# Publications **Complete List of Published Work:** **Nramp-Family Transition Metal Transporters** J. A. Licht, S. P. Berry, M. A. Gutierrez, R. Gaudet (2024) They all rock: A systematic comparisonof conformational movements in LeuT-fold transporters. *Structure*. Epub 20240712. doi: 10.1016/j.str.2024.06.015. [PMID: 39025067](< 39025067>). S. Ray, R. Gaudet (2023) Structures and coordination chemistry of transporters involved in manganese and iron homeostasis. *Biochem Soc Trans*. **51**(3):897-923. doi: 10.1042/BST20210699. Review. [PMID: 37283482](https://pubmed.ncbi.nlm.nih.gov/37283482/); PMCID: [PMC10330786](https://pmc.ncbi.nlm.nih.gov/articles/PMC10330786/). S. Ray, S. P. Berry, E. A. Wilson, C. H. Zhang, M. Shekhar, A. Singharoy , R. Gaudet (2023) High-resolution structures with bound Mn(2+) and Cd(2+) map the metal import pathway inan Nramp transporter. *Elife*. **12**. Epub 20230411. doi: 10.7554/eLife.84006. [PMID: 37039477](https://pubmed.ncbi.nlm.nih.gov/37039477/); PMCID: [PMC10185341](https://pmc.ncbi.nlm.nih.gov/articles/PMC10185341/). R. B. Stockbridge, R. Gaudet, M. Grabe, D. L. Minor Jr. Inroads into Membrane Physiology through Transport Nanomachines (2021) *J Mol Biol* **433**, 167101. PMID: [34119492](https://pubmed.ncbi.nlm.nih.gov/34119492/). A.T. Bozzi, R. Gaudet (2021) Molecular Mechanism of Nramp-Family Transition Metal Transport. *J Mol Biol* **433**, 166991. PMID: [33865868](https://pubmed.ncbi.nlm.nih.gov/33865868/); PMCID: [PMC8292206](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8292206/). A.T. Bozzi, A.L. McCabe, B.C.Barnett, R. Gaudet (2020) Transmembrane helix 6b links proton- and metal-release pathways and drives conformational change in an Nramp-family transition metal transporter. *J Biol Chem*. **295**(5), 1212-1224. [PubMed: 31882536](https://www.ncbi.nlm.nih.gov/pubmed/31882536) [PMCID: PMC6996879](http://www.jbc.org/content/early/2019/12/27/jbc.RA119.011336) A.T. Bozzi, L.B. Bane, C.M. Zimanyi, R. Gaudet (2019) Unique structural features in an Nramp metal transporter impart substrate-specific proton cotransport and a kinetic bias to favor import. *J Gen Physiol*. 151(12):1413-1429. [PubMed: 31619456](https://www.ncbi.nlm.nih.gov/pubmed/31619456) [PMCID: PMC6888756](https://rupress.org/jgp/article/151/12/1413/132561/Unique-structural-features-in-an-Nramp-metal) A.T. Bozzi, C.M. Zimanyi, J.M. Nicoludis, B.K. Lee, C.H. Zhang, R. Gaudet (2019) Structures in multiple conformations reveal distinct transition metal and proton pathways in an Nramp transporter. *eLife* Epub 20190204. [PubMed: 30714568](https://www.ncbi.nlm.nih.gov/pubmed/30714568) PMCID: [PMC6398981](https://pmc.ncbi.nlm.nih.gov/articles/PMC6398981/). A.T. Bozzi, L.B. Bane, W.A. Weihofen, A. Singharoy, E.R. Guillen, H.L. Ploegh, K. Schulten, and R. Gaudet (2016) Crystal Structure and Conformational Change Mechanism of a Bacterial Nramp-Family Divalent Metal Transporter. Structure 24, 2102-2114. [PubMed: 27839948](https://www.ncbi.nlm.nih.gov/pubmed/?term=Crystal%20Structure%20and%20Conformational%20Change%20Mechanism%20of%20a%20Bacterial%20Nramp-Family%20Divalent%20Metal%20Transporter) [PMCID: PMC5143219](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5143219/) [PDB: 5KTE](http://www.rcsb.org/structure/5KTE) A. T. Bozzi, L. B. Bane, W. A. Weihofen, A. L. McCabe, A. Singharoy, C. J. Chipot, K. Schulten, and R. Gaudet (2016) Conserved methionine dictates substrate preference in Nramp-family divalent metal transporters. Proc. Natl Acad. Sci. USA 113, 10310-5. [PubMed: 27573840](https://www.ncbi.nlm.nih.gov/pubmed/?term=onserved%20methionine%20dictates%20substrate%20preference%20in%20Nramp-family%20divalent%20metal%20transporters) [PMCID: PMC5027461.](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5027461/) **Prodrug-Activating Peptidases** J. A. Velilla, M. R. Volpe, G. E. Kenney, R. M. Walsh Jr, E. P. Balskus, R. Gaudet (2023) Structural basis of colibactin activation by the ClbP peptidase. *Nat Chem Biol*. **19**(2):151-8. Epub 20221017. doi: 10.1038/s41589-022-01142-z. [PMID: 36253550](https://pubmed.ncbi.nlm.nih.gov/36253550/); [PMCID: PMC9889268](https://pmc.ncbi.nlm.nih.gov/articles/PMC9889268/). M. R. Volpe, J. A. Velilla, M. Daniel-Ivad, J. J. Yao, A. Stornetta, P .W. Villalta, H. C. Huang, D. A. Bachovchin, S. Balbo, R. Gaudet, E. P. Balskus (2023). A small molecule inhibitor prevents gut bacterial genotoxin production. *Nat Chem Biol.* **19**(2):159-67. Epub 20221017. doi: 10.1038/s41589-022-01147-8. [PMID: 36253549](https://pubmed.ncbi.nlm.nih.gov/36253549/); [PMCID: PMC9889270](https://pmc.ncbi.nlm.nih.gov/articles/PMC9889270/). J. A. Velilla, G. E. Kenney, R. Gaudet (2023) Structure and function of prodrug-activatingpeptidases. *Biochimie*. **205**:124-35. Epub 20221108. doi: 10.1016/j.biochi.2022.07.019. [PMID: 36803695](https://pubmed.ncbi.nlm.nih.gov/36803695/); [PMCID: PMC10030199](https://pmc.ncbi.nlm.nih.gov/articles/PMC10030199/). **Structural Studies of Sensory Receptors** È. Catalina-Hernández, M. López-Martín M, D. Mctasnou-Sánchez, M. Martins, V. A. Lorenz- Fonfria, F. Jiménez-Altayó, U. A. Hellmich, H Inada H, A. Alcaraz, Y. Furutani, A. Nonell-Canals, J. L. Vázquez-Ibar, C. Domene, R. Gaudet, A. Perálvarez-Marín (2024) Experimental and computational biophysics to identify vasodilator drugs targeted at TRPV2 using agonists based on the probenecid scaffold. *Comput Struct Biotechnol J.* Dec;23:473-482. doi: 10.1016/j.csbj.2023.12.028. PubMed [PMID: 38261868](https://pubmed.ncbi.nlm.nih.gov/38261868/); PubMed Central [PMCID: PMC10796807](https://pmc.ncbi.nlm.nih.gov/articles/PMC10796807/). S. H. Berth, L. Vo, D. H. Kwon, T. Grider, Y. S. Damayanti, G. Kosmanopoulos, A. Fox, A. R. Lau, P. Carr, J. K. Donohue, M. Hoke, S. Thomas, C. Karim, A. J. Fay, E. Meltzer, T. O. Crawford, R. Gaudet, M. E. Shy, U. A. Hellmich, S. Y. Lee, C. J. Sumner, B. A. McCray (2024) Combinedclinical, structural, and cellular studies discriminate pathogenic and benign TRPV4variants. *Brain*. Epub 20240718. doi: 10.1093/brain/awae243. [PMID: 39021275](https://pubmed.ncbi.nlm.nih.gov/39021275/) H. M. Frank, S. Walujkar, R. M. Walsh Jr, W. J. Laursen, D. L. Theobald, P. A. Garrity, R. Gaudet (2024) Structural basis of ligand specificity and channel activation in an insect gustatory receptor. *Cell Rep*. **43**(4):114035. Epub 20240403. doi: 10.1016/j.celrep.2024.114035. [PMID: 38573859](https://pubmed.ncbi.nlm.nih.gov/38573859/); [PMCID: PMC11100771](https://pmc.ncbi.nlm.nih.gov/articles/PMC11100771/). A. P. Koivisto, M. G. Belvisi, R. Gaudet, A. Szallasi (2022) Advances in TRP channel drug discovery: from target validation to clinical studies. *Nat Rev Drug Discov* **21**, 41-59. doi: 10.1038/s41573-021-00268-4. PMID: [34526696](https://pubmed.ncbi.nlm.nih.gov/34526696/); PMCID: [PMC8442523](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8442523/). L. Zhang, C. Simonsen, L. Zimova, K. Wang, L. Moparthi, R. Gaudet, M. Ekoff, G. Nilsson, U.A. Hellmich, V. Vlachova, P. Gourdon, P.M. Zygmunt (2022) Cannabinoid non-cannabidiol site modulation of TRPV2 structure and function. *Nat Commun* **13**, 7483. doi: 10.1038/s41467-022-35163-y. [PMID: 36470868](https://pubmed.ncbi.nlm.nih.gov/36470868/); [PMCID: PMC9722916](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9722916/). K.A. Skinner, J. S. Wzorek, D. Kahne, R. Gaudet (2021) Efficient and flexible synthesis of new photoactivatable propofol analogs. *Bioorg Med Chem Lett.* **39**:127927. Epub 20210309. doi: 10.1016/j.bmcl.2021.127927. [PMID: 33705906](https://pubmed.ncbi.nlm.nih.gov/33705906/) J. Velilla, M.M. Marchetti, A. Toth-Petroczy, C. Grosgogeat, A.H. Bennett, N. Carmichael, E. Estrella, B.T. Darras, N.Y. Frank, J. Krier, R. Gaudet, V.A. Gupta (2019)Homozygous TRPV4 mutation causes congenital distal spinal muscular atrophy and arthrogryposis. *Neurol Genet.* **5**(2):e312. Epub 20190307. doi: 10.1212/NXG.0000000000000312. [PMID: 31041394](https://pubmed.ncbi.nlm.nih.gov/31041394/); [PMCID: PMC6454305](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6454305/) R.K. Finol-Urdaneta, J.R. McArthur, M.P. Goldschen-Ohm, R. Gaudet, D. B. Tikhonov, B.S. Zhorov, R.J. French. Batrachotoxin acts as a stent to hold open homotetrameric prokaryotic voltage-gated sodium channels. Journal of General Physiology (2019) Feb 4;151(2):186-199. doi: 10.1085/jgp.201812278. Epub 2018 Dec 26. [PubMed: 30587506](https://www.ncbi.nlm.nih.gov/pubmed/30587506) [PMCID: PMC6363421](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6363421/) B. Goretzki, N.A. Glogowski, E. Diehl, E. Duchardt-Ferner, C. Hacker, R. Gaudet, U.A. Hellmich (2018) Structural Basis of TRPV4 N Terminus Interaction with Syndapin/PACSIN1-3 and PIP2. *Structure*, Dec 4;26(12):1583-1593.e5. DOI: [10.1016/j.str.2018.08.002](https://doi.org/10.1016/j.str.2018.08.002) [PubMed: 30244966](https://www.ncbi.nlm.nih.gov/pubmed/30244966) K. Woll, K. Skinner, E. Gianti, N. Bhanu, B. Garcia, V. Carnevale, R. Eckenhoff, and R. Gaudet (2017) Sites Contributing to TRPA1 Activation by the Anesthetic Propofol Identified by Photoaffinity Labeling. *Biophysical Journal,* Nov 21; 113(10): 2168–2172. doi: [10.1016/j.bpj.2017.08.040](https://dx.doi.org/10.1016/j.bpj.2017.08.040) PMID: [28935134](https://www.ncbi.nlm.nih.gov/pubmed/28935134) M.S.J. Brewster and R. Gaudet (2015) How the TRPA1 receptor transmits painful stimuli: Inner workings revealed by electron cryomicroscopy. *BioEssays* **37**, 1184-1192. [PubMed: 26387779](https://www.ncbi.nlm.nih.gov/pubmed/?term=How%20the%20TRPA1%20receptor%20transmits%20painful%20stimuli:%20Inner%20workings%20revealed%20by%20electron%20cryomicroscopy) [PMCID: PMC4862669](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4862669/) Z.A. Knecht, R. Gaudet, and P.A. Garrity (2015) The Touching Tail of a Mechanotransduction Channel. *Cell* **162**, 1214-6. [PubMed: 26359983](https://www.ncbi.nlm.nih.gov/pubmed/?term=The%20Touching%20Tail%20of%20a%20Mechanotransduction%20Channel) R. Gaudet, B. Roux, and D. L. Minor Jr. (2015) Insights into the molecular foundations of electrical excitation. *J Mol Biol.* **427**, 1-2. [PubMed: 25542854](https://www.ncbi.nlm.nih.gov/pubmed/?term=Insights%20into%20the%20molecular%20foundations%20of%20electrical%20excitation) [PMCID: PMC5544904](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5544904/) U.A. Hellmich, and R. Gaudet (2014) High-resolution views of TRPV1 and their implications for the TRP channel superfamily. *Handb Exp Pharmacol.* **223**, 991-1004. [PubMed: 24961977](https://www.ncbi.nlm.nih.gov/pubmed/?term=High-resolution%20views%20of%20TRPV1%20and%20their%20implications%20for%20the%20TRP%20channel%20superfamily) [PMCID: PMC5075239](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5075239/) U.A. Hellmich, and R. Gaudet (2014) Structural Biology of TRP Channels. *Handb Exp Pharmacol.* **223**, 963-90. [PubMed: 24961976](https://www.ncbi.nlm.nih.gov/pubmed/24961976) [PMCID: PMC5075240](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5075240/) J. M. Sullivan, C. M. Zimanyi, W. Aisenberg, B. Bears, D.-H. Chen, J. W. Day, T. D. Bird, C. E. Siskind, R. Gaudet, and C. J. Sumner (2015) Novel mutations highlight the key role of the ankyrin repeat domain in TRPV4-mediated neuropathy. *Neurology Genetics*, **1**, e29. [PubMed: 27066566](https://www.ncbi.nlm.nih.gov/pubmed/?term=PMC4811381) [PMCID: PMC4811381](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4811381/) J. M. Sullivan, G. Landouré, R. Gaudet, C. Sumner. WriteClick: Phenotypic spectrum and incidence of TRPV4 mutations in patients with Inherited axonal neuropathy. Neurology (2014) 83, 1991. [PubMed: 25404646](https://www.ncbi.nlm.nih.gov/pubmed/25404646) A. Garcia-Elias, S. Mrkonjic, C. Pardo-Pastor, H. Inada, U. A. Hellmich, F. Rubio-Moscardó, C. Plata, R. Gaudet, R. Vicente, M. A. Valverde. Phosphatidylinositol-4,5-biphosphate-dependent rearrangement of TRPV4 cytosolic tails enables channel activation by physiological stimuli. Proc. Natl Acad. Sci. USA (2013) 110, 9553-9558. [PubMed: 23690576](https://www.ncbi.nlm.nih.gov/pubmed/?term=Phosphatidylinositol-4,5-biphosphate-dependent%20rearrangement%20of%20TRPV4%20cytosolic%20tails%20enables%20channel%20activation%20by%20physiological%20stimuli.) [PMCID: PMC3677448](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3677448/). A. Perálvarez-Marín, P. Doñate-Macian, and R. Gaudet (2013) What do we know about the transient receptor potential vanilloid 2 (TRPV2) ion channel? *FEBS J.* **280**, 5471-87. [PubMed: 23615321](https://www.ncbi.nlm.nih.gov/pubmed/?term=PMC3783526) [PMCID: PMC3783526](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3783526/) S.Y. Lau, E. Procko, and R. Gaudet (2012) Distinct properties of Ca2+–calmodulin binding to N- and C-terminal regulatory regions of the TRPV1 channel. Journal of General Physiology 140, 541-555. [PubMed: 23109716](https://www.ncbi.nlm.nih.gov/pubmed/?term=Distinct%20properties%20of%20Ca2+%E2%80%93calmodulin%20binding%20to%20N-%20and%20C-terminal%20regulatory%20regions%20of%20the%20TRPV1%20channel) [PMCID: PMC3483115](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3483115/) [PDB: 3SUI](http://www.pdb.org/pdb/explore/explore.do?structureId=3SUI) H. Inada, E. Procko, M. Sotomayor and R. Gaudet. Structural and Biochemical Consequences of Disease-Causing Mutations in the Ankyrin Repeat Domain of the Human TRPV4 Channel. Biochemistry (2012) 51: 6195-206. [PubMed: 22702953](https://www.ncbi.nlm.nih.gov/pubmed/22702953) [PMCID: PMC3413242](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3413242/) PDB: [4DX1](http://www.pdb.org/pdb/explore/explore.do?structureId=4DX1) [4DX2](http://www.pdb.org/pdb/explore/explore.do?structureId=4DX2) G. Landouré, J. M. Sullivan, J. O. Johnson, C. H. Munns, Y. Shi, O. Diallo, J. R. Gibbs, R. Gaudet, C. L Ludlow, K. H. Fischbeck, B. J. Traynor, B. G. Burnett and C. J. Sumner. Exome sequencing identifies a novel TRPV4 mutation in a CMT2C family. Neurology (2012) 79: 192-4. [PubMed: 22675077](https://www.ncbi.nlm.nih.gov/pubmed/?term=Exome%20sequencing%20identifies%20a%20novel%20TRPV4%20mutation%20in%20a%20CMT2C%20family) [PMCID: PMC3390542](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3390542/) M. Zimon, J. Baets, M. Auer-Grumbach, J. Berciano, A. Garcia, E. Lopez-Laso, L. Merlini, D. Hilton-Jones, M. McEntagart, A. H. Crosby, N. Barisic, E. Boltshauser, C. E. Shaw, G. Landouré, C. L. Ludlow, R. Gaudet, H. Houlden, M. M. Reilly, K. H. Fischbeck, C. J. Sumner, V. Timmerman, A. Jordanova and P. De Jonghe. Dominant mutations in the cation channel gene transient receptor potential vanilloid 4 cause an unusual spectrum of neuropathies. Brain (2010) 133: 1798-809. [PubMed: 20460441](https://www.ncbi.nlm.nih.gov/pubmed/?term=Dominant%20mutations%20in%20the%20cation%20channel%20gene%20transient%20receptor%20potential%20vanilloid%204%20cause%20an%20unusual%20spectrum%20of%20neuropathies) [PMCID: PMC2912694](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2912694/) G. Landouré, A.A. Zdebik, T.L. Martinez, B.G. Burnett, H.C. Stanescu, H. Inada, Y. Shi, A.A Taye, L. Kong, C.H Munns, S.S. Choo, C.B. Phelps, R. Paudel, H. Houlden, C.L. Ludlow1, M.J. Caterina, R. Gaudet, R. Kleta, K.H. Fischbeck and C.J. Sumner. Mutations in TRPV4 cause Charcot-Marie-Tooth disease type 2C. Nature Genetics (2010) 42: 170-4. [PubMed: 20037586](https://www.ncbi.nlm.nih.gov/pubmed/20037586) [PMCID: PMC2812627](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2812627/) PDB: [3JXI](http://www.pdb.org/pdb/explore/explore.do?structureId=3JXI) [3JXJ](http://www.pdb.org/pdb/explore/explore.do?structureId=3JXJ) C.B. Phelps, R.R. Wang, S.S. Choo and R. Gaudet. Differential regulation of TRPV1, TRPV3 AND TRPV4 sensitivity through a conserved binding site on the ankyrin repeat domain. J. Biol. Chem. (2010) 285: 731-40. [PubMed: 19864432](https://www.ncbi.nlm.nih.gov/pubmed/?term=Differential%20regulation%20of%20TRPV1,%20TRPV3%20AND%20TRPV4%20sensitivity%20through%20a%20conserved%20binding%20site%20on%20the%20ankyrin%20repeat%20domain) [PMCID: PMC2804222](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2804222/) R. Gaudet. Divide and conquer: high resolution structural information on TRP channel fragments. J Gen Physiol. (2009) 133: 231-7. [PubMed:19237587](https://www.ncbi.nlm.nih.gov/pubmed/?term=Divide%20and%20conquer:%20high%20resolution%20structural%20information%20on%20TRP%20channel%20fragments) [PMCID: PMC2654082](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2654082/) R. Gaudet. A primer on ankyrin repeat function in TRP channels and beyond. Mol Biosyst. (2008) 4: 372-9. Epub 2008 Mar 26. Review. [PubMed:18414734](https://www.ncbi.nlm.nih.gov/pubmed/?term=A%20primer%20on%20ankyrin%20repeat%20function%20in%20TRP%20channels%20and%20beyond) [PMCID: PMC3006086](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3006086/) R. Gaudet. TRP channels entering the structural era. J Physiol. (2008) 586: 3565-75. Epub 2008 Jun 5. Review. [PubMed:18535090](https://www.ncbi.nlm.nih.gov/pubmed/?term=TRP%20channels%20entering%20the%20structural%20era.) PMCID: [PMC2538826](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2538826/) C.B. Phelps, R.J. Huang, P.V. Lishko, R.R. Wang and R. Gaudet. Structural analyses of the Ankyrin Repeat Domain of TRPV6 and related TRPV ion channels. Biochemistry (2008) 47: 2476-2484. [PubMed](http://www.ncbi.nlm.nih.gov/pubmed/18232717?ordinalpos=10&itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_DefaultReportPanel.Pubmed_RVDocSum) [2RFA](http://www.pdb.org/pdb/explore.do?structureId=2RFA) C.B. Phelps and R. Gaudet The Role of the N-Terminus and Transmembrane Domain of TRPM8 in Channel Localization and Tetramerization. Journal of Biological Chemistry (2007) 282: 36474-80. [PubMed: 17908685](https://www.ncbi.nlm.nih.gov/pubmed/?term=The%20Role%20of%20the%20N-Terminus%20and%20Transmembrane%20Domain%20of%20TRPM8%20in%20Channel%20Localization%20and%20Tetramerization) C.B. Phelps, E. Procko, P.V. Lishko, R.R. Wang and R. Gaudet Insights into the roles of conserved and divergent residues in the ankyrin repeats of TRPV ion channels. Channels (2007) 1: 148-51. Epub 2007 Jul 9. [PubMed: 18690026](https://www.ncbi.nlm.nih.gov/pubmed/?term=Insights%20into%20the%20roles%20of%20conserved%20and%20divergent%20residues%20in%20the%20ankyrin%20repeats%20of%20TRPV%20ion%20channels) P.V. Lishko, E. Procko, X. Jin, C.B. Phelps and R. Gaudet The ankyrin repeats of TRPV1 bind multiple ligands and modulate channel sensitivity. Neuron (2007) 54: 905-918. [PubMed: 17582331](https://www.ncbi.nlm.nih.gov/pubmed/?term=The%20ankyrin%20repeats%20of%20TRPV1%20bind%20multiple%20ligands%20and%20modulate%20channel%20sensitivity) PDB: [2PNN](http://www.pdb.org/pdb/explore.do?structureId=2PNN) [2NYJ](http://www.pdb.org/pdb/explore.do?structureId=2NYJ) R. Gaudet Structural Insights into the Function of TRP Channels TRP Ion Channel Function in Sensory Transduction and Cellular Signaling Cascades, W. Liedtke, and S. Heller, eds. (Boca Raton, FL: CRC Press 2007), pp. 349-359. [PubMed: 21204513](https://www.ncbi.nlm.nih.gov/pubmed/?term=Structural%20Insights%20into%20the%20Function%20of%20TRP%20Channels%20TRP%20Ion%20Channel%20Function%20in%20Sensory%20Transduction%20and%20Cellular%20Signaling%20Cascades) X. Jin, J. Touhey and R. Gaudet Structure of the N-terminal ankyrin repeat domain of the TRPV2 ion channel. J. Biol. Chem. (2006) 281: 25006-10. [PubMed: 16809337](https://www.ncbi.nlm.nih.gov/pubmed/16809337) PDB: [2ETA](http://www.pdb.org/pdb/explore.do?structureId=2ETA) [2ETB](http://www.pdb.org/pdb/explore.do?structureId=2ETB) [2ETC](http://www.pdb.org/pdb/explore.do?structureId=2ETC) **Structural Studies of ABC Transporters** S. Srikant, R. Gaudet, A. W. Murray (2023) Extending the reach of homology by usingsuccessive computational filters to find yeast pheromone genes. *Curr Biol*. **33**(19):4098-110 e3. Epub 20230911. doi: 10.1016/j.cub.2023.08.039. [PMID: 37699395](https://pubmed.ncbi.nlm.nih.gov/37699395/); [PMCID: PMC10592104](https://pmc.ncbi.nlm.nih.gov/articles/PMC10592104/). C. Thomas, S.G Aller, K. Beis, E.P. Carpenter, G. Chang, L. Chen, E. Dassa, M. Dean, F. Duong Van Hoa, D. Ekiert, R. Ford, R. Gaudet, X. Gong, I.B. Holland, Y. Huang, D.K. Kahne, H. Kato, V. Koronakis, C.M. Koth, Y. Lee, O. Lewinson, R. Lill, E. Martinoia, S. Murakami, H.W. Pinkett, B. Poolman, D. Rosenbaum, B. Sarkadi, L. Schmitt, E. Schneider, Y. Shi, S.L. Shyng, D.J. Slotboom, E. Tajkhorshid, D.P. Tieleman, K. Ueda, A. Váradi, P.C. Wen, N. Yan, P. Zhang, H. Zheng, J. Zimmer, R. Tampé (2020) Structural and functional diversity calls for a new classification of ABC transporters. *FEBS Lett* **594**, 3767-3775. PMID: [32978974](https://pubmed.ncbi.nlm.nih.gov/32978974/). S. Srikant, R. Gaudet, A.W. Murray (2020) Selecting for Altered Substrate Specificity Reveals the Evolutionary Flexibility of ATP-Binding Cassette Transporters. *Curr Biol* **30**, 1689-1702.e6. doi: 10.1016/j.cub.2020.02.077. PMID: [32220325](https://pubmed.ncbi.nlm.nih.gov/32220325/); PMCID: [PMC7243462](http://www.ncbi.nlm.nih.gov/pmc/articles/pmc7243462/). S. Srikant, R.Gaudet (2019) Mechanics and pharmacology of substrate selection and transport by eukaryotic ABC exporters. Nat Struct Mol Biol. **26**(9):792-801. [PubMed: 31451804](https://www.ncbi.nlm.nih.gov/pubmed/31451804) [PMCID: PMC6822692](https://www.nature.com/articles/s41594-019-0280-4) A.S. Vakkasoglu, S. Srikant, and R. Gaudet (2017) D-helix influences dimerization of the ATP-binding cassette (ABC) transporter associated with antigen processing 1 (TAP1) nucleotide-binding domain. *PLoS One* **12**:e0178238. [PubMed: 28542489](https://www.ncbi.nlm.nih.gov/pubmed/?term=D-helix%20influences%20dimerization%20of%20the%20ATP-binding%20cassette%20(ABC)%20transporter%20associated%20with%20antigen%20processing%201%20(TAP1)%20nucleotide-binding%20domain) [PMCID: PMC5441636](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5441636/). N. Grossmann, A. S. Vakkasoglu, S. Hulpke, R. Abele, R. Gaudet\*, R. Tampé\* Mechanistic determinants of the directionality and energetics of active export by a heterodimeric ABC transporter. Nature Communications (2014) 5, 5419. [PubMed: 25377891](https://www.ncbi.nlm.nih.gov/pubmed/?term=Mechanistic%20determinants%20of%20the%20directionality%20and%20energetics%20of%20active%20export%20by%20a%20heterodimeric%20ABC%20transporter) [PMCID: PMC4242082](https://www.ncbi.nlm.nih.gov/pubmed/?term=PMC4242082.) E. Procko and R. Gaudet. Antigen processing and presentation: TAPping into ABC transporters. Curr Opin Immunol. (2009) 21: 84-91. Epub 2009 Mar 2. [PubMed: 19261456](https://www.ncbi.nlm.nih.gov/pubmed/?term=Antigen%20processing%20and%20presentation:%20TAPping%20into%20ABC%20transporters) E. Procko, M.L. O'Mara, W.F. Bennett, D.P. Tieleman and R. Gaudet. The mechanism of ABC transporters: general lessons from structural and functional studies of an antigenic peptide transporter. FASEB Journal. (2009) 23: 1287-302. Epub 2009 Jan 27. [PubMed: 19174475](https://www.ncbi.nlm.nih.gov/pubmed/?term=The%20mechanism%20of%20ABC%20transporters:%20general%20lessons%20from%20structural%20and%20functional%20studies%20of%20an%20antigenic%20peptide%20transporter.) R. Gaudet. The ABCs of trans(porter) inhibition. Nat Chem Biol. (2008) 4: 454-5. [PubMed:18641624](https://www.ncbi.nlm.nih.gov/pubmed/?term=The%20ABCs%20of%20trans(porter)%20inhibition) E. Procko and R. Gaudet. Functionally important interactions between the nucleotide-binding domains of an antigenic peptide transporter. Biochemistry. (2008) 47: 5699-708. Epub 2008 May 2. [PubMed: 18452308](https://www.ncbi.nlm.nih.gov/pubmed/?term=Functionally%20important%20interactions%20between%20the%20nucleotide-binding%20domains%20of%20an%20antigenic%20peptide%20transporter) E. Procko, I. Ferrin-O'Connell, S-.L. Ng and R. Gaudet. Distinct structural and functional properties of the ATPase sites in an asymmetric ABC transporter. Mol Cell. (2006) 24: 51-62. [PubMed](http://www.ncbi.nlm.nih.gov/pubmed/17018292?ordinalpos=16&itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_DefaultReportPanel.Pubmed_RVDocSum) [2IXE](http://www.pdb.org/pdb/explore.do?structureId=2IXE) [2IXF](http://www.pdb.org/pdb/explore.do?structureId=2IXF) [2IXG](http://www.pdb.org/pdb/explore.do?structureId=2IXG) E. Procko, G. Raghuraman, D.C. Wiley, M. Raghavan and R. Gaudet. Identification of domain boundaries within the N-termini of TAP1 and TAP2 and their importance in tapasin binding and tapasin-mediated increase in peptide loading of MHC class I. Immunol. Cell. Biol. (2005) 83: 475-482. [PubMed](http://www.ncbi.nlm.nih.gov/pubmed/16174096?ordinalpos=18&itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_DefaultReportPanel.Pubmed_RVDocSum) R. Gaudet and D.C. Wiley. Structure of the ABC ATPase domain of human TAP1, the transporter associated with antigen processing. EMBO J. (2001) 20: 4964-4972. [PubMed](http://www.ncbi.nlm.nih.gov/pubmed/11532960?ordinalpos=24&itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_DefaultReportPanel.Pubmed_RVDocSum) [1JJ7](http://www.pdb.org/pdb/explore.do?structureId=1JJ7) **Cadherins Superfamily Neuronal Development of Hearing and Deafness** J.M.Nicoludis, A.G.Green, S.Walujkar, E.J.May, M.Sotomayor, D.S.Marks, R.Gaudet (2019) Interaction specificity of clustered protocadherins inferred from sequence covariation and structural analysis. Proc Natl Acad Sci USA. **116**(36):17825-17830. [PubMed: 31431536](https://www.ncbi.nlm.nih.gov/pubmed/31431536) [PMCID: PMC6731663](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6731663/) R.E. Powers, R. Gaudet\*, and M. Sotomayor\* A Partial Calcium-Free Linker Confers Flexibility to Inner-Ear Protocadherin-15. Structure (2017) 25:482-495. [PubMed: 28238533](https://www.ncbi.nlm.nih.gov/pubmed/?term=A%20Partial%20Calcium-Free%20Linker%20Confers%20Flexibility%20to%20Inner-Ear%20Protocadherin-15) [PMCID: PMC5363953](https://www.ncbi.nlm.nih.gov/pubmed/?term=PMC5363953) PDB: [5T4M](https://www.rcsb.org/structure/5t4m) [5T4N](https://www.rcsb.org/structure/5T4N) J. M. Nicoludis, B. E. Vogt, A. G. Green, C. P. Schärfe, D. S. Marks, and R. Gaudet Antiparallel protocadherin homodimers use distinct affinity- and specificity-mediating regions in cadherin repeats 1-4. Elife. (2016) 5. pii, e18449. [PubMed: 27472898](https://www.ncbi.nlm.nih.gov/pubmed/?term=Antiparallel%20protocadherin%20homodimers%20use%20distinct%20affinity-%20and%20specificity-mediating%20regions%20in%20cadherin%20repeats%201-4) [PMCID: PMC5001838](https://www.ncbi.nlm.nih.gov/pubmed/?term=PMC5001838) [PDB: 5K8R](https://www.rcsb.org/structure/5k8r) J. M. Nicoludis, S.-Y. Lau, C. P. I. Schärfe, D. S. Marks, W. A. Weihofen, and R. Gaudet Structure and Sequence Analyses of Clustered Protocadherins Reveal Antiparallel Interactions that mediate homophilic specificity. Structure (2015) 23, 2087-2096. [PubMed: 26481813](https://www.ncbi.nlm.nih.gov/pubmed?term=structure%20and%20sequence%20analyses%20of%20clustered%20protocadherin%20reveal%20antiparallel%20interactions%20that%20mediate%20homophilic%20specificity&cmd=correctspelling) [PMCID: PMC4635037](https://www.ncbi.nlm.nih.gov/pubmed/?term=PMC4635037) PDB: [4Z18](https://www.rcsb.org/structure/4z18) [4Z19](https://www.rcsb.org/structure/4z19) M. Sotomayor, R. Gaudet, and D. P. Corey (2014) Sorting out a promiscuous superfamily: towards cadherin connectomics. *Trends Cell Biol.* **24**, 524-36. [PubMed: 24794279](https://www.ncbi.nlm.nih.gov/pubmed/?term=PMC4294768) [PMCID: PMC4294768](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4294768/) R. Geng, M. Sotomayor, K. J. Kinder, S. R. Gopal, J. Gerka-Stuyt, D. H. Chen, R. E. Hardisty-Hughes, G. Ball, A. Parker, R. Gaudet, D. Furness, S. D. Brown, D. P. Corey, and K. N. Alagramam. Noddy, a mouse harboring a missense mutation in protocadherin-15, reveals the impact of disrupting a critical interaction site between tip-link cadherins in inner ear hair cells. Journal of Neuroscience (2013) 33, 4395-4404. [PubMed: 23467356](https://www.ncbi.nlm.nih.gov/pubmed/?term=Noddy,%20a%20mouse%20harboring%20a%20missense%20mutation%20in%20protocadherin-15,%20reveals%20the%20impact%20of%20disrupting%20a%20critical%20interaction%20site%20between%20tip-link%20cadherins%20in%20inner%20ear%20hair%20cells.) [PMCID: PMC3618968](https://www.ncbi.nlm.nih.gov/pubmed/?term=PMC3618968) M. Sotomayor, W.A. Weihofen, R. Gaudet and D.P. Corey. Structure of a force-conveying cadherin bond essential for inner-ear mechanotransduction. Nature (2012) Published online 2012-11-07. doi:10.1038/nature11590 [PubMed: 23135401](https://www.ncbi.nlm.nih.gov/pubmed/?term=Structure%20of%20a%20force-conveying%20cadherin%20bond%20essential%20for%20inner-ear%20mechanotransduction.) [PMCID: PMC3518760](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3518760/) [4APX](http://www.pdb.org/pdb/explore.do?structureId=4APX) [4AXW](http://www.pdb.org/pdb/explore.do?structureId=4AXW) [4AQ8](http://www.pdb.org/pdb/explore.do?structureId=4AQ8) [4AQA](http://www.pdb.org/pdb/explore.do?structureId=4AQA) [4AQE](http://www.pdb.org/pdb/explore.do?structureId=4AQE) M. Sotomayor, W.A. Weihofen, R. Gaudet and D.P. Corey. Structural Determinants of Cadherin-23 Function in Hearing and Deafness. Neuron (2010) 66: 85-100. [PubMed: 20399731](https://www.ncbi.nlm.nih.gov/pubmed/?term=Structural%20Determinants%20of%20Cadherin-23%20Function%20in%20Hearing%20and%20Deafness) [PMCID: PMC2948466](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2948466/) [2WBX](http://www.pdb.org/pdb/explore.do?structureId=2WBX) [2WCP](http://www.pdb.org/pdb/explore.do?structureId=2WCP) [2WHV](http://www.pdb.org/pdb/explore.do?structureId=2WHV) [2WD0](http://www.pdb.org/pdb/explore.do?structureId=2WD0) **Ubiquitylation Pathways** K. Artavanis-Tsakonas, W.A. Weihofen, J.M. Antos, B.I. Coleman, C.A. Comeaux, M.T. Duraisingh, R. Gaudet and H.L. Ploegh. Characterization and structural studies of the Plasmodium falciparum ubiquitin and NEDD8 hydrolase UCHL3. J. Biol. Chem. (2010) 285: 6857-66. [PubMed](http://www.ncbi.nlm.nih.gov/pubmed/20042598?itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_RVDocSum&ordinalpos=1) [2WDT](http://www.pdb.org/pdb/explore.do?structureId=2WDT) [2WE6](http://www.pdb.org/pdb/explore.do?structureId=2WE6) C. Schlieker, W.A. Weihofen, E. Frijns, L.M. Kattenhorn, R. Gaudet and H.L. Ploegh. Structure of a herpesvirus-encoded cysteine protease reveals a unique class of deubiquitinating enzymes. Mol Cell. (2007) 25: 677-87. [PubMed](http://www.ncbi.nlm.nih.gov/pubmed/17349955?ordinalpos=15&itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_DefaultReportPanel.Pubmed_RVDocSum) [2J7Q](http://www.pdb.org/pdb/explore.do?structureId=2J7Q) S. Misaghi, P.J. Galardy, W.J. N. Meester, H. Ovaa, H.L. Ploegh and R. Gaudet. Structure of the ubiquitin hydrolase UCH-L3 complexed with a suicide substrate. J. Biol. Chem. (2005) 280: 1512-1520. [PubMed](http://www.ncbi.nlm.nih.gov/pubmed/15531586?ordinalpos=19&itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_DefaultReportPanel.Pubmed_RVDocSum) [1XD3](http://www.pdb.org/pdb/explore.do?structureId=1XD3) **Phosducin Regulation of G Protein Signaling** M. Obin, B.Y. Lee, C. Thulin, G. Meinke, A. Bohm, R.H. Lee, R. Gaudet, J.A. Hopp, V.Y. Arshavsky, B.M. Willardson and A. Taylor. Ubiquitylation of Transducin (T) subunits: Regulation by Phosducin. J. Biol. Chem. (2002) 277: 44566-44575. [PubMed: 12215439](https://www.ncbi.nlm.nih.gov/pubmed/?term=Ubiquitylation%20of%20Transducin%20(T)%20subunits:%20Regulation%20by%20Phosducin) R. Gaudet, J.R. Savage, J.N. McLaughlin, B.M. Willardson and P.B. Sigler. A molecular mechanism for the phosphorylation-dependent regulation of heterotrimeric G Proteins by phosducin. Mol. Cell (1999) 3: 649-660. [PubMed: 10360181](https://www.ncbi.nlm.nih.gov/pubmed/?term=A%20molecular%20mechanism%20for%20the%20phosphorylation-dependent%20regulation%20of%20heterotrimeric%20G%20Proteins%20by%20phosducin.) [1B9X](http://www.pdb.org/pdb/explore.do?structureId=1B9X) [1B9Y](http://www.pdb.org/pdb/explore.do?structureId=1B9Y) A. Bohm, R. Gaudet and P.B. Sigler. Structural aspects of heterotrimeric G-protein signaling. Curr. Opin. Biotechnol. (1997) 8: 480-487. [PubMed: 9265729](https://www.ncbi.nlm.nih.gov/pubmed/9265729) R. Gaudet, A. Bohm and P.B. Sigler. Crystal structure at 2.4 Å resolution of the complex of transducin bg and its regulator, phosducin. Cell (1996) 87: 577-588. [PubMed: 8898209](https://www.ncbi.nlm.nih.gov/pubmed/8898209?ordinalpos=38&itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_DefaultReportPanel.Pubmed_RVDocSum) [2TRC](http://www.pdb.org/pdb/explore.do?structureId=2TRC) **Additional Works** H.R. Foster, X. Lin, S. Srikant, R.R. Cueny, T.G. Falbel, J.L. Keck, R. Gaudet, B.M. Burton (2022) Natural Transformation Protein ComFA Exhibits Single-Stranded DNA Translocase Activity. *J Bacteriol* **204**, e0051821. doi: 10.1128/JB.00518-21. Epub 2022 Jan 18. [PMID: 35041498](https://pubmed.ncbi.nlm.nih.gov/35041498/); [PMCID: PMC8923215](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8923215/). Thomas C, Aller SG, Beis K, Carpenter EP, Chang G, Chen L, Dassa E, Dean M, Duong Van Hoa F, Ekiert D, Ford R, Gaudet R, Gong X, Holland IB, Huang Y, Kahne DK, Kato H, Koronakis V, Koth CM, Lee Y, Lewinson O, Lill R, Martinoia E, Murakami S, Pinkett HW, Poolman B, Rosenbaum D, Sarkadi B, Schmitt L, Schneider E, Shi Y, Shyng SL, Slotboom DJ, Tajkhorshid E, Tieleman DP, Ueda K, Váradi A, Wen PC, Yan N, Zhang P, Zheng H, Zimmer J, Tampé R. [Structural and functional diversity calls for a new classification of ABC transporters. ](https://www.ncbi.nlm.nih.gov/pubmed/32978974/)FEBS Lett. 2020 Dec;594(23):3767-3775. doi: 10.1002/1873-3468.13935. Epub 2020 Oct 26. Review. PubMed [PMID: 32978974](https://pubmed.ncbi.nlm.nih.gov/32978974/). J.M. Sullivan, W.W. Motley, J.O. Johnson, W.H. Aisenberg, K.L. Marshall, K.E. Barwick, L. Kong, J.S. Huh, P.C. Saavedra-Rivera, M.M. McEntagart, M.H. Marion, L.A. Hicklin, H. Modarres, E.L. Baple, M.H. Farah, A.R. Zuberi, C.M. Lutz, R. Gaudet, B.J. Traynor, A.H. Crosby, C.J. Sumner (2020) Dominant mutations of the Notch ligand Jagged1 cause peripheral neuropathy. *J Clin Invest* **130**, 1506-1512. doi: 10.1172/JCI128152. PMID: [32065591](https://pubmed.ncbi.nlm.nih.gov/32065591/); PMCID: [PMC7269582](http://www.ncbi.nlm.nih.gov/pmc/articles/pmc7269582/). R.L.Policarpo, L.Decultot, E.May, P.Kuzmič, S.Carlson, D.Huang, V.Chu, B.A.Wright, S.Dhakshinamoorthy, A.Kannt, S.Rani, S.Dittakavi, J,D.Panarese, R.Gaudet, M.D.Shair (2019) High-Affinity Alkynyl Bisubstrate Inhibitors of Nicotinamide N-Methyltransferase (NNMT). J Med Chem. **62**(21):9837-9873. [PubMed: 31589440](https://www.ncbi.nlm.nih.gov/pubmed/31589440) [doi: 10.1021/acs.jmedchem.9b01238](https://pubs.acs.org/doi/abs/10.1021/acs.jmedchem.9b01238). J.M. Nicoludis and R. Gaudet (2018) Applications of sequence coevolution in membrane protein biochemistry. *Biochim Biophys Acta Biomember.* 1860(4):895-908. doi: 10.1016/j.bbamem.2017.10.004. Epub 2017 Oct 7. [PubMed: 28993150](https://www.ncbi.nlm.nih.gov/pubmed/?term=Applications%20of%20sequence%20coevolution%20in%20membrane%20protein%20biochemistry) PMCID: PMC5807202 Bradshaw N, Levdikov VM, Zimanyi CM, Gaudet R, Wilkinson AJ, Losick R. [A widespread family of serine/threonine protein phosphatases shares a common regulatory switch with proteasomal proteases](https://scholar.harvard.edu/rlosick/publications/widespread-family-serinethreonine-protein-phosphatases-shares-common-regulatory). Elife. 2017;6. [PubMed: 28527238](https://www.ncbi.nlm.nih.gov/pubmed/?term=A%20widespread%20family%20of%20serine/threonine%20protein%20phosphatases%20shares%20a%20common%20regulatory%20switch%20with%20proteasomal%20proteases) PMCID: [PMC5468089](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5468089/) PDB: [5MQH](https://www.rcsb.org/structure/5MQH) [5UCG](https://www.rcsb.org/structure/5UCG) P.A. Meyer, S. Socias, J. Key, E. Ransey, E.C. Tjon, A. Buschiazzo, M. Lei, C. Botka, J. Withrow, D. Neau, K. Rajashankar, K. S. Anderson, R. H. Baxter, S. C. Blacklow, T. J. Boggon, A. M. Bonvin, D. Borek, T. J. Brett, A. Caflisch, C. I. Chang, W. J. Chazin, K. D. Corbett, M. S. Cosgrove, S. Crosson, S. Dhe-Paganon, E. Di Cera, C. L. Drennan, M. J. Eck, B. F. Eichman, Q. R. Fan, A. R. Ferré-D'Amaré, J. C. Fromme, K. C. Garcia, R. Gaudet, P. Gong, S. C. Harrison, E. E. Heldwein, Z. Jia, R. J. Keenan, A. C. Kruse, M. Kvansakul, J.S. McLellan, Y. Modis, Y. Nam, Z. Otwinowski, E. F. Pai, P. J. Pereira, C. 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