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Karki, A., Campbell K. B, Mozumder, S., Fisher, A. J., and Beal, P. A. (2024). Impact of Disease-Associated Mutations on the Deaminase Activity of ADAR1. Biochemistry, 63:282-293 (PMID: 38190734)

Feng, Y., Lyu, X., Cong, Y., Miao, T., Fang, B., Zhang, C., Shen, Q., Matthews, M., Fisher, A. J., Zhang, J. Z. H., Zhang, L., and Yang, R. (2023) A precise swaying map for how promiscuous cellobiose-2-epimerase operate bi-reaction. Int. J. Bio. Macromol. 253:127093.  (PMID: 37758108)

Doherty, E., Karki, A., Wilcox, X., Mendoza, H., Manjunath, A., Jauregui-Matos, V., Fisher, A. J., and Beal, P. A. (2022). ADAR Activation by Inducing a Syn Conformation at Guanosine Adjacent to an Editing Site. Nucleic Acids Res., 50:10857-10868.

Liu, L., Wilcox, X., Fisher, A. J., Boyd, S. D., Zhi, J., Winkler, D. D., Bulla, L. A.(2022). Functional and Structural Analysis of the Toxin-Binding Site of the Cadherin G‑Protein-Coupled Receptor, BT‑R1, for Cry1A Toxins of Bacillus thuringiensis. Biochemistry. 61:752-766.

Mohanty, A. K., Choudhary, S., Kaushik, J. K., and Fisher, A. J. (2021). Crystal structure of breast regression protein 39 (BRP39), a signaling glycoprotein expressed during mammary gland apoptosis, at 2.6 Å resolution. J. Struct. Biol., 213:107737.   (PMID: 33838225)


Doherty, E., Wilcox, X., van Sint Fiet, L., Kemmel, C., Turunen, J., Klein, B., Tantillo, D., Fisher, A. J., and Beal, P. A. (2021). Rational Design of RNA Editing Guide Strands: Cytidine Analogs at the Orphan Position. J. Am. Chem. Soc., 143:6865-6876.

Yu, Q., Anderson, D. E., Kaur, R., Fisher, A. J. and Ames, J. B. (2021). The Crystal Structure of Calmodulin Bound to the Cardiac Ryanodine Receptor (RyR2) at Residues Phe4246-Val4271 Reveals a Fifth Calcium Binding Site. Biochemistry 60:1088–1096.

Unger, E. K., Keller, J. P., Altermatt, M., Liang, R., Matsui, A., Dong, C., Hon, O. J., Yao, Z., Sun, J., Banala, S., Flanigan, M. E., Jaffe, D. A., Hartanto, S., Carlen, J., Mizuno, G. O., Borden, P. M., Shivange, A. V., Cameron, L. P., Sinning, S., Underhill, S. M., Olson, D. E., Amara, S. G., Temple Lang, D., Rudnick, G., Marvin, J. S., Lavis, L. D., Lester, H. A., Alvarez, V. A., Fisher, A. J., Prescher, J. A., Kash, T. L., Yarov-Yarovoy, V., Gradinaru, V., Looger, L. L., and Tian, L. (2020). Directed Evolution of a Selective and Sensitive Serotonin Sensor via Machine Learning.  Cell  183:1986-2002

Moreno, M. V., Rockwell, N. C., Mora, M., Fisher, A. J., and Lagarias, J. C. (2020). A far-red cyanobacteriochrome lineage specific for verdins. Proc. Natl. Acad. Sci. U.S.A117:27962-27970.

Hurlburt, N. K., Guan, J., Ong, H., Yu, H., Chen, X., and Fisher, A. J. (2020). Structural characterization of a non-hydrolyzing UDP-GlcNAc 2-epimerase from Neisseria meningitidis serogroup A.  Acta Crystallogr. F Struct. Biol. Commun. 76:557-567.

Feng, Y., Hua, X., Shen, Q., Matthews, M., Zhang, Y., Fisher, A. J., Lyu, X., and Yang, R. (2020) Insight into the potential factors influencing the catalytic direction in cellobiose 2-epimerase by crystallization and mutagenesis. Acta Crystallogr. D Struct. Biol. 76:1104-1113.

Matthews, M. M., McArthur, J. B., Li, Y., Yu, H., Chen, X., Fisher, A. J. (2020). Catalytic cycle of Neisseria meningitidis CMP-sialic acid synthetase illustrated by high-resolution protein crystallography. Biochemistry59:3157-3168. [PDF Reprint]

Thuy-Boun, A. S., Thomas, J. M., Grajo, H. L., Palumbo, C. M., Park, S., Nguyen, L. T., Fisher, A. J., and Beal, P. A. (2020). Asymmetric Dimerization of Adenosine Deaminase acting on RNA Facilitates Substrate Recognition. Nucleic Acids Res.48:7958-7972. [PDF Reprint]

Li, Y., Li, R., Yu, H., Sheng, X., Wang, J., Fisher, A. J., Chen, X. (2020). Enterococcus faecalis α1–2-mannosidase (EfMan-I): an efficient catalyst for glycoprotein N-glycan modification. FEBS Letters 594:439-451. [PDF Reprint]

Monteleone, L. R., Matthews, M. M., Palumbo, C. M., Thomas, J. M., Zheng, Y., Chiang, Y, Fisher, A., J., and Beal, P. A. (2019). A bump-hole approach for directed RNA editing. Cell Chem. Biol. 26:269-277. [PDF Reprint]

Hurlburt, N. K., Chen, L. H., Stergiopoulos, I., and Fisher, A. J. (2018). Structure of the Cladosporium fulvum Avr4 effector in complex with (GlcNAc)6 reveals the ligand-binding mechanism and uncouples its intrinsic function from recognition by the Cf-4 resistance protein. PLoS Pathog. 14(8):e1007263. [PDF Reprint]

Fisher, A. J., and Beal, P. A. (2018). Structural basis for eukaryotic mRNA modification. Curr. Opin. Struct. Biol. 53:59-68. [PDF Reprint]

McArthur, J. B., Yu, H., Tasnima, N., Lee, C. M., Fisher, A. J., and Chen, X. (2018). α2-6-Neosialidase: A sialyltransferase mutant as a sialyl linkage-specific sialidase. ACS Chemical Biology 13:1228-1234. [PDF Reprint]

Lal, N. K., Nagalakshmi, U., Hurlburt, N. K., Flores, R., Bak, A., Sone, P., Ma, X., Song, G., Walley, J., Shan, L., He, P., Casteel, C., Fisher, A. J., Dinesh-Kumar, S. P. (2018). The Receptor-like Cytoplasmic Kinase BIK1 Localizes to the Nucleus and Regulates Defense Hormone Expression during Plant Innate Immunity. Cell & Host Microbe  23:485-497.  [PDF Reprint]

Sauter, S. R., Ball-Jones, A., Mumbleau, M. M., Valenzuela, R., Ibarra-Soza, J., Owens, H., Fisher, A. J., and Beal, P. A. (2017). Controlling miRNA-like Off-target Effects of an siRNA with Nucleobase Modifications. Org. Biomol. Chem. 15:10029-10036. [PDF Reprint]

Fisher, A. J., and Beal, P. A. (2017). Effects of Aicardi-Goutières Syndrome Mutations Predicted from ADAR-RNA Structures. RNA Biology 14:164-170. [PDF Reprint]

Lal, N. K., Fisher, A. J. and Dinesh-Kumar, S. P. (2016) Arabidopsis receptor-like cytoplasmic kinase BIK1: purification, crystallization, and X-ray diffraction analysis. Acta Crystallogr. F Struct. Biol. Commun72:738-742. [PDF Reprint]

Kohler, A. C., Chen, L.-H., Hurlburt, N., Salvucci, A., Schwessinger, B., Fisher, A. J. and Stergiopoulos, I. (2016) Structural analysis of an Avr4 effector ortholog offers insight into chitin-binding and recognition by the Cf-4 receptor. Plant Cell  28:1945-1965. [PDF Reprint]

*Matthews, M. M., *Thomas, J. M., Zheng, Y., Tran, K., Phelps, K. J., Scott, A. I., Havel, J., Fisher, A. J., and Beal, P. A. (2016). Structures of human ADAR2 bound to dsRNA reveal base-flipping mechanism and basis for site selectivity. Nat. Struct. Mol. Biol23:426-433. [PDF Reprint] (*Authors contributed equally)

Erickson, A. I., Sarsam, R. D., and Fisher, A. J. (2015) Structures of Mycobacterium tuberculosis CysQ, with substrate and products bound. Biochemistry 54:6830-6841. [PDF Reprint]

Ngo, A., Fong, K. T., Cox, D. L., Chen, X., and Fisher, A. J. (2015) Structure of Bacteroides fragilis uridine 5’-diphosphate-N-acetylglucosamine (UDP-GlcNAc) acyltransferase (BfLpxA). Acta Crystallogr. D Struct. Biol71:1068-1076. [PDF Reprint]

Phelps, K., Tran, K., Eifler, T., Erickson, A. I., Fisher, A. J., and Beal, P. A. (2015) Recognition of Duplex RNA by the Deaminase Domain of the RNA Editing Enzyme ADAR2. Nucleic Acids Res43:1123-1132. [PDF Reprint]

Huynh, N., Li, Y., Hai Y., Huang, S., Lau, K., Chen, X., and Fisher, A. J. (2014) Crystal Structures of Sialyltransferase from Photobacterium damselae. FEBS Lett588:4720-4729. [PDF Reprint]

Phelps, K., Ibarra-Soza, J. M., Tran, K., Fisher, A. J., and Beal, P. A. (2014). Click Modification of RNA at Adenosine: Structure and Reactivity of 7-Ethynyl- and 7-Triazolyl-8-aza-7-deazaadenosine in RNA. ACS Chem. Bio9:1780-1787. [PDF Reprint]

Erickson, A. I., Sarsam, R. D., and Fisher, A. J. (2014) Expression, purification and preliminary crystallographic analysis of Mycobacterium tuberculosis CysQ, a phosphatase involved in sulfur metabolism. Acta Crystallogr. F Struct. Biol. Commun70:747-749. [PDF Reprint]

Huynh, N., Aye, A., Li, Y., Yu, H., Cao, H., Tiwari, V. K., Shin, D.-W., Chen, X., and Fisher, A. J. (2013) Structural basis for substrate specificity and mechanism of N-acetyl-D-neuraminic acid lyase from Pasteurella multocida. Biochemistry  52:8570-8579. [PDF Reprint]

Kabasakal, B., V., Gae, D. D., Li, J., Lagarias, J. C., Koehl, P., and Fisher, A. J. (2013) His74 conservation in the bilin reductase PcyA family reflects and important role in protein-substrate structure and dynamics. Arch. Biochem. Biophys537:233-242. [PDF Reprint]

Addington, T. A., Mertz, R. W., Siegel, J. B., Thompson, J. M., Fisher, A. J., Filkov, V.,  Fleischman, N. M., Suen, A. A., Zhang, C., and Toney, M. D. (2013) Janus: prediction and ranking of mutations required for functional interconversion of enzymes. J. Mol. Biol425:1378-1389. [PDF Reprint]

Sugiarto, G., Lau, K., Qu, J., Li, Y., Lim, S., Mu, S., Ames, J. B., Fisher, A. J., and Chen, X.  (2012). A Sialyltransferase Mutant with Decreased Donor Hydrolysis and Reduced Sialidase Activities for Directly Sialylating Lewisx. ACS Chem. Bio7:1232-1240. [PDF Reprint]

Griswold, W. R., Castro, J. N., Fisher, A. J., and Toney, M. D. (2012). Ground-State Electronic Destabilization via Hyperconjugation in Aspartate Aminotransferase.  J. Am. Chem. Soc134:8436-8438. [PDF Reprint]

Fisher, A. J. (2012). “X-ray Structure Determination of Proteins and Peptides.” Chapter 2. In: Amino Acids, Peptides and Proteins in Organic Chemistry. Hughes, A. B. (Ed.), pp. 51-96, Wiley-VCH, Weinheim, Germany. [PDF Reprint]

Griswold, W. R., Fisher, A. J., and Toney, M. D. (2011). Crystal Structure of Aspartate Aminotransferase Reconstituted with 1-Deazapyridoxal 5’-Phosphate: Internal Aldimine and  Stable L-Aspartate External Aldimine.  Biochemistry 50:5918-5924. [PDF Reprint]

Kohler, A. C., Gae, D. D., Richley M. A., Stoll S., Gunn, A., Sunghyuk Lim S., Martin S. S., Tzanko I. Doukov T. I., Britt, R. D., Ames, J. B., Lagarias, J. C., and Fisher, A. J. (2010). Structural basis for hydration dynamics in radical stabilization of bilin reductase mutants. Biochemistry 49:6206-6218. [PDF Reprint]

Gay, S. C., Segel, I. H., and Fisher, A. J. (2009). Crystal structure of the two-domain, hexameric APS kinase from Thiobacillus denitrificans: structural basis for the absence of ATP sulfurylase activity. Acta Crystallogr. D Biol. Crystallogr65:1021-1031. [PDF Reprint]

Gay, S. C., Fribourgh, J. L., Donohoue, P. D., Segel, I. H., and Fisher, A. J. (2009). Kinetic Properties of ATP Sulfurylase and APS Kinase from Thiobacillus denitrificans. Arch. Biochem. Biophys. 489:110-117. [PDF Reprint]

Stoll, S., Gunn, A., Brynda, M., Sughrue, W., Kohler, A. C., Ozarowski, A., Fisher, A. J., Lagarias, J. C., Britt, R. D. (2009). The Structure of the Biliverdin Radical Intermediate in Phycocyanobilin:Ferredoxin Oxidoreductase Identified by high-field EPR and DFT. J. Am. Chem. Soc. 131:1986-1995. [PDF Reprint]

Mohanty, A. K., Fisher, A. J., Yu, Z., Pradeep, M. A., Janjanam, J., Kaushik, J. K. (2009). Cloning, Expression, Characterization and Crystallization of BRP39, a Signaling Glycoprotein Expressed during Mammary Gland Apoptosis. Protein Expression and Purification 64:213-218. [PDF Reprint]

Yu, Z., Lemongello, D., Segel, I. H., and Fisher, A. J. (2008). Crystal structure of Saccharomyces cerevisiae 3′-Phosphoadenosine-5′-phosphosulfate Reductase complexed with adenosine 3′,5′-bisphosphate. Biochemistry 47:12777-12786. [PDF Reprint]

Wingard, J. N., Ladner, J., Vanarotti, M., Fisher, A. J., Robinson, H., Buchanan, K. T., Engman, D. M., and Ames, J. B., (2008). Structural insights into membrane-targeting by the flagellar calcium-binding protein (FCaBP), a myristolylated and palmitoylated calcium sensor in Trypanosoma cruzi. J. Biol. Chem. 283:23388-23396. [PDF Reprint]

Ni, L., Chokhawala, H. A., Cao, H., Henning, R., Ng, L., Huang, S., Yu, H., Chen, X., and Fisher, A. J. (2007). Crystal structures of Pasteurella multocida sialyltransferase complexes with acceptor and donor analogs reveal substrate binding sites and catalytic mechanism. Biochemistry 46:6288-6298. [PDF Reprint]

Murata, K., Fisher, A. J., and Hedrick, J. L., (2007). Crystallization and X-ray analysis of the salmon egg lectin, SEL24K. Acta Crystallograph Sect F Struct Biol Cryst Commun. F63:396-398. [PDF Reprint]

Tu, S.-L., Rockwell, N. C., Lagarias, J. C., and Fisher, A. J. (2007). Insight into the Radical Mechanism of Phycocyanobilin:Ferredoxin Oxidoreductase (PcyA) Revealed by X-ray Crystallography and Biochemical Measurements. Biochemistry 46:1484-1494. [PDF Reprint]

Yu, Z., Lansdon, E. B., Segel, I. H., and Fisher, A. J. (2007). Crystal Structure of the Bifunctional ATP Sulfurylase – APS Kinase from the Chemolithotrophic Thermophile Aquifex aeolicus. J. Mol. Biol. 365:732-743. [PDF Reprint]

Ni, L., Sun, M., Chokhawala, H., Chen, X, and Fisher, A. J. (2006). CMP-Induced Strctural Changes in a Multifunctional Sialyltransferase from Pasteurella multocida. Biochemistry 45:2139-2148. [PDF Reprint]

Liu, W., Peterson, P. E., Langston, J. A., Jin, X., Zhou, X., Fisher, A. J., and Toney, M. D. (2005). Kinetic and Crystallographic Analysis of Active Site Mutants of Escherichia coli γ-Aminobutyrate Aminotransferase. Biochemistry 44:2982-2992. [PDF Reprint]

Fisher, A. J., MacRae, I. J., Beynon, J. D., Lansdon, E. B., and Segel, I. H. (2004). Optimizing an enzyme for its physiological role: Structural and functional comparisons of ATP sulfurylases from three different organisms. In: Conformational Proteomics of Macromolecular Architecture. Cheng, R. H., and Hammar, L. (Eds.) World Scientific Publishing Co., London. p. 222-241.

Liu, W., Peterson, P. E., Carter, R. J., Zhou, X., Langston, J., Fisher, A. J., and Toney, M. D. (2004). Crystal Structures of Unbound and Aminooxyacetate-bound Escherichia coli γ-Aminobutyrate Aminotransferase. Biochemistry 43:10896 -10905. [PDF Reprint]

Lansdon, E. B., Fisher, A. J., and Segel, I. H. (2004). Human PAPS Synthetase (Isoform 1; Brain): Kinetic Properties of the ATP Sulfurylase and APS Kinase Domains. Biochemistry 43:4356-4365. [PDF Reprint]

Forsyth, C., M., Lemongello, D., LaCount, D. J., Friesen, P. D., and Fisher, A. J. (2004). Crystal Structure of an Invertebrate Caspase. J. Biol. Chem279:7001-7008. [PDF Reprint]

Hanna, E., Ng, K. F., MacRae, I. J., Bley, C. J., Fisher, A. J., and Segel, I. H. (2004). Kinetic and Stability Properties of P. Chrysogenum ATP Sulfurylase Missing the C-Terminal Regulatory Domain. J. Biol. Chem279:4415-4424. [PDF Reprint]

Corneillie, T. M., Fisher, A. J., and Meares, C. F. (2003). Crystal Structure of Two Complexes of the Rare Earth-DOTA-Binding Antibody 2D12.5: Ligand Generality from a Chiral System. J. Am. Chem. Soc. 125:15039-15048. [PDF Reprint]

Corneillie, T. M., Whetstone, P. A., Fisher, A. J., and Meares, C. F. (2003). A Rare Earth-DOTA-Binding Antibody: Probe Properties and Binding. J. Am. Chem. Soc. 125:3436-3437. [PDF Reprint]

MacRae, I. J., Segel, I. H., and Fisher, A. J. (2002). Allosteric Inhibition via R-State Destabilization in ATP Sulfurylase from P. chrysogenum. Nature Struc. Biol. 9:945-949. [PDF Reprint]

Lansdon, E. B., Segel, I. H., and Fisher, A. J. (2002). Ligand-Induced Structural Changes in Adenosine 5´-Phosphosulfate Kinase from Penicillium chrysogenum. Biochemistry 41:13672-13680. [PDF Reprint]

Hanna, E., MacRae, I. J., Medina, D., Fisher, A. J., and Segel, I. H. (2002). ATP Sulfurylase from the Hyperthermophilic Chemolithotroph Aquifex aeolicus. Arch. Biochem. Biophys. 406:275 -288. [PDF Reprint]

Liu, W., Rogers, C. J., Fisher, A. J., Toney, M. D. (2002). Aminophosphonate inhibitors of dialkylglycine decarboxylase: Structural basis for slow, tight binding inhibition. Biochemistry 41:12320-12328. [PDF Reprint]

Eddins, M. J., Lemongello, D., Friesen, P. D., and Fisher, A. J. (2002). Crystallization and low-resolution structure of an effector caspase-P35 complex: similarities and differences to an initiator caspase-P35 complex. Acta CrystD58:299-302. [PDF Reprint]

Beynon, J. D., MacRae, I. J., Huston, S. L., Nelson, D. C., Segel, I. H., and Fisher, A. J. (2001). Crystal Structure of Bacterial ATP Sulfurylase Isolated from the Symbiont of the Hydrothermal Vent Tubeworm Riftia pachyptila. Biochemistry 40:14509-14517. [PDF Reprint]

Medina, D., Hanna, E., MacRae, I. J., Fisher, A. J., and Segel, I. H. (2001). Temperature Effects on the Allosteric Transition of ATP Sulfurylase from Penicillium chrysogenum. Arch. Biochem. Biophys393:51-60. [PDF Reprint]

dela Cruz, W. P., Friesen, P. D., and Fisher, A. J. (2001). Crystal structure of baculovirus P35 reveals a large conformational change in the reactive site loop after caspase cleavage. J. Biol. Chem. 276:32933-32939. [PDF Reprint]

Mogilner, A., Fisher, A. J., and Baskin, R. J. (2001). Structural changes in the neck linker of kinesin explain the load dependence of the motor’s mechanical cycle. J. Theor. Biol. 211:143-157. [PDF Reprint]

MacRae, I. J., Segel, I. H., and Fisher, A. J. (2001). Crystal Structure of ATP Sulfurylase from Penicillium chrysogenum: Insights into allosteric regulation of sulfur assimilation. Biochemistry 40:6795-6804. [PDF Reprint]

MacRae, I. J., Hanna, E., Ho, J. D., Fisher, A. J., and Segel, I. H. (2000). Induction of positive cooperativity by amino acid replacements within the C-terminal domain of P. chrysogenum ATP sulfurylase. J. Biol. Chem. 275:36303-36310. [PDF Reprint]

Beynon, J. Rafanan Jr., E., R., Shen, B., and Fisher A. J. (2000). Crystallization and Preliminary X-ray analysis of Tetracenomycin A2 Oxygenase: A Flavoprotein Hydroxylase Involved in Polyketide Biosynthesis. Acta CrystD56:1647-1651. [PDF Reprint]

MacRae, I. J., Segel, I. H., and Fisher, A. J. (2000). Crystal Structure of Adenosine 5’-Phosphosulfate (APS) Kinase from Penicillium chrysogenum. Biochemistry 39:1613-1621. [PDF Reprint]

Stevenson, S., Rice, G., Glass, T., Harich, K., Cromer, F., Jordan, M. R., Craft, J., Hadju, E., Bible, R., Olmstead, M. M., Maitra, K., Fisher, A. J., Balch, A. L., and Dorn, H. C. (1999). Small-bandgap endohedral metallofullerenes in high yield and purity. Nature 401:55-57. [PDF Reprint]

Fisher, A. J., dela Cruz, W., Zoog, S. J., Schneider, C. L., and Friesen, P. D. (1999). Crystal structure of baculovirus P35: Role of a novel reactive-site loop in apoptotic caspase inhibition. EMBO J. 18:2031-2039. [PDF Reprint]

Rao-Naik, C., delaCruz, W., Laplaza, J. M., Tan, S., Callis, J., and Fisher, A. J. (1998). The Rub family of ubiquitin-like proteins: Crystal structure of Arabidopsis RUB1 and expression of multiple RUBs in Arabidopsis. J. Biol. Chem. 273:34976-34982. [PDF Reprint]

Khoury, R.G., Jaquinod, L., Aoyagi, K., Olmstead, M. M., Fisher, A. J., and Smith, K. M. (1997). A Calix[4]arenoporphyrin. Angewandte Chemie. 36: 2497-2500. [PDF Reprint]

Thoden, J. B., Holden, H. M., Fisher, A. J., Sinclair, J. F., Wesenberg, G, Baldwin, T. O., and Rayment, I. (1997). Structure of the β2 homodimer of bacterial luciferase from Vibrio harveyi: X-ray analysis of a kinetic protein folding trap. Protein Science 6:13-23. [PDF Reprint]

Fisher, A. J., Thompson, T. B., Thoden, J. B., Baldwin, T. O., and Rayment, I. (1996). The 1.5-Å resolution crystal structure of bacterial luciferase in low salt conditions. J. Biol. Chem. 271:21956-21968. [PDF Reprint]

Baldwin, T. O., Christopher, J. A., Raushel, F. M., Sinclair, J. F., Ziegler, M. M., Fisher, A. J., and Rayment, I. (1995). Structure of bacterial luciferase. Curr. Opin. Struc. Biol. 5:798-809. [PDF Reprint]

Fisher, A. J., Smith, C. A., Thoden, J., Smith, R., Sutoh, K., Holden, H. M., and Rayment, I. (1995). X-ray structures of the myosin motor domain of Dictyostelium discoideum complexed with MgADP•BeFx and MgADP•AlF4-. Biochemistry 34:8960-8972. [PDF Reprint]

Fisher, A. J., Raushel, F. M., Baldwin, T. O., and Rayment, I. (1995). The Three-dimensional structure of bacterial luciferase from Vibrio harveyi at 2.4 Å Resolution. Biochemistry 34:6581-6586. [PDF Reprint]

Fisher, A. J., Smith, C. A., Thoden, J., Smith, R., Sutoh, K., Holden, H. M., and Rayment, I. (1995). Structural studies of myosin-nucleotide complexes: A revised model for the molecular basis of muscle contraction. Biophysical J. 68:19s-28s. [PDF Reprint]

McKinney, B. R., Agrawal, D., Fisher, A. J., Johnson, J. E., Schneemann, A., and Rueckert, R. R. (1994). Production and crystallization of virus-like particles assembled in a heterologous protein expression system. Acta CrystD50:351-354. [PDF Reprint]

Johnson, J. E. and Fisher, A. J. (1994). Principles in Virus Structure, In Encyclopedia of Virology, (R. G. Webster and A. Granoff, eds), pp 1573-1586, Academic Press Inc. London.

Johnson, J. E., Munshi, S., Liljas, L., Agrawal, D., Olson, N. H., Reddy, V., Fisher, A., McKinney, B., Schmidt, T., and Baker, T. S. (1994). Comparative studies of T=3 and T=4 icosahedral RNA insect viruses. Arch. Virol. Suppl. 9:497-512. [PDF Reprint]

Cheng, R. H., Reddy, V. S., Olson, N. H., Fisher, A. J., Baker, T. S., and Johnson, J. E. (1994). Functional implications of quasi-equivalence in a T=3 icosahedral animal virus established by cryo-electron microscopy and X-ray crystallography. Structure 2:271-282. [PDF Reprint]

Fisher, A. J., McKinney, B. R., Schneemann, A., Rueckert, R. R., and Johnson, J. E. (1993). Crystallization of virus-like particles assembled from Flock House virus coat protein expressed in a baculovirus system. J. Virol. 67:2950-2953. [PDF Reprint]

Fisher, A. J. and Johnson, J. E. (1993). Ordered duplex RNA controls capsid architecture in an icosahedral animal virus. Nature 361:176-179. [PDF Reprint]

Fisher, A. J., McKinney, B. R., Wery, J.-P., and Johnson, J. E. (1992). Crystallization and preliminary data analysis of Flock House virus. Acta CrystB48:515-520. [PDF Reprint]

Chen, Z., Stauffacher, C., Schmidt, T., Fisher, A. and Johnson, J. E., (1990). RNA packaging in bean pod mottle virus. In New Aspects of Positive-Strand RNA Virus, (M.A. Brinton and F.X. Heinz, eds), pp 218-226, Amer. Soc. Microbiol. Press, Washington, D.C.