Core-Related Publications

Accelerating Discovery

Since 2017, the core has served over ~125 research groups, including intramural and extramural academia, industry, and government. This has contributed to over ~100 peer-reviewed articles, and numerous meeting abstracts and graduate dissertations.


  1. Lyu M, Malyutin AG, Stadtmueller BM. The structure of the teleost Immunoglobulin M core provides insights on polymeric antibody evolution, assembly, and function. bioRxiv [Preprint]. 2023 Sep 5:2023.03.29.534771. (2023).
  2. Goldman, N., Chandra, A., Johnson, I. et al. Intrinsically disordered domain of transcription factor TCF-1 is required for T cell developmental fidelity. Nat Immunol 24, 1698–1710 (2023).
  3. Bryan, N.W., A. Ali, E. Niedzialkowska,, L. Mayne, P.T. Stukenberg, and B.E. Black*. Structural basis for the phase separation of the chromosome passenger complex. (2023).
  4. Eilers G*, Gupta K*, Allen A, Montermoso S, Murali H, Sharp R, Hwang Y, Bushman FD, Van Duyne G. Structure of a HIV-1 IN-Allosteric inhibitor complex at 2.93 Å resolution: Routes to inhibitor optimization. PLoS Pathog. 2023 Mar;19(3):e1011097. doi: 10.1371/journal.ppat.1011097. (*=co-first authors) (2023).
  5. Sun Y., Florio T.J., Gupta S., Young M.C., Marshall Q.F., Gar nkle S.E., Papadaki G.F., Truong H.V., Mycek E., Li P., Farrel A., Church N.L., Jabar S., Beasley M.D., Kiefel B.R., Yarmarkovich M., Mallik L., Maris J.M., Sgourakis N.G. Structural principles of peptide-centric Chimeric Antigen Receptor recognition guide therapeutic expansion. Science Immunology, In Press (2023)
  6. McShan A.C., Flores-Solis D., Sun Y., Garfinkle S., Young M.C., Toor J., Sgourakis N.G. Conformational plasticity of RAS Q61 family of neoepitopes results in distinct features for targeted recognition. Nature Communications, accepted (2023)
  7. Gupta S., Nerli S., Kutti Kandi S., Merski G.L., Sgourakis N.G. HLA3DB: comprehensive annotation of peptide/HLA complexes enables blind structure prediction of T cell epitopes. Nature Communications, 14(1):6349 (2023)
  8. Papadaki G.F., Woodward C.H., Young M.C., Winters T.J., Burslem G.M., Sgourakis N.G. A Chicken Tapasin ortholog can chaperone empty HLA-B37:01 molecules independent of other peptide-loading components. Journal of Biological Chemistry, 299(10):105136 (2023)
  9. Sun Y., Young M.C., Woodward C.H., Danon J.N., Truong H.V., Gupta S., Winters T.J., Font-Burgada J. Burslem G.M., Sgourakis N.G. Universal open MHC-I molecules for rapid peptide loading and enhanced complex stability across HLA allotypes Proc Natl Acad Sci U S A 120(25) (2023)
  10. Sun Y., Papadaki G.F., Devlin C.A., Young M.C., Woodward C.H., Danon J.N., Truong H.V., Gupta S., Winters T.J., Burslem G.M., Procko E., Sgourakis N.G. Xeno interactions between MHC-I proteins and molecular chaperones enable ligand exchange on a broad repertoire of HLA allotypes Science Advances 9(8) (2023)
  11. Papadaki G.F., Ani O., Florio T.J., Young M.C., Danon J.N., Sun Y., Dersh D., Sgourakis N.G. Decoupling peptide binding from T cell receptor recognition with engineered chimeric MHC-I molecules. Frontiers in Immunology 14:1116906 (2023)
  12. Gorbea Colón JJ, Palao L 3rd, Chen SF, Kim HJ, Snyder L, Chang YW, Tsai KL, Murakami K. Structural basis of a transcription pre-initiation complex on a divergent promoter. Mol Cell. 2023 Feb 16;83(4):574-588.e11. (2023)
  13. Fregoso FE, Boczkowska M, Rebowski G, Carman PJ, van Eeuwen T, Dominguez R. Mechanism of synergistic activation of Arp2/3 complex by cortactin and WASP- family proteins. Nat Commun. (2023)
  14. Carman PJ, Rebowski G, Dominguez R, Alqassim SS. Single particle cryo-EM analysis of Rickettsia conorii Sca2 reveals a formin-like core. J Struct Biol. Jun;215(2):107960. (2023)


  1. Hashimoto, H., Ramirez, D.H., Lautier, O., Pawlak, N., Blobel, G., Palancade, B., Debler, E.W. Structure of the pre-mRNA leakage 39-kDa protein reveals a single domain of integrated zf-C3HC and Rsm1 modules. Scientific Reports volume 12, Article number: 17691 (2022).
  2. Segura-Peña, D., O. Hovet, H. Gogoi, J.M. Dawicki-McKenna, S.M.H. Wøien, M. Carrer, B.E. Black, M. Cascella, and N. Sekulic. 2023. The structural basis of the multi-step allosteric activation of Aurora B kinase. eLife, 12:e85328. (2022).
  3. Mandal, P., K. Eswara, Z. Yerkesh, V. Kharchenko, L. Zandarashvili, K. Szczepski, D. Bensaddek, L. Jaremko, B.E. Black, and W. Fischle. Molecular basis of UHRF1 allosteric activation for synergistic histone modification binding by PI5P. Sci. Adv., 8:eabl9461 (2022).
  4. Faylo JL, van Eeuwen T, Gupta K, Murakami K, Christianson D. Order in the Core: Transient Prenyltransferase-Cyclase Association in Bifunctional Fuscoccadiene Synthase. Biochemistry 61(21):2417-2430 (2022).
  5. Cupo RR, Rizo AN, Braun GA, Tse E, Chuang E, Gupta K, Southworth DR, Shorter J. Unique structural features govern the activity of a human mitochondrial AAA+ disaggregase, Skd3. Cell Reports 40(13):111408 (2022).
  6. Doll SG, Meshkin H, Bryer AJ, Li F, Ko YH, Lokareddy RK, Gillian R, Gupta K, Perilla JR, Cingolani C. Recognition and phosphorylation of the TDP-43 Nuclear Localization Signal. Cell Reports 39(13):111007 (2022).
  7. Jiang J., Taylor D.K., Kim E.J., Boyd L.F., Ahmad J., Mage M.G., Truong H.V., Woodward C.H., Sgourakis N.G. Cresswell P., Margulies D.H., Natarajan K. Structural mechanism of tapasin-mediated MHC-I peptide loading in antigen presentation Nature Communications 13:5470. (2022)
  8. McShan A.C., Devlin C.A., Papadaki G.F., Sun Y., Green A.I., Morozov G.I., Burslem G.M., Procko E., Sgourakis N.G. TAPBPR employs a ligand-independent docking mechanism to chaperone MR1 molecules Nature Chemical Biology 18:859-868. (2022)
  9. Fregoso FE, van Eeuwen T, Simanov G, Rebowski G, Boczkowska M, Zimmet A, Gautreau AM, Dominguez R. Molecular mechanism of Arp2/3 complex inhibition by Arpin. Nat Commun. Feb 2;13(1):628. (2022)
  10. El Khatib M, Cheprakov AV, Vinogradov SA. Unusual Reactivity and Metal Affinity of Water-Soluble Dipyrrins. Inorg Chem. 2022 Aug 15;61(32):12746-12758. (2022)
  11. Yang C, Fujiwara R, Kim HJ, Basnet P, Zhu Y, Gorbea Colón JJ, Steimle S, Garcia BA, Kaplan CD, Murakami K. Structural visualization of de novo transcription initiation by Saccharomyces cerevisiae RNA polymerase II. Mol Cell. (2022)


  1. Xia P, Dutta A, Koppula A, Gupta K, Batish M, Parashar V. Structural basis of oligoadenylate binding by Csa3 transcription factors. Journal of Biological Chemistry 298(2):101591 (2021).
  2. Ye, X., Mayne, L. & Englander, S.W. A conserved strategy for structure change and energy transduction in Hsp104 and other AAA+ protein motors. J Biol Chem 297, 101066 (2021).
  3. Langelier, M.F., R. Billur, A. Sverzhinsky, B.E. Black, and J.M. Pascal. 2021. HPF1 dynamically controls the PARP1/2 balance between initiating and elongating ADP-ribose modifications. Nat. Commun. 12:6675.
  4. Shi, F. et al. ROR and RYK extracellular region structures suggest that receptor tyrosine kinases have distinct WNT-recognition modes. Cell Reports 37, 109834 (2021).
  5. Schulte, J.E., Roggiani, M., Shi, H., Zhu, J. & Goulian, M. The phosphohistidine phosphatase SixA dephosphorylates the phosphocarrier NPr. Journal of Biological Chemistry 296(2021).
  6. Maciunas, L.J., Porter, N., Lee, P.J., Gupta, K. & Loll, P.J. Structures of full-length VanR from Streptomyces coelicolor in both the inactive and activated states. Acta Crystallogr D Struct Biol 77, 1027-1039 (2021).
  7. Lénon, M. et al. A useful epitope tag derived from maltose binding protein. Protein Science 30, 1235-1246 (2021).
  8. Hatstat, A.K. et al. Characterization of Small-Molecule-Induced Changes in Parkinson's-Related Trafficking via the Nedd4 Ubiquitin Signaling Cascade. Cell Chem Biol 28, 14-25.e9 (2021).
  9. Happ, J.T. et al. A PKA Inhibitor Motif within Smoothened Controls Hedgehog Signal Transduction. bioRxiv, 2021.07.05.451193 (2021).
  10. Gupta, K. et al. Assembly of higher-order SMN oligomers is essential for metazoan viability and requires an exposed structural motif present in the YG zipper dimer. Nucleic Acids Res 49, 7644-7664 (2021).
  11. Gupta, K. et al. Allosteric HIV Integrase Inhibitors Promote Formation of Inactive Branched Polymers via Homomeric Carboxy-Terminal Domain Interactions. Structure 29, 213-225.e5 (2021).
  12. Faylo, J.L. Ph.D., University of Pennsylvania (2021).
  13. Dutta, A., Batish, M. & Parashar, V. Structural basis of KdpD histidine kinase binding to the second messenger c-di-AMP. Journal of Biological Chemistry 296(2021).
  14. Arturo, E.C. et al. Manipulation of a cation-π sandwich reveals conformational flexibility in phenylalanine hydroxylase. Biochimie 183, 63-77 (2021).
  15. Allu, S. R.; Ravotto, L.; Troxler, T.; Vinogradov, S. A. syn-Diarylphthalimidoporphyrins: Effects of symmetry breaking on two-photon absorption and linear photophysical properties.  J. Phys. Chem. A, 125(14), 2977-2988 (2021).
  16. McShan A.C., Devlin C.A., Morozov G.I., Overall S.A., Moschidi D., Akella N., Procko E., Sgourakis N.G. TAPBPR promotes antigen loading on MHC-I molecules using a peptide trap. Nature Communications 12(1):3174. (2021)
  17. Nerli S., De Paula V.S., McShan A.C., Sgourakis N.G. Backbone-independent NMR resonance assignments of methyl probes in large proteins. Nature Communications 12(1):691.(2021)
  18. Faylo JL, van Eeuwen T, Kim HJ, Gorbea Colón JJ, Garcia BA, Murakami K, Christianson DW. Structural insight on assembly-line catalysis in terpene biosynthesis. Nat Commun. Jun 9;12(1):3487. (2021)
  19. Jones CM, Petersson GA, Petersson EJ. Synthesis and characterization of fluorescent amino acid dimethylaminoacridonylalanine. ARKIVOC. 2021;2021:97-109. (2021)
  20. van Eeuwen T, Li T, Kim HJ, Gorbea Colón JJ, Parker MI, Dunbrack RL, Garcia BA, Tsai KL, Murakami K. Structure of TFIIK for phosphorylation of CTD of RNA polymerase II. Sci Adv. (2021)
  21. Baskaran SG, Sharp TP, Sharp KA. Computational Graphics Software for Interactive Docking and Visualization of Ligand-Protein Complementarity. J Chem Inf Model. (2021)
  22. 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)
  23. Li YC, Chao TC, Kim HJ, Cholko T, Chen SF, Li G, Snyder L, Nakanishi K, Chang CE, Murakami K, Garcia BA, Boyer TG, Tsai KL. Structure and noncanonical Cdk8 activation mechanism within an Argonaute-containing Mediator kinase module. Sci Adv. Jan 15;7(3):eabd4484. (2021)
  24. Pino LK, Baeza J, Lauman R, Schilling B, Garcia BA. Improved SILAC Quantification with Data-Independent Acquisition to Investigate Bortezomib- Induced Protein Degradation. J Proteome Res. 2021 Apr 2;20(4):1918-1927. doi: 10.1021/acs.jproteome.0c00938. (2021)
  25. Steimle S, van Eeuwen T, Ozturk Y, Kim HJ, Braitbard M, Selamoglu N, Garcia BA, Schneidman-Duhovny D, Murakami K, Daldal F. Cryo-EM structures of engineered active bc1-cbb3 type CIII2CIV super-complexes and electronic communication between the complexes. Nat Commun. (2021)
  26. Snoberger A, Barua B, Atherton JL, Shuman H, Forgacs E, Goldman YE, Winkelmann DA, Ostap EM. Myosin with hypertrophic cardiac mutation R712L has a decreased working stroke which is rescued by omecamtiv mecarbil. Elife. (2021)
  27. Allu SR, Ravotto L, Troxler T, Vinogradov SA. syn-Diarylphthalimidoporphyrins: Effects of Symmetry Breaking on Two-Photon Absorption and Linear Photophysical Properties. J Phys Chem A. 2021 Apr 15;125(14):2977-2988. doi: 10.1021/acs.jpca.1c01652. (2021)


  1. Ye, X., Lin, J., Mayne, L., Shorter, J. & Englander, S.W. Structural and kinetic basis for the regulation and potentiation of Hsp104 function. Proc Natl Acad Sci U S A 117, 9384-9392 (2020).
  2. Taylor, L.J. Ph.D., University of Pennsylvania (2020).
  3. Sweeny, E.A. et al. Structural and mechanistic insights into Hsp104 function revealed by synchrotron X-ray footprinting. J Biol Chem 295, 1517-1538 (2020).
  4. Ronnebaum, T.A., Gupta, K. & Christianson, D.W. Higher-order oligomerization of a chimeric αβγ bifunctional diterpene synthase with prenyltransferase and class II cyclase activities is concentration-dependent. J Struct Biol 210, 107463 (2020).
  5. O'Brien, E.S. et al. Membrane Proteins Have Distinct Fast Internal Motion and Residual Conformational Entropy. Angew Chem Int Ed Engl 59, 11108-11114 (2020).
  6. March, Z.M. et al. Therapeutic genetic variation revealed in diverse Hsp104 homologs. Elife 9(2020).
  7. Ji, H.-H. & Ostap, E.M. The regulatory protein 14-3-3β binds to the IQ motifs of myosin-IC independent of phosphorylation. Journal of Biological Chemistry 295, 3749-3756 (2020).
  8. Gupta, K. Hiding the Elephant in the Room with Experimental Neutrons. Biophys J 119, 234-235 (2020).
  9. Fung, H.Y.J., McKibben, K.M., Ramirez, J., Gupta, K. & Rhoades, E. Structural Characterization of Tau in Fuzzy Tau:Tubulin Complexes. Structure 28, 378-384.e4 (2020).
  10. Eilers, G. et al. Influence of the amino-terminal sequence on the structure and function of HIV integrase. Retrovirology 17, 28 (2020).
  11. DeRose, B.T. et al. Production and analysis of a mammalian septin hetero-octamer complex. Cytoskeleton 77, 485-499 (2020).
  12. De Paula, V.S., Dubey, A., Arthanari, H. & Sgourakis, N.G. A slow-exchange conformational switch regulates off-target cleavage by high-fidelity Cas9. bioRxiv, 2020.12.06.413757 (2020).
  13. Zandarashvili, L., M.F. Langelier, U.K. Velagapudi, M.A. Hancock, J.D. Steffen, R. Billur, Z.M. Hannan, A.J. Wicks, D.B. Krastev, S.J. Pettitt, C.J. Lord, T.T. Talele, J.M. Pascal*, and B.E. Black*. Structural basis for allosteric PARP-1 retention on DNA breaks. Science, 368:eaax6367 (2020).(*corresponding authors; contributed equally)
  14. Ravotto, L.; Meloni, S. L.; Esipova, T. V.; Masunov, A. E.; Anna, J. M.;  Vinogradov, S. A. Three-photon spectroscopy of porphyrins J. Phys. Chem. A, 124(52) 11038–11050 (2020).
  15. Ballester, M.; Ravotto, L.; Quirke, J. M. E.; de la Vega, R. L.; Shelnutt, J. A.; Cheprakov, A. V.; Vinogradov, S. A.;* Medforth, C. J.* Protonation of planar and nonplanar porphyrins: a calorimetric and computational study. J. Phys. Chem. A, 124(43), 8994-9003 (2020).
  16. Bartosik, P.; Fitzgerald, J.; El Khatib, M.; Yaseen, M. A.; Vinogradov, S. A., Niedre, M.  Prospects for the Use of Upconverting Nanoparticles as a Contrast Agent for Enumeration of Circulating Cells in vivo  Intl. J. Nanomed.15, 1709-1719 (2020).
  17. Christodoulou, C.; Spencer J. A.; Turcotte, R.; Kokkaliaris, K.D.; Panero, R.; Ramos, A.; Esipova, T. V.; Vinogradov, S. A.; Rudzinskas, S.; Zhang, Y.; Perkins, A.S.; Schroeder, T.; Lin, C. P.; Camargo, F. Live-Animal Imaging of Native Hematopoietic Stem and Progenitor cells, Nature  2020, 578, 278-283.
  18. Cao, X.; Rao Allu, S.; Jiang, S.; Jia, M.; Gunn, J. R.; Yao, C.; LaRochelle, E. P.; Shell, J. R.; Bruza, P.; Gladstone, D. J.; Jarvis, L. A.; Tian, J.; Vinogradov, S. A.;* Pogue, B. W.*  Tissue pO2 Distributions in Xenograft Tumors Dynamically Imaged by Cherenkov-Excited Phosphorescence during Fractionated Radiation Therapy, Nature Commun. 11,  Article number: 573 (2020).
  19. Isokuortti, J.; Rao Allu, S.; Efimov, A.; Vuorimaa-Laukkanen, E.; Tkachenko, N. V.; Vinogradov, S. A.; Laaksonen, T.; Durandin, N. A. Endothermic and Exothermic Energy Transfer Made Equally Efficient for Triplet−Triplet Annihilation Upconversion,  J. Phys. Chem. Lett.  11, 318-324 (2020).
  20. Plunkett, S.; El Khatib, M.; Sencan, I.; Porter, J.; Kumar, A. T. N.; Collins, J.; Sakadzic, S.; Vinogradov, S. A. In vivo deep-tissue microscopy with UCNP/Janus-dendrimers as imaging probes: resolution at depth and feasibility of ratiometric sensing,  Nanoscale 12, 2657-2672, DOI: 10.1039/c9nr07778b (2020).
  21. Palmer NJ, Eskici G, Axelsen PH. Non-Equilibrium Mass Exchange in AOT Reverse Micelles.J Phys Chem B. Jan 9;124(1):144-148. (2020). 
  22. Ravotto L, Meloni SL, Esipova TV, Masunov AE, Anna JM, Vinogradov SA. Three-Photon Spectroscopy of Porphyrins. J Phys Chem A. Dec 31;124(52):11038-11050. doi: 10.1021/acs.jpca.0c08334 (2020)
  23. Zimmet A, Van Eeuwen T, Boczkowska M, Rebowski G, Murakami K, Dominguez R. Cryo-EM structure of NPF-bound human Arp2/3 complex and activation mechanism. Sci Adv. (2020)


  1. Ye, X., Lin, J., Mayne, L., Shorter, J. & Englander, S.W. Hydrogen exchange reveals Hsp104 architecture, structural dynamics, and energetics in physiological solution. Proc Natl Acad Sci U S A 116, 7333-7342 (2019).
  2. Masson, G.R. et al. Recommendations for performing, interpreting and reporting hydrogen deuterium exchange mass spectrometry (HDX-MS) experiments. Nat Methods 16, 595-602 (2019).
  3. Komatsu, H., Meurice, C. & Axelsen, P.H. Variable Binding of Thioflavin T to Amyloid Fibrils. Biophysical Journal 116, 195a (2019).
  4. Kan, Z.Y., Ye, X., Skinner, J.J., Mayne, L. & Englander, S.W. ExMS2: An Integrated Solution for Hydrogen-Deuterium Exchange Mass Spectrometry Data Analysis. Anal Chem 91, 7474-7481 (2019).
  5. Fuglestad, B., Gupta, K., Wand, A.J. & Sharp, K.A. Water loading driven size, shape, and composition of cetyltrimethylammonium/hexanol/pentane reverse micelles. J Colloid Interface Sci 540, 207-217 (2019).
  6. Bazilevsky, G.A. et al. ATP-citrate lyase multimerization is required for coenzyme-A substrate binding and catalysis. Journal of Biological Chemistry 294, 7259-7268 (2019).
  7. Arturo, E.C., Gupta, K., Hansen, M.R., Borne, E. & Jaffe, E.K. Biophysical characterization of full-length human phenylalanine hydroxylase provides a deeper understanding of its quaternary structure equilibrium. J Biol Chem 294, 10131-10145 (2019).
  8. Schilling, K.; El Khatib, M.; Plunkett, S.; Xue, J. J.; Xia, Y. N.;  Vinogradov, S. A.;* Brown, E.;* Zhang, X. P.*  Electrospun Fiber Mesh for High-Resolution Measurements of Oxygen Tension in Cranial Bone Defect Repair.  ACS Appl. Mater. & Interf.  11 (37), 33548-33558 (2020).
  9. Esipova, T. V.; Barrett, M. J. P.; Erlebach, E.; Masunov, A. E.; Weber, B.; Vinogradov, S. A.  Oxyphor 2P: A High-Performance Probe for Deep-Tissue Longitudinal Oxygen Imaging.  Cell Metabolism 29 (3), 736 (2019).
  10. Del Secco, B.; Ravotto, L.; Esipova, T. V.; Vinogradov, S. A.;* Genovese, D.; Zaccheroni, N.; Rampazzo, E.;* Prodi, L.* Optimized synthesis of luminescent silica nanoparticles by a direct micelle-assisted method.  Photochem. Photobiol. Sci. 18 (9), 2142-2149 (2019).


  1. Ye, X., Mayne, L., Kan, Z.Y. & Englander, S.W. Folding of maltose binding protein outside of and in GroEL. Proc Natl Acad Sci U S A 115, 519-524 (2018).
  2. Sheehan, M.M. et al. Rational Construction of Compact de Novo-Designed Biliverdin-Binding Proteins. Biochemistry 57, 6752-6756 (2018).
  3. Ray-Gallet, D. et al. Functional activity of the H3.3 histone chaperone complex HIRA requires trimerization of the HIRA subunit. Nat Commun 9, 3103 (2018).
  4. Li, H., Sharp, R., Rutherford, K., Gupta, K. & Van Duyne, G.D. Serine Integrase attP Binding and Specificity. J Mol Biol 430, 4401-4418 (2018).
  5. Gray, K.M. et al. Self-oligomerization regulates stability of survival motor neuron protein isoforms by sequestering an SCF(Slmb) degron. Mol Biol Cell 29, 96-110 (2018).
  6. Ashkar, R. et al. Neutron scattering in the biological sciences: progress and prospects. Acta Crystallogr D Struct Biol 74, 1129-1168 (2018).
  7. Langelier, M.F., L. Zandarashvili, P.M. Aguiar, B.E. Black*, and J.M. Pascal*. NAD+ analog reveals PARP-1 substrate-blocking mechanism and allosteric communication from catalytic center to DNA-binding domains. Nat. Commun., 9:844. (2018) (*corresponding authors)
  8. Friedman, E. S.; Bittinger, K.; Esipova, T. V.; Hou, L.; Chau, L.; Jiang, J.; Mesaros, C.; Lund, P. J.; Liang, X.; FitzGerald, G. A.; Goulian, M.; Lee, D.; Garcia, B. A.; Blair, I. A.; Vinogradov, S. A.;* Wu, G. D.*  Microbes vs chemistry in the origin of the anaerobic gut lumen.  PNAS 115 (16), 4170-4175 (2018).


  1. Tischer, A. et al. Enhanced Local Disorder in a Clinically Elusive von Willebrand Factor Provokes High-Affinity Platelet Clumping. J Mol Biol 429, 2161-2177 (2017).
  2. Pauw, B.R., Kastner, C. & Thunemann, A.F. Nanoparticle size distribution quantification: results of a small-angle X-ray scattering inter-laboratory comparison. Journal of Applied Crystallography 50, 1280-1288 (2017).
  3. Mandali, S., Gupta, K., Dawson, A.R., Van Duyne, G.D. & Johnson, R.C. Control of Recombination Directionality by the Listeria Phage A118 Protein Gp44 and the Coiled-Coil Motif of Its Serine Integrase. J Bacteriol 199(2017).
  4. Gupta, K., Sharp, R., Yuan, J.B., Li, H. & Van Duyne, G.D. Coiled-coil interactions mediate serine integrase directionality. Nucleic Acids Res 45, 7339-7353 (2017).
  5. Englander, S.W. & Mayne, L. Reply to Eaton and Wolynes: How do proteins fold? Proc Natl Acad Sci U S A 114, E9761-e9762 (2017).
  6. Englander, S.W. & Mayne, L. The case for defined protein folding pathways. Proc Natl Acad Sci U S A 114, 8253-8258 (2017).
  7. Emptage, R.P., Lemmon, M.A. & Ferguson, K.M. Molecular determinants of KA1 domain-mediated autoinhibition and phospholipid activation of MARK1 kinase. Biochemical Journal 474, 385-398 (2017).
  8. Chetty, P.S., Mayne, L., Lund-Katz, S., Englander, S.W. & Phillips, M.C. Helical structure, stability, and dynamics in human apolipoprotein E3 and E4 by hydrogen exchange and mass spectrometry. Proc Natl Acad Sci U S A 114, 968-973 (2017).
  9. Guo, L.Y., P.K. Allu, L. Zandarashvili, K.L. McKinley, N. Sekulic, J.M. Dawicki-McKenna, D. Fachinetti, G.A. Logsdon, R.M. Jamiolkowski, D.W. Cleveland, I.M. Cheeseman, and B.E. Black*. Centromeres are maintained by fastening CENP-A to DNA and directing an arginine anchor-dependent nucleosome structural transition. Nat. Commun., 8:15775. (2022) (*corresponding author)
  10. Esipova, T. V.; Rivera-Jacquez, H. J.; Weber, B.; Masunov, A. E.;  Vinogradov, S. A.  Stabilizing g-states in centrosymmetric tetrapyrroles: two-photon-absorbing porphyrins with bright phosphorescence.  J. Phys. Chem. A 121 (33), 6243-6255 (2017).