Highlights

  • De Faveri C, Mattheisen J, Sakmar T, Coin I*. Noncanonical Amino Acid Tools and Their Application to Membrane Protein Studies; Chem Rev. (2024). doi: 10.1021/acs.chemrev.4c00181
  • Aydin Y, Böttke T, Lam JH, Ernicke S, Fortmann A, Tretbar M, Zarzycka B, Gurevich VV, Katritch V*, Coin I*. Structural details of a Class B GPCR - arrestin complex revealed by genetically encoded crosslinkers in living cells; Nat. Commun. (2023). doi: 10.1038/s41467-02336797-2
  • Serfling R, Lorenz C, Etzel M, Schicht GBöttke T, Mörl M, Coin I. Designer tRNAs for efficient incorporation of non-canonical amino acids by the pyrrolysine system in mammalian cells; Nucleic Acids Res. (2018). doi: 10.1093/nar/gkx1156
  • Seidel L, Zarzycka B, Zaidi SA, Katritch V, Coin I. Structural insight into the activation of a class B G-protein-coupled receptor by peptide hormones in live human cells. Elife (2017). doi: 10.7554/eLife.27711
  • Coin I, Katritch V, Sun T, Xiang Z, Siu FY, Beyermann M, Stevens RC, Wang L. Genetically encoded chemical probes in cells reveal the binding path of urocortin-I to CRF class B GPCR. Cell (2013). doi: 10.1016/j.cell.2013.11.008

2024

  • De Faveri C, Mattheisen J, Sakmar T, Coin I*. Noncanonical Amino Acid Tools and Their Application to Membrane Protein Studies; Chem Rev. (2024). doi: 10.1021/acs.chemrev.4c00181
  • Liao QQ, Shu X, Sun W, Mandapaka H, Xie F, Zhang Z, Dai T, Wang S, Zhao J, Jiang H, Zhang L, Lin J, Li SW, Coin I, Yang F, Peng J, Li K, Zhou F, Yang B. Capturing Protein-Protein Interactions with Acidic Amino Acids Reactive Cross-Linkers. Small (2024). doi: 10.1002/smll.202308383

2023

  • Coin I, Huster D. Ready for the sheet: β-strand folding of phosphorylation clusters guides GPCR binding to arrestin; Structure (2023). doi: 10.1016/j.str.2023.09.013
  • Ledwitch KV, Künze G, McKinney JR, Okwei E, Larochelle K, Pankewitz L, Ganguly S, Darling HL, Coin I, Meiler J. Sparse pseudocontact shift NMR data obtained from a non-canonical amino acid-linked lanthanide tag improves integral membrane protein structure prediction; J Biomol NMR (2023). doi: 10.1007/s10858-023-00412-9
  • Aydin Y, Böttke T, Lam JH, Ernicke S, Fortmann A, Tretbar M, Zarzycka B, Gurevich VV, Katritch V*, Coin I*. Structural details of a Class B GPCR - arrestin complex revealed by genetically encoded crosslinkers in living cells; Nat Commun (2023). doi: 10.1038/s41467-02336797-2
  • Shu X, Liao QQ, Li ST, Liu L, Zhang X, Zhou L, Zhang L, Coin I, Wang L, Wu H, Yang B. Detecting Active Deconjugating Enzymes with Genetically Encoded Activity-Based Ubiquitin and Ubiquitin-like Protein Probes. Anal Chem (2023). doi: 10.1021/acs.analchem.2c03270
  • Aydin Y, Coin I. Genetically encoded crosslinkers to address protein-protein interactions. Protein Sci (2023). doi: 10.1002/pro.4637 (Wiley Top Cited Article)

 

2021

  • Rudolf S, Kaempf K, Vu O, Meiler J, Beck-Sickinger AG, Coin I. Binding of Natural Peptide Ligands to the Neuropeptide Y5 Receptor. Angew Chem Int Ed Engl (2021). doi: 10.1002/anie.202108738
  • Aydin Y, Coin I. Biochemical Insights into Structure and Function of Arrestins. FEBS J (2021). doi: 10.1111/febs.15811
  • Işbilir A, Serfling R, Möller J, Thomas R, De Faveri C, Zabel U, Scarselli M, Beck-Sickinger AG, Bock A, Coin I, Lohse MJ, Annibale P. Determination of G-protein-coupled receptor oligomerization by molecular brightness analyses in single cells. Nat Protoc (2021). doi: 10.1038/s41596-020-00458-1

2020

  • Kaiser A, Coin I. Capturing Peptide-GPCR Interactions and Their Dynamics. Molecules (2020). doi: 10.3390/molecules25204724
  • Böttke TErnicke SSerfling R, Ihling C, Burda E, Gurevich VV, Sinz A, Coin I. Exploring GPCR-arrestin interfaces with genetically encoded crosslinkers. EMBO Rep (2020). doi: 10.15252/embr.202050437
  • Clark LJ, Krieger J, White AD, Bondarenko V, Lei S, Fang F, Lee JY, Doruker P, Böttke T, Jean-Alphonse F, Tang P, Gardella TJ, Xiao K, Sutkeviciute I, Coin I, Bahar I, Vilardaga JP. Allosteric interactions in the parathyroid hormone GPCR-arrestin complex formation. Nat Chem Biol (2020). doi: 10.1038/s41589-020-0567-0

2019

  • Serfling RSeidel L, Bock A, Lohse MJ, Annibale P and Coin I. Quantitative single-residue bioorthogonal labeling of G protein-coupled receptors in live cells. ACS Chem Bio (2019). doi: 10.1021/acschembio.8b01115
  • Seidel L, Zarzycka B, Katritch V, Coin I. Exploring Pairwise Chemical Crosslinking To Study Peptide-Receptor Interactions. Chembiochem (2019). doi: 10.1002/cbic.201800582

2018

  • Coin I. Application of non-canonical crosslinking amino acids to study protein-protein interactions in live cells. Curr Opin Chem Biol (2018). doi: 10.1016/j.cbpa.2018.07.019
  • Serfling RSeidel LBöttke TCoin I. Optimizing the Genetic Incorporation of Chemical Probes into GPCRs for Photo-crosslinking Mapping and Bioorthogonal Chemistry in Live Mammalian Cells. J Vis Exp (2018). doi: 10.3791/57069
  • Seidel LCoin I. Mapping of Protein Interfaces in Live Cells Using Genetically Encoded Crosslinkers. Methods Mol Biol (2018). doi: 10.1007/978-1-4939-7574-7_14
  • Serfling R, Lorenz C, Etzel M, Schicht GBöttke T, Mörl M, Coin I. Designer tRNAs for efficient incorporation of non-canonical amino acids by the pyrrolysine system in mammalian cells. Nucleic Acids Res (2018). doi: 10.1093/nar/gkx1156

2017

  • Seidel L, Zarzycka B, Zaidi SA, Katritch V, Coin I. Structural insight into the activation of a class B G-protein-coupled receptor by peptide hormones in live human cells. Elife (2017). doi: 10.7554/eLife.27711

2013

  • Coin I, Katritch V, Sun T, Xiang Z, Siu FY, Beyermann M, Stevens RC, Wang L. Genetically encoded chemical probes in cells reveal the binding path of urocortin-I to CRF class B GPCR. Cell (2013). doi: 10.1016/j.cell.2013.11.008
  • Kang JY, Kawaguchi D, Coin I, Xiang Z, O'Leary DD, Slesinger PA, Wang L. In vivo expression of a light-activatable potassium channel using unnatural amino acids. Neuron (2013). doi: 10.1016/j.neuron.2013.08.016
  • Xiang Z, Ren H, Hu YS, Coin I, Wei J, Cang H, Wang L. Adding an unnatural covalent bond to proteins through proximity-enhanced bioreactivity. Nat Methods (2013). doi: 10.1038/nmeth.2595

before 2013

  • Parrish AR, She X, Xiang Z, Coin I, Shen Z, Briggs SP, Dillin A, Wang L. Expanding the genetic code of Caenorhabditis elegans using bacterial aminoacyl-tRNA synthetase/tRNA pairs. ACS Chem Biol (2012). doi: 10.1021/cb200542j
  • Westendorf C, Schmidt A, Coin I, Furkert J, Ridelis I, Zampatis D, Rutz C, Wiesner B, Rosenthal W, Beyermann M, Schülein R. Inhibition of biosynthesis of human endothelin B receptor by the cyclodepsipeptide cotransin. J Biol Chem (2011). doi: 10.1074/jbc.M111.239244
  • Coin I, Perrin MH, Vale WW, Wang L. Photo-cross-linkers incorporated into G-protein-coupled receptors in mammalian cells: a ligand comparison. Angew Chem Int Ed Engl (2011). doi: 10.1002/anie.201102646
  • Coin I. The depsipeptide method for solid-phase synthesis of difficult peptides. J Pept Sci (2010). doi: 10.1002/psc.1224
  • Coin I, Schmieder P, Bienert M, Beyermann M. The depsipeptide technique for the solid phase peptide synthesis: from stepwise assembly to segment condensation. Adv Exp Med Biol (2009). doi: 10.1007/978-0-387-73657-0_56
  • Coin I, Beerbaum M, Schmieder P, Bienert M, Beyermann M. Solid-phase synthesis of a cyclodepsipeptide: cotransin. Org Lett (2008). doi: 10.1021/ol800855p
  • Coin I, Schmieder P, Bienert M, Beyermann M. The depsipeptide technique applied to peptide segment condensation: scope and limitations. J Pept Sci (2008). doi: 10.1002/psc.928
  • Coin I, Beyermann M, Bienert M. Solid-phase peptide synthesis: from standard procedures to the synthesis of difficult sequences. Nat Protoc (2007). doi: 10.1038/nprot.2007.454
  • Stella L, Burattini M, Mazzuca C, Palleschi A, Venanzi M, Coin I, Peggion C, Toniolo C, Pispisa B. Alamethicin interaction with lipid membranes: a spectroscopic study on synthetic analogues. Chem Biodivers (2007). doi: 10.1002/cbdv.200790111
  • Coin I, Dölling R, Krause E, Bienert M, Beyermann M, Sferdean CD, Carpino LA. Depsipeptide methodology for solid-phase peptide synthesis: circumventing side reactions and development of an automated technique via depsidipeptide units. J Org Chem (2006). doi: 10.1021/jo060914p
  • Peggion C, Coin I, Toniolo C. Total synthesis in solution of alamethicin F50/5 by an easily tunable segment condensation approach. Biopolymers (2004). doi: 10.1021/acschembio.8b01115