Publications

2022

  1. Cao X, Boyaci H, Chen J, Bao Y, Landick R, Campbell EA. Basis of narrow-spectrum activity of fidaxomicin on Clostridioides difficile. Nature. 2022.
  2. Capper MJ, Yang S, Stone AC, Vatansever S, Zilberg G, Mathiharan YK, Habib R, Hutchinson K, Schlessinger A, Mezei M, Osman R, Zhang B, Wacker D. Substrate Binding and Inhibition of the Anion Exchanger 1 Transporter. bioRxiv. 2022. [preprint].
  3. Chen J, Wang Q, Malone B, Llewellyn E, Pechersky Y, Maruthi K, Eng ET, Perry JK, Campbell EA, Shaw DE, Darst SA. Ensemble cryo-EM reveals conformational states of the nsp13 helicase in the SARS-CoV-2 helicase replication-transcription complex. Nat Struct Mol Biol. 2022;29(3):250-260.
  4. Chuang JZ, Yang N, Nakajima N, Otsu W, Fu C, Yang HH, Lee MP, Akbar AF, Badea TC, Guo Z, Nuruzzaman A, Hsu KS, Dunaief JL, Sung CH. Retinal pigment epithelium-specific CLIC4 mutant is a mouse model of dry age-related macular degeneration. Nat Commun. 2022;13(1):374.
  5. Gobeil SMC, Henderson R, Stalls V, Janowska K, Huang X, May A, Speakman M, Beaudoin E, Manne K, Li D, Parks R, Barr M, Deyton M, Martin M, Mansouri K, Edwards RJ, Sempowski GD, Saunders KO, Wiehe K, Williams W, Korber B, Haynes BF, Acharya P. Structural diversity of the SARS-CoV-2 Omicron spike. bioRxiv. 2022.
  6. Kendall AK, Chandra M, Xie B, Wan W, Jackson LP. Improved mammalian retromer cryo-EM structures reveal a new assembly interface. bioRxiv. 2022:2022.2003.2004.482375.
  7. Klykov O, Kopylov M, Carragher B, Heck AJR, Noble AJ, Scheltema RA. Label-free visual proteomics: Coupling MS- and EM-based approaches in structural biology. Mol Cell. 2022;82(2):285-303.
  8. Koo CW, Tucci FJ, He Y, Rosenzweig AC. Recovery of particulate methane monooxygenase structure and activity in a lipid bilayer. Science. 2022;375(6586):1287-1291.
  9. Laughlin ZT, Nandi S, Dey D, Zelinskaya N, Witek MA, Srinivas P, Nguyen HA, Kuiper EG, Comstock LR, Dunham CM, Conn GL. 50S subunit recognition and modification by the Mycobacterium tuberculosis ribosomal RNA methyltransferase TlyA. Proc Natl Acad Sci U S A. 2022;119(14):e2120352119.
  10. Liang WG, Wijaya J, Wei H, Noble AJ, Mancl JM, Mo S, Lee D, Lin King JV, Pan M, Liu C, Koehler CM, Zhao M, Potter CS, Carragher B, Li S, Tang WJ. Structural basis for the mechanisms of human presequence protease conformational switch and substrate recognition. Nat Commun. 2022;13(1):1833.
  11. Trinh TKH, Catalano C, Guo Y. Membrane-active Polymers: NCMNP13-x, NCMNP21-x and NCMNP21b-x for Membrane Protein Structural Biology. bioRxiv. 2022:2022.2001.2010.475744.
  12. Tsai K, Stojkovic V, Lee DJ, Young ID, Szal T, Klepacki D, Vazquez-Laslop N, Mankin AS, Fraser JS, Fujimori DG. Structural basis for context-specific inhibition of translation by oxazolidinone antibiotics. Nat Struct Mol Biol. 2022;29(2):162-171.
  13. Wasmuth EV, Broeck AV, LaClair JR, Hoover EA, Lawrence KE, Paknejad N, Pappas K, Matthies D, Wang B, Feng W, Watson PA, Zinder JC, Karthaus WR, de la Cruz MJ, Hite RK, Manova-Todorova K, Yu Z, Weintraub ST, Klinge S, Sawyers CL. Allosteric interactions prime androgen receptor dimerization and activation. bioRxiv. 2022. [preprint].
  14. Zheng X, Hu Z, Li H, Yang J. Structure of the human cone photoreceptor cyclic nucleotide-gated channel. Nat Struct Mol Biol. 2022;29(1):40-46.
  15. Yin Z, Bird JG, Kaelber JT, Nickels BE, Ebright RH. Structural basis of transcription antitermination by Qλ: NusA induces refolding of Qλ to form nozzle for RNA polymerase exit channel. bioRxiv. 2022. [preprint]
  16. Zimanyi CM, Kopylov M, Potter CS, Carragher B, Eng ET. Broadening access to cryoEM through centralized facilities. Trends Biochem Sci. 2022;47(2):106-116.

2021

  1. Catalano C, Ben-Hail D, Qiu W, Blount P, des Georges A, Guo Y. Cryo-EM Structure of Mechanosensitive Channel YnaI Using SMA2000: Challenges and Opportunities. Membranes. 2021;11(11):849.
  2. Cerutti G, Guo Y, Zhou T, Gorman J, Lee M, Rapp M, Reddem ER, Yu J, Bahna F, Bimela J, Huang Y, Katsamba PS, Liu L, Nair MS, Rawi R, Olia AS, Wang P, Zhang B, Chuang GY, Ho DD, Sheng Z, Kwong PD, Shapiro L. Potent SARS-CoV-2 neutralizing antibodies directed against spike N-terminal domain target a single supersite. Cell Host Microbe. 2021:2021.2001.2010.426120.
  3. Cerutti G, Rapp M, Guo Y, Bahna F, Bimela J, Reddem ER, Yu J, Wang P, Liu L, Huang Y, Ho DD, Kwong PD, Sheng Z, Shapiro L. Structural basis for accommodation of emerging B.1.351 and B.1.1.7 variants by two potent SARS-CoV-2 neutralizing antibodies. Structure. 2021;29(7):655-663 e654.
  4. Chen K-E, Guo Q, Cui Y, Kendall AK, Hill TA, Hall RJ, Sacharz J, Norwood SJ, Xie B, Leneva N, Yang Z, Ghai R, Stroud DA, Fairlie D, Suga H, Jackson LP, Teasdale RD, Passioura T, Collins BM. De novo macrocyclic peptides for inhibiting, stabilising and probing the function of the Retromer endosomal trafficking complex. bioRxiv. 2021. [preprint]
  5. Feldman J, Bals J, Altomare CG, St Denis K, Lam EC, Hauser BM, Ronsard L, Sangesland M, Bracamonte Moreno T, Okonkwo V, Hartojo N, Balazs AB, Bajic G, Lingwood D, Schmidt AG. Naive human B cells engage the receptor binding domain of SARS-CoV-2, variants of concern, and related sarbecoviruses. Sci Immunol. 2021:eabl5842.
  6. Gobeil SM, Janowska K, McDowell S, Mansouri K, Parks R, Manne K, Stalls V, Kopp MF, Henderson R, Edwards RJ, Haynes BF, Acharya P. D614G Mutation Alters SARS-CoV-2 Spike Conformation and Enhances Protease Cleavage at the S1/S2 Junction. Cell reports. 2021;34(2):108630.
  7. Gobeil SM, Janowska K, McDowell S, Mansouri K, Parks R, Stalls V, Kopp MF, Manne K, Li D, Wiehe K, Saunders KO, Edwards RJ, Korber B, Haynes BF, Henderson R, Acharya P. Effect of natural mutations of SARS-CoV-2 on spike structure, conformation, and antigenicity. Science. 2021;373(6555).
  8. He Y, Wang Y, Liu B, Helmling C, Sušac L, Cheng R, Zhou ZH, Feigon J. Structures of telomerase at several steps of telomere repeat synthesis. Nature. 2021;593(7859):454-459.
  9. Herrera NG, Morano NC, Celikgil A, Georgiev GI, Malonis RJ, Lee JH, Tong K, Vergnolle O, Massimi AB, Yen LY, Noble AJ, Kopylov M, Bonanno JB, Garrett-Thomson SC, Hayes DB, Bortz RH, 3rd, Wirchnianski AS, Florez C, Laudermilch E, Haslwanter D, Fels JM, Dieterle ME, Jangra RK, Barnhill J, Mengotto A, Kimmel D, Daily JP, Pirofski LA, Chandran K, Brenowitz M, Garforth SJ, Eng ET, Lai JR, Almo SC. Characterization of the SARS-CoV-2 S Protein: Biophysical, Biochemical, Structural, and Antigenic Analysis. ACS Omega. 2021;6(1):85-102.
  10. Klykov O, Gangwar SP, Yelshanskaya MV, Yen L, Sobolevsky AI. Structure and desensitization of AMPA receptor complexes with type II TARP gamma5 and GSG1L. Mol Cell. 2021.
  11. Kumar P, Cymes GD, Grosman C. Structure and function at the lipid-protein interface of a pentameric ligand-gated ion channel. Proc Natl Acad Sci U S A. 2021;118(23):e2100164118.
  12. Li D, Edwards RJ, Manne K, Martinez DR, Schafer A, Alam SM, Wiehe K, Lu X, Parks R, Sutherland LL, Oguin TH, 3rd, McDanal C, Perez LG, Mansouri K, Gobeil SMC, Janowska K, Stalls V, Kopp M, Cai F, Lee E, Foulger A, Hernandez GE, Sanzone A, Tilahun K, Jiang C, Tse LV, Bock KW, Minai M, Nagata BM, Cronin K, Gee-Lai V, Deyton M, Barr M, Von Holle T, Macintyre AN, Stover E, Feldman J, Hauser BM, Caradonna TM, Scobey TD, Rountree W, Wang Y, Moody MA, Cain DW, DeMarco CT, Denny TN, Woods CW, Petzold EW, Schmidt AG, Teng IT, Zhou T, Kwong PD, Mascola JR, Graham BS, Moore IN, Seder R, Andersen H, Lewis MG, Montefiori DC, Sempowski GD, Baric RS, Acharya P, Haynes BF, Saunders KO. In vitro and in vivo functions of SARS-CoV-2 infection-enhancing and neutralizing antibodies. Cell. 2021.
  13. Malone B, Chen J, Wang Q, Llewellyn E, Choi YJ, Olinares PDB, Cao X, Hernandez C, Eng ET, Chait BT, Shaw DE, Landick R, Darst SA, Campbell EA. Structural basis for backtracking by the SARS-CoV-2 replication-transcription complex. Proc Natl Acad Sci U S A. 2021;118(19).
  14. Moghadamchargari Z, Shirzadeh M, Liu C, Schrecke S, Packianathan C, Russell DH, Zhao M, Laganowsky A. Molecular assemblies of the catalytic domain of SOS with KRas and oncogenic mutants. Proc Natl Acad Sci U S A. 2021;118(12).
  15. Nadezhdin KD, Neuberger A, Nikolaev YA, Murphy LA, Gracheva EO, Bagriantsev SN, Sobolevsky AI. Extracellular cap domain is an essential component of the TRPV1 gating mechanism. Nat Commun. 2021;12(1):2154.
  16. Olinares PDB, Kang JY, Llewellyn E, Chiu C, Chen J, Malone B, Saecker RM, Campbell EA, Darst SA, Chait BT. Native Mass Spectrometry-Based Screening for Optimal Sample Preparation in Single-Particle Cryo-EM. Structure. 2021;29(2):186-195 e186.
  17. Nadezhdin KD, Neuberger A, Trofimov YA, Krylov NA, Sinica V, Kupko N, Vlachova V, Zakharian E, Efremov RG, Sobolevsky AI. Structural mechanism of heat-induced opening of a temperature-sensitive TRP channel. Nat Struct Mol Biol. 2021;28(7):564-572.
  18. Rangarajan ES, Izard T. The Cryogenic Electron Microscopy Structure of the Cell Adhesion Regulator Metavinculin Reveals an Isoform-Specific Kinked Helix in Its Cytoskeleton Binding Domain. Int J Mol Sci. 2021;22(2).
  19. Rapp M, Guo Y, Reddem ER, Yu J, Liu L, Wang P, Cerutti G, Katsamba P, Bimela JS, Bahna FA, Mannepalli SM, Zhang B, Kwong PD, Huang Y, Ho DD, Shapiro L, Sheng Z. Modular basis for potent SARS-CoV-2 neutralization by a prevalent VH1-2-derived antibody class. Cell reports. 2021;35(1):108950.
  20. Sauer DB, Wang B, Sudar JC, Song J, Marden J, Rice WJ, Wang DN. The ups and downs of elevator-type di-/tricarboxylate membrane transporters. FEBS J. 2021.
  21. Schmitz AJ, Turner JS, Liu Z, Zhou JQ, Aziati ID, Chen RE, Joshi A, Bricker TL, Darling TL, Adelsberg DC, Altomare CG, Alsoussi WB, Case JB, VanBlargan LA, Lei T, Thapa M, Amanat F, Jeevan T, Fabrizio T, O’Halloran JA, Shi PY, Presti RM, Webby RJ, Krammer F, Whelan SPJ, Bajic G, Diamond MS, Boon ACM, Ellebedy AH. A vaccine-induced public antibody protects against SARS-CoV-2 and emerging variants. Immunity. 2021;54(9):2159-2166 e2156.
  22. Sharif H, Hollingsworth LR, Griswold AR, Hsiao JC, Wang Q, Bachovchin DA, Wu H. Dipeptidyl peptidase 9 sets a threshold for CARD8 inflammasome formation by sequestering its active C-terminal fragment. Immunity. 2021.
  23. Sun D, Sang Z, Kim YJ, Xiang Y, Cohen T, Belford AK, Huet A, Conway JF, Sun J, Taylor DJ, Schneidman-Duhovny D, Zhang C, Huang W, Shi Y. Potent neutralizing nanobodies resist convergent circulating variants of SARS-CoV-2 by targeting diverse and conserved epitopes. Nat Commun. 2021;12(1):4676.
  24. van Eeuwen T, Shim Y, Kim HJ, Zhao T, Basu S, Garcia BA, Kaplan CD, Min JH, Murakami K. Cryo-EM structure of TFIIH/Rad4-Rad23-Rad33 in damaged DNA opening in nucleotide excision repair. Nat Commun. 2021;12(1):3338.
  25. Wang JC, Chen L. Structural basis for the structural dynamics of human mitochondrial chaperonin mHsp60. Sci Rep. 2021;11(1):14809.
  26. Williams WB, Meyerhoff RR, Edwards RJ, Li H, Manne K, Nicely NI, Henderson R, Zhou Y, Janowska K, Mansouri K, Gobeil S, Evangelous T, Hora B, Berry M, Abuahmad AY, Sprenz J, Deyton M, Stalls V, Kopp M, Hsu AL, Borgnia MJ, Stewart-Jones GBE, Lee MS, Bronkema N, Moody MA, Wiehe K, Bradley T, Alam SM, Parks RJ, Foulger A, Oguin T, Sempowski GD, Bonsignori M, LaBranche CC, Montefiori DC, Seaman M, Santra S, Perfect J, Francica JR, Lynn GM, Aussedat B, Walkowicz WE, Laga R, Kelsoe G, Saunders KO, Fera D, Kwong PD, Seder RA, Bartesaghi A, Shaw GM, Acharya P, Haynes BF. Fab-dimerized glycan-reactive antibodies are a structural category of natural antibodies. Cell. 2021;184(11):2955-2972 e2925.
  27. Yang D, Gouaux E. Illumination of serotonin transporter mechanism and role of the allosteric site. Sci Adv. 2021;7(49):eabl3857.

2020

  1. Acharya P, Williams W, Henderson R, Janowska K, Manne K, Parks R, Deyton M, Sprenz J, Stalls V, Kopp M, Mansouri K, Edwards RJ, Meyerhoff RR, Oguin T, Sempowski G, Saunders K, Haynes BF. A glycan cluster on the SARS-CoV-2 spike ectodomain is recognized by Fab-dimerized glycan-reactive antibodies. bioRxiv. 2020. [preprint]
  2. Chen J, Malone B, Llewellyn E, Grasso M, Shelton PMM, Olinares PDB, Maruthi K, Eng ET, Vatandaslar H, Chait BT, Kapoor TM, Darst SA, Campbell EA. Structural Basis for Helicase-Polymerase Coupling in the SARS-CoV-2 Replication-Transcription Complex. Cell. 2020;182(6):1560-1573 e1513.
  3. Durie CL, Sheedlo MJ, Chung JM, Byrne BG, Su M, Knight T, Swanson M, Lacy DB, Ohi MD. Structural analysis of the Legionella pneumophila Dot/Icm type IV secretion system core complex. Elife. 2020;9.
  4. Henderson R, Edwards RJ, Mansouri K, Janowska K, Stalls V, Gobeil SMC, Kopp M, Li D, Parks R, Hsu AL, Borgnia MJ, Haynes BF, Acharya P. Controlling the SARS-CoV-2 spike glycoprotein conformation. Nat Struct Mol Biol. 2020;27(10):925-933.
  5. Li Q, Pellegrino J, Lee DJ, Tran AA, Chaires HA, Wang R, Park JE, Ji K, Chow D, Zhang N, Brilot AF, Biel JT, van Zundert G, Borrelli K, Shinabarger D, Wolfe C, Murray B, Jacobson MP, Muhle E, Chesneau O, Fraser JS, Seiple IB. Synthetic group A streptogramin antibiotics that overcome Vat resistance. Nature. 2020;586(7827):145-150.
  6. Liu L, Wang P, Nair MS, Yu J, Rapp M, Wang Q, Luo Y, Chan JF, Sahi V, Figueroa A, Guo XV, Cerutti G, Bimela J, Gorman J, Zhou T, Chen Z, Yuen KY, Kwong PD, Sodroski JG, Yin MT, Sheng Z, Huang Y, Shapiro L, Ho DD. Potent neutralizing antibodies against multiple epitopes on SARS-CoV-2 spike. Nature. 2020;584(7821):450-456.
  7. Santosh V, Musayev FN, Jaiswal R, Zarate-Perez F, Vandewinkel B, Dierckx C, Endicott M, Sharifi K, Dryden K, Henckaerts E, Escalante CR. The Cryo-EM structure of AAV2 Rep68 in complex with ssDNA reveals a malleable AAA+ machine that can switch between oligomeric states. Nucleic Acids Res. 2020;48(22):12983-12999.
  8. Vien TN, Wang J, Ng LCT, Cao E, DeCaen PG. Molecular dysregulation of ciliary polycystin-2 channels caused by variants in the TOP domain. Proc Natl Acad Sci U S A. 2020;117(19):10329-10338.
  9. Wang C, Molodtsov V, Firlar E, Kaelber JT, Blaha G, Su M, Ebright RH. Structural basis of transcription-translation coupling. Science. 2020;369(6509):1359-1365.
  10. Yang X, Wang Q, Cao E. Structure of the human cation-chloride cotransporter NKCC1 determined by single-particle electron cryo-microscopy. Nat Commun. 2020;11(1):1016.
  11. Yoder N, Gouaux E. The His-Gly motif of acid-sensing ion channels resides in a reentrant ‘loop’ implicated in gating and ion selectivity. eLife. 2020;9:e56527.
  12. Zheng X, Fu Z, Su D, Zhang Y, Li M, Pan Y, Li H, Li S, Grassucci RA, Ren Z, Hu Z, Li X, Zhou M, Li G, Frank J, Yang J. Mechanism of ligand activation of a eukaryotic cyclic nucleotide-gated channel. Nat Struct Mol Biol. 2020;27(7):625-634.
  13. Zhou T, Teng IT, Olia AS, Cerutti G, Gorman J, Nazzari A, Shi W, Tsybovsky Y, Wang L, Wang S, Zhang B, Zhang Y, Katsamba PS, Petrova Y, Banach BB, Fahad AS, Liu L, Lopez Acevedo SN, Madan B, Oliveira de Souza M, Pan X, Wang P, Wolfe JR, Yin M, Ho DD, Phung E, DiPiazza A, Chang LA, Abiona OM, Corbett KS, DeKosky BJ, Graham BS, Mascola JR, Misasi J, Ruckwardt T, Sullivan NJ, Shapiro L, Kwong PD. Structure-Based Design with Tag-Based Purification and In-Process Biotinylation Enable Streamlined Development of SARS-CoV-2 Spike Molecular Probes. Cell reports. 2020;33(4):108322.
  14. Zhou T, Tsybovsky Y, Gorman J, Rapp M, Cerutti G, Chuang GY, Katsamba PS, Sampson JM, Schon A, Bimela J, Boyington JC, Nazzari A, Olia AS, Shi W, Sastry M, Stephens T, Stuckey J, Teng IT, Wang P, Wang S, Zhang B, Friesner RA, Ho DD, Mascola JR, Shapiro L, Kwong PD. Cryo-EM Structures of SARS-CoV-2 Spike without and with ACE2 Reveal a pH-Dependent Switch to Mediate Endosomal Positioning of Receptor-Binding Domains. Cell Host Microbe. 2020;28(6):867-879 e865.