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Aaron, J. A., Lin, X., Cane, D. E., and Christianson, D. W. (2010) Structure of epi-isozizaene synthase from Streptomyces coelicolor A3(2), a platform for new terpenoid cyclization templates. Biochemistry. 49, 1787-97
Abhishek, S., Deeksha, W., and Rajakumara, E. (2021) Helical and β-Turn Conformations in the Peptide Recognition Regions of the VIM1 PHD Finger Abrogate H3K4 Peptide Recognition.. Biochemistry. 10.1021/acs.biochem.1c00191
Abraham, J., Corbett, K. D., Farzan, M., Choe, H., and Harrison, S. C. (2010) Structural basis for receptor recognition by New World hemorrhagic fever arenaviruses. Nat Struct Mol Biol. 17, 438-44
Abskharon, R., Seidler, P. Matthew, Sawaya, M. R., Cascio, D., Yang, T. P., Philipp, S., Williams, C. Kazu, Newell, K. L., Ghetti, B., DeTure, M. A., Dickson, D. W., Vinters, H. V., Felgner, P. L., Nakajima, R., Glabe, C. G., and Eisenberg, D. S. (2020) Crystal structure of a conformational antibody that binds tau oligomers and inhibits pathological seeding by extracts from donors with Alzheimer's disease. J Biol Chem. 10.1074/jbc.RA120.013638
Abskharon, R., Pan, H., Sawaya, M. R., Seidler, P. M., Olivares, E. J., Chen, Y., Murray, K. A., Zhang, J., Lantz, C., Bentzel, M., Boyer, D. R., Cascio, D., Nguyen, B. A., Hou, K., Cheng, X., Pardon, E., Williams, C. K., Nana, A. L., Vinters, H. V., Spina, S., Grinberg, L. T., Seeley, W. W., Steyaert, J., Glabe, C. G., Loo, R. R. Ogorzale, Loo, J. A., and Eisenberg, D. S. (2023) Structure-based design of nanobodies that inhibit seeding of Alzheimer's patient-extracted tau fibrils. Proc Natl Acad Sci U S A. 120, e2300258120
Adachi, M. S., Taylor, A. B., P Hart, J., and Fitzpatrick, P. F. (2012) Mechanistic and structural analyses of the roles of active site residues in yeast polyamine oxidase Fms1: characterization of the N195A and D94N enzymes. Biochemistry. 51, 8690-7
Adachi, M. S., Taylor, A. B., P Hart, J., and Fitzpatrick, P. F. (2012) Mechanistic and structural analyses of the role of His67 in the yeast polyamine oxidase Fms1. Biochemistry. 51, 4888-97
Adak, S., Ye, N., Calderone, L. A., Schäfer, R. J. B., Lukowski, A. L., Pandelia, M. - E., Drennan, C. L., and Moore, B. S. (2023) Oxidative rearrangement of tryptophan to indole nitrile by a single diiron enzyme. bioRxiv. 10.1101/2023.08.03.551874
Adam, S., Anteneh, H., Hornisch, M., Wagner, V., Lu, J., Radde, N. E., Bashtrykov, P., Song, J., and Jeltsch, A. (2020) DNA sequence-dependent activity and base flipping mechanisms of DNMT1 regulate genome-wide DNA methylation. Nat Commun. 11, 3723
Adams, M. C., Schiltz, C. J., Sun, J., Hosford, C. J., Johnson, V. M., Pan, H., Borbat, P. P., Freed, J. H., Thomason, L. C., Court, C., Court, D. L., and Chappie, J. S. (2024) The crystal structure of bacteriophage λ RexA provides novel insights into the DNA binding properties of Rex-like phage exclusion proteins.. Nucleic Acids Res. 52, 4659-4675
Adams, M. C., Schiltz, C. J., Heck, M. L., and Chappie, J. S. (2021) Crystal structure of the potato leafroll virus coat protein and implications for viral assembly. J Struct Biol. 214, 107811
Adhikari, A. A., Seegar, T. C. M., Ficarro, S. B., McCurry, M. D., Ramachandran, D., Yao, L., Chaudhari, S. N., Ndousse-Fetter, S., Banks, A. S., Marto, J. A., Blacklow, S. C., and A Devlin, S. (2020) Development of a covalent inhibitor of gut bacterial bile salt hydrolases. Nat Chem Biol. 16, 318-326
Adlakha, J., Hong, Z., Li, P. Q., and Reinisch, K. M. (2022) Structural and biochemical insights into lipid transport by VPS13 proteins. J Cell Biol. 10.1083/jcb.202202030
Afshar, S., Sawaya, M. R., and Morrison, S. L. (2009) Structure of a mutant human purine nucleoside phosphorylase with the prodrug, 2-fluoro-2'-deoxyadenosine and the cytotoxic drug, 2-fluoroadenine. Protein Sci. 18, 1107-14
Agarkar, V. B., Babayeva, N. D., Wilder, P. J., Rizzino, A., and Tahirov, T. H. (2010) Crystal structure of mouse Elf3 C-terminal DNA-binding domain in complex with type II TGF-beta receptor promoter DNA. J Mol Biol. 397, 278-89
Agarkar, V. B., Babayeva, N. D., Pavlov, Y. I., and Tahirov, T. H. (2011) Crystal structure of the C-terminal domain of human DNA primase large subunit: implications for the mechanism of the primase-polymerase α switch.. Cell Cycle. 10, 926-31
Agarkar, V. B., Babayeva, N. D., Rizzino, A., and Tahirov, T. H. (2009) Preliminary crystallographic analysis of mouse Elf3 C-terminal DNA-binding domain in complex with type II TGF-beta receptor promoter DNA. Acta Crystallogr Sect F Struct Biol Cryst Commun. 65, 1261-3
Agdanowski, M. P., Castells-Graells, R., Sawaya, M. R., Cascio, D., Yeates, T. O., and Arbing, M. A. (2024) X-ray crystal structure of a designed rigidified imaging scaffold in the ligand-free conformation. Acta Crystallogr F Struct Biol Commun. 80, 107-115
Aguilar, F., Yu, S., Grant, R. A., Swanson, S., Ghose, D., Su, B. G., Sarosiek, K. A., and Keating, A. E. (2023) Peptides from human BNIP5 and PXT1 and non-native binders of pro-apoptotic BAK can directly activate or inhibit BAK-mediated membrane permeabilization. Structure. 31, 265-281.e7
Ahmad, M. Faiz, Alam, I., Huff, S. E., Pink, J., Flanagan, S. A., Shewach, D., Misko, T. A., Oleinick, N. L., Harte, W. E., Viswanathan, R., Harris, M. E., and Dealwis, C. Godfrey (2017) Potent competitive inhibition of human ribonucleotide reductase by a nonnucleoside small molecule. Proc Natl Acad Sci U S A. 114, 8241-8246
Ahmad, S., Xu, J., Feng, J. A., Hutchinson, A., Zeng, H., Ghiabi, P., Dong, A., Centrella, P. A., Clark, M. A., Guié, M. - A., Guilinger, J. P., Keefe, A. D., Zhang, Y., Cerruti, T., Cuozzo, J. W., von Rechenberg, M., Bolotokova, A., Li, Y., Loppnau, P., Seitova, A., Li, Y. - Y., Santhakumar, V., Brown, P. J., Ackloo, S., and Halabelian, L. (2023) Discovery of a First-in-Class Small-Molecule Ligand for WDR91 Using DNA-Encoded Chemical Library Selection Followed by Machine Learning. J Med Chem. 66, 16051-16061
Ahmad, M. Faiz, Huff, S. E., Pink, J., Alam, I., Zhang, A., Perry, K., Harris, M. E., Misko, T., Porwal, S. K., Oleinick, N. L., Miyagi, M., Viswanathan, R., and Dealwis, C. Godfrey (2015) Identification of Non-nucleoside Human Ribonucleotide Reductase Modulators. J Med Chem. 58, 9498-509
Ahmad, S., Wang, B., Walker, M. D., Tran, H. - K. R., Stogios, P. J., Savchenko, A., Grant, R. A., McArthur, A. G., Laub, M. T., and Whitney, J. C. (2019) An interbacterial toxin inhibits target cell growth by synthesizing (p)ppApp. Nature. 575, 674-678
Ahmad, M. Faiz, Wan, Q., Jha, S., Motea, E., Berdis, A., and Dealwis, C. (2012) Evaluating the therapeutic potential of a non-natural nucleotide that inhibits human ribonucleotide reductase. Mol Cancer Ther. 11, 2077-86
Ahmad, M. Faiz, Kaushal, P. Singh, Wan, Q., Wijerathna, S. R., An, X., Huang, M., and Dealwis, C. Godfrey (2012) Role of arginine 293 and glutamine 288 in communication between catalytic and allosteric sites in yeast ribonucleotide reductase. J Mol Biol. 419, 315-29

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