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Publications

Highlights

  • 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., doi: 10.1038/s41467-02336797-2
  • Serfling R, Lorenz C, Etzel M, Schicht G, Böttke 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

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

 

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 T, Ernicke S, Serfling 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 R, Seidel 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 R, Seidel L, Böttke T, Coin 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 L, Coin 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 G, Böttke 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