi.org/10.1038/nchembio786.
Shiu HY, Chan TC, Ho CM, Liu, Wong MK, Che CM. 2009. Electron‐Deficient Alkynes as Cleavable Reagents for the Modification of Cysteine‐Containing Peptides in Aqueous Medium. Chemistry – A European Journal 15, 3839-3850.
Song W, Wang Y, Qu J, Madden MM, Lin Q. 2008. A photoinducible 1,3-dipolar cycloaddition reaction for rapid, selective modification of tetrazole-containing proteins. Angewandte Chemie International Edition english 47, 2832-5. http://dx.doi.org/10.1002/anie.200705805.
Speers AE, Adam GC, Cravatt BF. 2003. Activity-based protein profiling in vivo using a copper(i)-catalyzed azide-alkyne [3 + 2] cycloaddition. Journal of the American Chemical Society 125, 4686-7.
Spicer CD, Davis BG. 2013. Rewriting the bacterial glycocalyx via Suzuki-Miyaura cross-coupling. Chemical Communications 49, 2747-9. http://dx.doi.org/10.1039/c3cc38824g.
Spicer CD, Davis BG. 2014. Selective chemical protein modification. Nature Communications 5, 4740.
Spicer CD, Triemer T, Davis BG. 2012. Palladium-mediated cell-surface labeling. Journal of the American Chemical Society 134, 800-3. http://dx.doi.org/10.1021/ja209352s.
Srinivasarao M, Galliford CV, Low PS. 2015. Principles in the design of ligand-targeted cancer therapeutics and imaging agents. Nature Reviews Drug Discovery 14, 203-19.
Stöckmann H, Neves AA, Stairs S, Brindle KM, Leeper FJ. 2011. Exploring isonitrile-based click chemistry for ligation with biomolecules. Organic & Biomolecular Chemistry 9, 7303-7305.
Strop P, Delaria K, Foletti D, Witt JM, Hasa-Moreno A, Poulsen K, Casas MG, Dorywalska M, Farias S, Pios A, Lui V, Dushin R, Zhou D, Navaratnam T, Tran, TT, Sutton J, Lindquist, KC, Han B, Liu SH, Shelton DL, Pons J, Rajpal A. 2015. Site-specific conjugation improves therapeutic index of antibody drug conjugates with high drug loading. Nature Biotechnology 33, 694-6. http://dx.doi.org/10.1038/nbt.3274.
Strop P, Liu SH, Dorywalska M, Delaria K, Dushin RG, Tran TT, Ho WH, Farias S, Casas MG, Abdiche Y, Zhou D, Chandrasekaran R, Samain C, Loo C, Rossi A, Rickert M, Krimm S, Wong T, Chin SM, Yu J, Dilley J, Chaparro-Riggers J, Filzen GF, O’Donnell CJ, Wang F, Myers JS, Pons J, Shelton DL, Rajpal A. 2013. Location matters: site of conjugation modulates stability and pharmacokinetics of antibody drug conjugates. Chemistry & Biology 20, 161-7. http://dx.doi.org/10.1016/j.chembiol.2013.01.010.
Summerer D, Chen S, Wu N, Deiters A, Chin JW, Schultz PG. 2006. A genetically encoded fluorescent amino acid. Proceedings of the National Academy of Sciences of the United States of America 103, 9785-9.
Sun C, Luo G, Neravetla S, Ghosh SS, Forood B. 2013. Native chemical ligation derived method for recombinant peptide/protein C-terminal amidation. Bioorganic & Medicinal Chemistry Letters 23, 5203-8. http://dx.doi.org/10.1016/j.bmcl.2013.06.095.
Sun MM, Beam KS, Cerveny CG, Hamblett KJ, Blackmore RS, Torgov MY, Handley FG, Ihle NC, Senter PD, Alley SC. 2005. Reduction-alkylation strategies for the modification of specific monoclonal antibody disulfides. Bioconjugate Chemistry 16, 1282-90.
Sun X, Zhang A, Baker B, Sun L, Howard A, Buswell J, Maurel D, Masharina A, Johnsson K, Noren CJ, Xu MQ, Correa IR. 2011. Development of SNAP-tag fluorogenic probes for wash-free fluorescence imaging. ChemBioChem 12, 2217-26. http://dx.doi.org/10.1002/cbic.201100173.
Swarts BM, Guo Z. 2010. Synthesis of a glycosylphosphatidylinositol anchor bearing unsaturated lipid chains. Journal of the American Chemical Society 132, 6648-50.
Takahara M, Hayashi K, Goto M, Kamiya N. 2016. Enzymatic conjugation of multiple proteins on a DNA aptamer in a tail-specific manner. Biotechnology Journal 11, 814-23. http://dx.doi.org/10.1002/biot.201500560.
Tam A, Arnold U, Soellner MB, Raines RT. 2007. Protein prosthesis: 1, 5-disubstituted [1, 2, 3] triazoles as cis-peptide bond surrogates. Journal of the American Chemical Society 129, 12670-12671.
Tanaka K, Fukase K, Katsumura S. 2011. Exploring a unique reactivity of 6π-azaelectrocyclization to enzyme inhibition, natural products synthesis, and molecular imaging: An approach to chemical biology by synthetic chemists. Synlett 2011, 2115-2139.
Tanaka Y, Nakahara Y, Hojo H, Nakahara Y. 2003. Studies directed toward the synthesis of protein-bound GPI anchor. Tetrahedron 59, 4059-4067. http://dx.doi.org/10.1016/s0040-4020(03)00615-x.
Teicher BA, Chari RV. 2011. Antibody conjugate therapeutics: challenges and potential. Clinical Cancer Research 17, 6389-97. http://dx.doi.org/10.1158/1078-0432.CCR-11-1417.
Thielges MC, Axup JY, Wong D, Lee HS, Chung JK, Schultz PG, Fayer MD. 2011. Two-dimensional IR spectroscopy of protein dynamics using two vibrational labels: a site-specific genetically encoded unnatural amino acid and an active site ligand. The Journal of Physical Chemistry B 115, 11294-304. http://dx.doi.org/10.1021/jp206986v.
Thompson O, Edgley M, Strasbourger P, Flibotte S, Ewing B, Adair R, Au V, Chaudhry I, Fernando L, Hutter H, Kieffer A, Lau J, Lee N, Miller A, Raymant G, Shen B, Shendure J, Taylor J, Turner, EH, Hillier LW, Moerman DG, Waterston RH. 2013. The million mutation project: a new approach to genetics in Caenorhabditis elegans. Genome Research 23, 1749-62. http://dx.doi.org/10.1101/gr.157651.113.
Tian F, Lu Y, Manibusan A, Sellers A, Tran H, Sun Y, Phuong T, Barnett R, Hehli B, Song F, DeGuzman MJ, Ensari S, Pinkstaff JK, Sullivan LM, Biroc SL, Cho H, Schultz PG, DiJoseph J, Dougher M, Ma D, Dushin R, Leal, M, Tchistiakova L, Feyfant E, Gerber HP, Sapra P. 2014. A general approach to site-specific antibody drug conjugates. Proceedings of the National Academy of Sciences of the United States of America 111, 1766-71. http://dx.doi.org/10.1073/pnas.1321237111.
Tilley SD, Francis MB. 2006. Tyrosine-selective protein alkylation using π-allylpalladium complexes. Journal of the American Chemical Society 128, 1080-1081.
Toda N, Asano S, Barbas CF. 2013. Rapid, Stable, Chemoselective Labeling of Thiols with Julia–Kocieński‐like Reagents: A Serum‐Stable Alternative to Maleimide‐Based Protein Conjugation. Angewandte Chemie International Edition (English) 52, 12592-12596.
Toti US, Guru BR, Grill AE, Panyam J. 2010. Interfacial activity assisted surface functionalization: a novel approach to incorporate maleimide functional groups and cRGD peptide on polymeric nanoparticles for targeted drug delivery. Molecular Pharmaceutics 7, 1108-17. http://dx.doi.org/10.1021/mp900284c.
van der Velden VHJ. 2001. Targeting of the CD33-calicheamicin immunoconjugate Mylotarg (CMA-676) in acute myeloid leukemia: in vivo and in vitro saturation and internalization by leukemic and normal myeloid cells. Blood 97, 3197-3204. http://dx.doi.org/10.1182/blood.V97.10.3197.
Venkat S, Gregory C, Sturges J, Gan Q, Fan C. 2017. Studying the Lysine Acetylation of Malate Dehydrogenase. Journal of Molecular Biology 429, 1396-1405.
Veronese FM, Mero A. 2008. The Impact of PEGylation on Biological Therapies. BioDrugs 22, 315-329. http://dx.doi.org/10.2165/00063030-200822050-00004.
Veronese FM, Pasut G. 2005. PEGylation, successful approach to drug delivery. Drug Discovery Today 10, 1451-1458.
Wagner-Rousset E, Janin-Bussat MC, Colas O, Excoffier M, Ayoub D, Haeuw JF, Rilatt I, Perez M, Corvaia N, Beck A. 2014. Antibody-drug conjugate model fast characterization by LC-MS following IdeS proteolytic digestion. MAbs, 6, 273-85. http://dx.doi.org/10.4161/mabs.26773.
Walsh G, Jefferis R. 2006. Post-translational modifications in the context of therapeutic proteins. Nature Biotechnology 24, 1241-52.
Wang F, Sambandan D, Halder R, Wang J, Batt SM, Weinrick B, Ahmad I, Yang P, Zhang Y, Kim J, Hassani M, Huszar S, Trefzer C, Ma Z, Kaneko T, Mdluli KE, Franzblau S, Chatterjee AK, Johnsson K, Mikusova K, Besra GS, Futterer K, Robbins SH, Barnes SW, Walker JR, Jacobs WR, Jr, Schultz PG. 2013. Identification of a small molecule with activity against drug-resistant and persistent tuberculosis. Proceedings of the National Academy of Sciences of the United States of America 110, E 2510-7. http://dx.doi.org/10.1073/pnas.1309171110.
Wang J, Zhang W, Song W, Wang Y, Yu Z, Li J, Wu M, Wang L, Zang J, Lin Q. 2010. A biosynthetic route to photoclick chemistry on proteins. Journal of the American Chemical Society 132, 14812-8.
Wang L, Schultz PG. 2004. Expanding the genetic code. Angewandte Chemie International Edition english 44, 34-66. http://dx.doi.org/10.1002/anie.200460627.
Wang L, Schultz PG. 2005. Expanding the Genetic
Code. Angewandte Chemie International Edition english 44, 34-66.
Wang Q, Chan TR, Hilgraf R, Fokin VV, Sharpless KB, Finn MG. 2003. Bioconjugation by copper(I)-catalyzed azide-alkyne [3 + 2] cycloaddition. Journal of the American Chemical Society 125, 3192-3. http://dx.doi.org/10.1021/ja021381e.
Wang ZU, Wang YS, Pai PJ, Russell WK, Russell DH, Liu WR. 2012. A facile method to synthesize histones with posttranslational modification mimics. Biochemistry 51, 5232-4. http://dx.doi.org/10.1021/bi300535a.
Weidner T, Castner DG. 2013. SFG analysis of surface bound proteins: a route towards structure determination. Physical Chemistry Chemical Physics 15, 12516-24.
Wiehler J, Jung G, Seebacher C, Zumbusch A, Steipe B. 2003. Mutagenic stabilization of the photocycle intermediate of green fluorescent protein (GFP). ChemBioChem 4, 1164-1171.
Wright TH, Vallee MR, Davis BG. 2016. From Chemical Mutagenesis to Post-Expression Mutagenesis: A 50 Year Odyssey. Angewandte Chemie International Edition english 55, 5896-903. http://dx.doi.org/10.1002/anie.201509310.
Wu BY, Hou SH, Huang L, Yin F, Zhao ZX, Anzai JI, Chen Q. 2008. Oriented immobilization of immunoglobulin G onto the cuvette surface of the resonant mirror biosensor through layer-by-layer assembly of multilayer films. Materials Science and Engineering: C 28, 1065-1069. http://dx.doi.org/10.1016/j.msec.2007.04.035.
Wu P, Shui W, Carlson BL, Hu N, Rabuka D, Lee J, Bertozzi CR. 2009. Site-specific chemical modification of recombinant proteins produced in mammalian cells by using the genetically encoded aldehyde tag. Proceedings of the National Academy of Sciences of the United States of America 106, 3000-5. http://dx.doi.org/10.1073/pnas.0807820106.
Wu Z, Guo Z. 2012. Sortase-Mediated Transpeptidation for Site-Specific Modification of Peptides, Glycopeptides, and Proteins. Journal of Carbohydrate Chemistry 31, 48-66.
Xiao H, Peters FB, Yang PY, Reed S, Chittuluru JR, Schultz PG. 2014. Genetic incorporation of histidine derivatives using an engineered pyrrolysyl-tRNA synthetase. ACS Chemical Biology 9, 1092-6. http://dx.doi.org/10.1021/cb500032c.
Xiao H, Wu R. 2017. Global and Site-Specific Analysis Revealing Unexpected and Extensive Protein S-GlcNAcylation in Human Cells. Analytical Chemistry 89, 3656-3663. http://dx.doi.org/10.1021/acs.analchem.6b05064.
Xue J, Shao N, Guo Z. 2003. First total synthesis of a GPI-anchored peptide. The Journal of Organic Chemistry 68, 4020-9.
You L, Cho EJ, Leavitt J, Ma LC, Montelione GT, Anslyn EV, Krug RM, Ellington A, Robertus JD. 2011. Synthesis and evaluation of quinoxaline derivatives as potential influenza NS1A protein inhibitors. Bioorganic & Medicinal Chemistry Letters 21, 3007-3011.
Yu S, Guo Z, Johnson C, Gu G, Wu Q. 2013. Recent progress in synthetic and biological studies of GPI anchors and GPI-anchored proteins. Current Opinion in Chemical Biology 17, 1006-13.
Yu SF, Zheng B, Go M, Lau J, Spencer S, Raab, H, Soriano R, Jhunjhunwala S, Cohen R, Caruso M, Polakis P, Flygare J, Polson AG. 2015. A Novel Anti-CD22 Anthracycline-Based Antibody-Drug Conjugate (ADC) That Overcomes Resistance to Auristatin-Based ADCs. Clinical Cancer Research 21, 3298-306. http://dx.doi.org/10.1158/1078-0432.CCR-14-2035.
Yuan Y, Liang G. 2014. A biocompatible, highly efficient click reaction and its applications. Organic & Biomolecular Chemistry 12, 865-871.
Zeng H, Xie J, Schultz PG. 2006. Genetic introduction of a diketone-containing amino acid into proteins. Bioorganic & Medicinal Chemistry Letters 16, 5356-9. http://dx.doi.org/10.1016/j.bmcl.2006.07.094.
Zhang FL, Casey PJ. 1996. Protein prenylation: molecular mechanisms and functional consequences. Annual Review of Biochemistry 65, 241-69. http://dx.doi.org/10.1146/annurev.bi.65.070196.001325.
Zhang X, He X. 2016. Methods for Studying Wnt Protein Modifications/Inactivations by Extracellular Enzymes, Tiki and Notum. Methods in Molecular Biology 1481, 29-38. http://dx.doi.org/10.1007/978-1-4939-6393-5_4.
Zhang Z, Smith BA, Wang L, Brock A, Cho C, Schultz PG. 2003. A new strategy for the site-specific modification of proteins in vivo. Biochemistry 42, 6735-46. http://dx.doi.org/10.1021/bi0300231.
Zioudrou C, Wilchek M, Patchornik A. 2002. Conversion of the L-Serine Residue to an L-Cysteine Residue in Peptides*. Biochemistry 4, 1811-1822. http://dx.doi.org/10.1021/bi00885a018
Fabrice Ndayisenga, Po-Han Lin, Runan Li, Abdul Hameed, Yue Zhang, Kamel Meguellati (2020), Site-specific modification of proteins by chemical/enzymatic strategies; IJB, V16, N3, March, P12-50
https://innspub.net/site-specific-modification-of-proteins-by-chemical-enzymatic-strategies/
Copyright © 2020
By Authors and International
Network for Natural Sciences
(INNSPUB) https://innspub.net
This article is published under the terms of the
Creative Commons Attribution License 4.0