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1995 Faculty Publications

Abmayr, S.M., M.S. Erickson, and B.A. Bour. Embryonic Development of the Larval Body Wall Musculature of Drosophila Trends Genet. ll:l53-l59.

Bour, B.A., M.A. O'Brien, W.L. Lockwood, E.S. Goldstein, R. Bodmer, P.H. Taghert, S.M. Abmayr, and H.T. Nguyen. Drosophila MEF2, a Transcription Factor that is Essential for Myogenesis. Genes Dev. 9:730-74l.

Rushton, E., R. Drysdale, S.M. Abmayr, A.M. Michelson, and M. Bate. Mutations in a Novel Gene, Myoblast City, Provide Evidence in Support of the Founder Cell Hypothesis for Drosophila Muscle Development. Development l2l:l979-l988.

Babitzke, P. and C. Yanofsky. Structural Features of L-Tryptophan Required for Activation of TRAP, the trp RNA-Binding Attenuation Protein of Bacillus subtilis. J. Biol. Chem. 270:12452-12456.

Babitzke, P., D.G. Bear, and C. Yanofsky. TRAP, the trp RNA-binding Attenuation Protein of Bacillus subtilis, is a Toroid-shaped Molecule that Binds Transcripts Containing GAG or UAG Repeats Separated by Two Nucleotides. Proc. Natl. Acad. Sci USA 92:1-5.

Enrique, M., P. Babitzke, and C. Yanofsky. trpRNA-Binding Attenuation Protein (TRAP)-trpLeader RNA Interactions Mediate Translational as well as Transcriptional Regulation of the Bacillus subtilis trp Operon. J. Bacteriol. 177:6362-6370.

Bollinger, J.M., Jr., D.S. Kwon, G.W. Huisman, R. Kolter, and C.T. Walsh. Glutathionylspermidine Metabolism in E. coli: Purification, Cloning, Overproduction and Characterization of a Bifunctional Glutathionylspermidine Synthetase/Amidase. J. Biol. Chem. 270:l403l-l404l.

Bollinger, J.M., Jr., W.H. Tong, N. Ravi, B.H. Huynh, D.E. Edmondson, and J. Stubbe. Use of Rapid Kinetics Methods to Study the Assembly of the Diferric-Tyrosyl Radical Cofactor of E. coli Ribonucleotide Reductase. Methods Enzymol. 258:278-303.

Hidalgo, E., J. M. Bollinger, Jr., T.M. Bradley, C.T. Walsh, B. Demple. Binuclear FeS Centers in the Escherichia coli SoxR Protein and Role of the Metal Centers in Transcription. J. Biol. Chem. 270:20908-209l4.

Pulver, S.C., W.H. Tong, J. M. Bollinger, Jr., J. Stubbe, and E.I. Solomon. Circular Dichroism and Magnetic Circular Dichroism Studies of the Fully Reduced Binuclear Non-Heme Iron Active Site in the Escherichia coli R2 Subunit of Ribonucleoside Diphosphate Reductase. J. Am. Chem. Soc. ll7:l2664-l2687.

Gutshall, K., D. Trimbur, J. Kasmir, and J. Brenchley. Analysis of a Novel Gene and b-Galactosidase Isozyme from a Psychrotrophic Arthrobacter Isolate. J. Bacteriol. l77:l98l-l988.

Chung, S., C.U. Jakobs, J.G. Ormerod, and D.A. Bryant. Protein Components of Chlorosomes from Chlorobium tepidum and Interposon Mutagenesis of csmA and csmC from Chlorobium vibrioforme 8327D. In: Photosynthesis: from Light to Biosphere. (P. Mathis, ed.), Vol. I, pp. ll-l6, Kluwer, Dordrecht, Netherlands.

Debreczeny, M.P., K. Sauer, J. Zhou, and D.A. Bryant. Comparison of Calculated and Experimentally Resolved Rate Constants for Excitation Energy Transfer in C-Phycocyanin. 1. Monomers. J. Phys. Chem. 99:8412-8419.

Debreczeny, M.P., K. Sauer, J. Zhou, and D.A. Bryant. Comparison of Calculated and Experimentally Resolved Rate Constants for Excitation Energy Transfer in C-Phycocyanin. 2. Trimers. J. Phys. Chem. 99:8420-8431.

Jung, Y.-S., J. Yu, L. Yu, J. Zhao, D.A. Bryant, L. McIntosh, and J.H. Golbeck. In vivo Site-directed Mutations of the Cysteine Ligands to F_A and F_B in Synechocystis sp. PCC 8603: A Comparison with in vitro Reconstituted Photosystem I Complexes. In: Photosynthesis: from Light to Biosphere. (P. Mathis, ed.), Vol. II, pp. l27-l30, Kluwer, Dordrecht, Netherlands.

Mehari, T., F. Qiao, M.P. Scott, D.F. Nellis, J. Zhao, D.A. Bryant, and J.H. Golbeck. Modified Ligands to F_A and F_>B in Photosystem I. I. Structural Constraints for the Formation of Iron-sulfur Clusters in Free and Rebound PsaC. J. Biol. Chem. 270:28108-28117.

Shen, G., and D.A. Bryant. Characterization of a Synechococcus sp. Strain PCC 7002 Mutant Lacking Photosystem I. Protein Assembly and Energy Distribution in the Absence of the Photosystem I Reaction Center Core Complex. Photosynth. Res. 44:41-53.

Shevelev, E., D.A. Bryant, W. Loffelhardt, and H.J. Bohnert. Ribonuclease-P RNA Gene of the Plastid Chromosome from Cyanophora Paradoxa. DNA Res. 2:231-234.

Stirewalt, V.L., C.B. Michalowski, W. Loffelhardt, H.J. Bohnert, and D.A. Bryant. Nucleotide Sequence of the Cyanelle Genome from Cyanophora Paradoxa. Plant Mol. Biol. Reporter 13:327-332.

Xia, Z., R.W. Broadhurst, E.D. Laue, D.A. Bryant, J.H. Golbeck, and D.S. Bendall. Spectroscopic Evidence for the Flexibility of PsaD in Solution. In: Photosynthesis: from Light to Biosphere. (P. Mathis, ed.), Vol. II, pp.74l-744, Kluwer, Dordrecht, Netherlands.

Yu, L., I.R. Vassiliev, Y-S. Jung, D.A. Bryant, and J.H. Golbeck. Modified Ligands to F_A and F_B in Photosystem I. II. Characterization of a Mixed Ligand [4Fe-4S] Cluster in the C51D Mutant of PsaC Upon Rebinding to P700-F_X Cores. J. Biol. Chem. 270:28118-28125.

Yu, L., D.A. Bryant, and J.H. Golbeck. Evidence for a Mixed-Ligand [4Fe-4S] Cluster in the Cl4D Mutant of PsaC. Altered Reduction Potentials and EPR Spectral Properties of the F_A and F_B Clusters on Rebinding to the P700-F_X Core. Biochemistry 34:7861-7868.

Banerjee, S., F. Anderson, and G.K. Farber. The Evolution of Sugar Isomerases. Prot. Eng. 8:1189-1195.

Farber, G.K. It's Show Time. Current Biology 5:l088-l090.

Reardon, D., and G.K. Farber. The Structure and Evolution of a/b Barrel Proteins. FASEB J. 9:497-503.

Stoddard, B.L., and G.K. Farber. Direct Measurement of Reactivity in the Protein Crystal by Steady-State Kinetic Studies. Structure 3:99l-996.

Yennawar, H.P., Yennawar, N.Y., and G.K. Farber. A Structural Explanation for Enzyme Memory in Nonaqueous Solvents. J. Am. Chem . Soc. ll7:577-585.

Alber, B.E., and J.G. Ferry. Purification of Carbonic Anhydrase from Methanosarcina thermophila. In: Archaea, A Laboratory Manual. (F.T. Robb, A.R. Place, K.R. Sowers, H.J. Schreier, S. DasSarma and E.M. Fleischmann, eds.), pp. 243-246, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.

Baron, S.F., and J.G. Ferry. Purification of the Coenzyme F₄₂₀-reducing Hydrogenase from Methanobacterium formicicum. In: Archaea, A Laboratory Manual. (F.T. Robb, A.R. Place, K.R. Sowers, H.J. Schreier, S. DasSarma and E.M. Fleischmann, eds.), pp. 217-220, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.

Clements, A.P., and J.G. Ferry. Purification of the Carbon Monoxide Dehydrogenase-linked Ferredoxin from Methanosarcina thermophila. In: Archaea, A Laboratory Manual. (F.T. Robb, A.R. Place, K.R. Sowers, H.J. Schreier, S. DasSarma and E.M. Fleischmann, eds.), pp. 237-241, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.

Ferry, J.G. CO Dehydrogenase. Annu. Rev. Microbiol. 49:305-333.

Latimer, M.T., and J.G. Ferry. Purification of Methanosarcina thermophila Acetate Kinase and Phosphotransacetylase Overproduced in Escherichia coli. In: Archaea, A Laboratory Manual. (F.T. Robb, A.R. Place, K.R. Sowers, H.J. Schreier, S. DasSarma and E.M. Fleischmann, eds.), pp. 225-230, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.

Maupin-Furlow, J.A., and J.G. Ferry. A Proteasome from the Methanogenic Archaeon Methanosarcina thermophila. J. Biol. Chem. 270:28617-28622.

Rasche, M.E., K.C. Terlesky, D.R. Abbanat, and J.G. Ferry. Purification of Carbon Monoxide Dehydrogenase from Methanosarcina thermophila. In: Archaea, A Laboratory Manual. (F.T. Robb, A.R. Place, K.R. Sowers, H.J. Schreier, S. DasSarma and E.M. Fleischmann, eds.), pp. 231-235, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.

Schauer, N.L., and J.G. Ferry. Purification of formate Dehydrogenase from Methanobacterium formicicum. In: Archaea, A Laboratory Manual. (F.T. Robb, A.R. Place, K.R. Sowers, H.J. Schreier, S. DasSarma and E.M. Fleischmann, eds.), pp. 221-224, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.

Singh-Wissmann, K., and J.G. Ferry. Transcriptional Regulation of the Phosphotransacetylase-Encoding and Acetate Kinase-Encoding Genes (pta and ack) from Methanosarcina thermophila. J. Bacteriol. 177:1699-1702.

Chen, N.N., C.-F. Chang, G.L. Gallia, D.A. Kerr, E.M. Johnson, C.P. Krachmarov, S. Barr, R.J. Frisque, B. Bollag, and K. Khalili. Cooperative Action of Cellular Proteins YB-l and Pura with the Tumor Antigen of the Human JC Polyomavirus Determines Their Interaction with the Viral Lytic Control Element. Proc. Natl. Acad. Sci. USA 92:l087-l09l.

Frisque, R.J., G. Barbanti-Brodano, L.V. Crawford, S.D. Gardner, P.M. Howley, G. Orth, K.V. Shah, J. van der Noordaa, and H. zur Hausen. The Papovaviridae. In: Virus Taxonomy: Sixth Report of the International Committee on Taxonomy of Viruses, Arch. Virol., Supplement l0. (F.A. Murphy, C.M. Fauquet, D.H.L. Bishop, S.A. Ghabrial, A.W. Jarvis, G.P. Martelli, M.A. Mayo, and M.D. Summers, eds.), pp. 136-142, Springer-Verlag, Wien, N. Y.

O'Neill, F.J., R.J. Frisque, X. Xu, Y. Hu, and H. Carney. Immortalization of Human Cells by Mutant and Chimeric Primate Polyomavirus T-antigen Genes. Oncogene l0:ll3l-ll39.

Trowbridge, P.W., and R.J. Frisque. Identification of Three New JC Virus Proteins Generated by Alternative Splicing of the Early Viral mRNA. J. NeuroVirology l:l95-206.

Swenson, J.J., and R.J. Frisque. Biochemical Characterization and Localization of JC Virus Large T Antigen Phosphorylation Domains. Virology 2l2:295-308.

Gay, C.V., and Q.P. Lloyd. Characterization of Calcium Efflux by Osteoblasts Derived from Long Bone Periosteum. Comp. Biochem. Physiol. 111A:257-26l.

Guillemin, G., S.J. Hunter, and C.V. Gay. Resorption of Natural Calcium Carbonate by Avian Osteoclasts in vitro. Cells and Materials 5:l57-l65.

Lloyd, Q.P., M.A. Kuhn, and C.V. Gay. Characterization of Calcium Translocation Across the Plasma Membrane of Primary Osteoblasts Using a Lipophilic Calcium-sensitive Fluorescent Dye, Calcium Green C₁₈. J. Biol. Chem. 270:22445-22451.

Gilmour, D.S. UV Crosslinking of DNA-protein Complexes in vitro. Methods Mol. Cell Biol. 5:162-168.

Weber, J.A., and D.S. Gilmour. Genomic Footprinting of the hsp70 and Histone H3 Promoters in Drosophila Embryos Reveals Novel Protein-DNA Interactions. Nucleic Acids Res. 23:3327-3334.

Andrews, J.C., J.P. Nolan, R.H. Hammerstedt, and B.D. Bavister. Characterization of N-(6-Methoxy-8-Quinolyl)-p-Toluenesulfonamide for the Detection of Zinc in Living Sperm Cells. Cytometry 2l:l53-l59.

Hammerstedt, R.H. Cryopreservation of Poultry Semen-Current Status and Economics. In: Proceedings of the First International Congress in Artificial Insemination in Poultry. (M.R. Bakst and G.J. Wishart, eds.), pp. 229-250, Poultry Science Association, Savoy, IL.

Nolan, J.P., S.F. Magargee, R.G. Posner, and R.H. Hammerstedt. Flow Cytometric Analysis of Transmembrane Phospholipid Movement in Bull Sperm. Biochemistry 34:3907-39l5.

Hardison, R., L. Elnitsky, A. Goldstrohm, A. El Sherbini, C. Riemer, S. Schwartz, N. Stojanovic, and W. Miller. Globin Gene Server: An Aid to Studying the Regulation of Mammalian Globin Genes. In: Molecular Biology of Hemoglobin Switching. (G. Stamatoyannopoulos, ed.), pp. 405-426, Intercept Ltd., Andover, UK.

Jackson, J., A. El Sherbini, C. Riemer, N. Stojanovic, W. Miller, and R. Hardison. Effects of Hypersensitive Sites from the þ-Globin LCR on Enhancement in Transfected Cells: Synergism Between HS3 and HS2. In: Molecular Biology of Hemoglobin Switching. (G. Stamatoyannopoulos, ed.), pp. 87-109, Intercept Ltd., Andover, UK.

James-Pederson, M., S. Yost, B. Shewchuk, T. Zeigler, R. Miller, and R. Hardison. Flanking and Intragenic Sequences Regulating the Expression of the Rabbit a-Globin Gene. J. Biol. Chem. 270:3965-3973.

Miller, W., A. El Sherbini, J. Peck, C. Riemer, S. Schwartz, N. Stojanovic, and R. Hardison. A Database for Globin Gene Expression Data. In: Proceedings of the 28th Annual Hawaii Conference on System Sciences. pp. 62-7l, Ieee Press, Philadelphia, PA.

Gilbert, S.P., M.R. Webb, M. Brune, and K.A. Johnson. Pathway of Processive ATP Hydrolysis by Kinesin. Nature 373:671-676.

Spence, R.A., W.M. Kati, K.S. Anderson, and K.A. Johnson. Mechanism of Inhibition of HIV-l Reverse Transcriptase by Nonnucleoside Inhibitors. Science 267:988-993.

Johnson, K.A. Pathway of the Microtubule-Kinesin ATPase. Biophys J. 68:s173-s179.

Johnson, K.A. Rapid Quench Kinetic Analysis of Polymerases, Adenosinetriphosphatases, and Enzyme Intermediates. Methods Enzymol. 249:38-61.

Johnson, K.A. Transient State Kinetic Analysis of Enzyme Reactions. In: Molecular Biology and Biotechnology: A Comprehensive Desk Reference. (R.A. Meyers, ed.), pp. 292-294, VCH Pub., Inc., New York, NY.

Read, S.M., E. Newbigin, A.E. Clarke, B.A. McClure, and T.-H. Kao. Disputed Ancestry: Comments on a Model for the Origin of Incompatibility in Flowering Plants. Plant Cell 7:66l-664.

Richman, A.D., T.-H. Kao, S.W. Schaeffer, and M.K. Uyenoyama. S-allele Sequence Diversity in Natural Populations of Solanum carolinense, Horsenettle. Heredity 75:405-4l5.

Treisman, J.E., Z.-C. Lai, and G.M. Rubin. Shortsighted Acts in the Decapentaplegic Pathway in Drosophila Eye Development and has Homology to a Mouse TGF-beta-responsive Gene. Development l2l:2835-2845.

Grove, D.S., S.A. Pishak, and A. M. Mastro. The Effect of a 10-day Space Flight on the Function, Phenotype, and Adhesion Molecule Expression of Splenocytes and Lymph Node Lymphocytes. Exp. Cell Res. 219:102-109.

Bates, L.G., D.S. Grove, and A. M. Mastro. Mechanisms of Activation and Suppression in Rat Nb2 Lymphoma Cells: A model for Interactions Between Prolactin and the Immune System. Exp. Cell Res. 218:567-572.

Cao, Y.-Z., A.M. Mastro, M.L. Eskew, G. Hildenbrandt, P.V. Reddy, and C.C. Reddy. The Mechanism of Sphingosine Enhancement of Phorbol Ester-mediated Phospholipase D Activation in Lymphocytes. Biochem Biophys. Res. Comm. 2l7:908-9l5.

Pazur, J.H. Coupled Gel Electrophoresis-agar Diffusion Method for the Detection of Tumor Antigens. J. Chromatogr. 663:51-57.

Pazur, J.H., F.J. Miskiel, and N.T. Marchetti. Properties and Applications of Anti-xanthan Antibodies. Carbohydr. Polymers 27:85-9l.

Phillips, A.T. Unit 4.6 Concentration, Desalting and Buffer Exchange Techniques. In: Current Protocols in Protein Science (H. Ploegh, ed.), Vol. 2, pp. 1-10, J. Wiley and Sons, Inc., New York NY.

Coleman, R.A., and B.F. Pugh. Evidence for Functional Binding and Stable Sliding of the TATA Binding Protein on Nonspecific DNA. J. Biol. Chem. 270:13850-13859.

Coleman, R.A., A.K. Taggart, L.R. Benjamin, and B.F. Pugh. Dimerization of the TATA-binding Protein. J. Biol. Chem. 270:13842-13849.

Jackson, A.J., M. Ittman, and B.F. Pugh. The BN5l Protein is a Polymerase (Pol)-specific Subunit of RNA Pol III which Reveals a Link between Pol III Transcription and pre-rRNA Processing. Mol. Cell Biol. l5:94-l0l.

Pugh, B.F. Preparation of HeLa Nuclear Extracts. In: Methods in Molecular Biology, In Vitro Transcription and Translation Protocols (M.J. Tymms, ed.), Vol. 37, pp. 349-358, Humana Press, Inc., Totowa, N.J.

Pugh, B.F. Purification of the Human TATA-binding Protein, TBP. In: Methods in Molecular Biology, In Vitro Transcription and Translation Protocols (M.J. Tymms, ed.), Vol. 37, pp. 359-367, Humana Press, Inc., Totowa, N.J.

Bevers, E.M., T. Wiedmer, P. Confurius, J. Zhao, E.F. Smeets, R.A. Schlegel, A.J. Schroit, H.J. Weiss, P. Williamson, R.F.A. Zwaal, and P.J. Sims. The Complex of Phosphatidylinositol 4,5-biphosphate and Calcium Ions is not Responsible for Ca²⁺-induced Loss of Phospholipid Asymmetry in the Human Erythrocyte: A Study in Scott Syndrome, a Disorder of Calcium-induced Phospholipid Scrambling. Blood 86:1983-1991.

Halleck, M.S., S. Pownall, K.W. Harder, A.M.V. Duncan, F.R. Jirik, and R.A. Schlegel. A Widely-distributed Putative Mammalian Transcriptional Regulator Containing Multiple Paired Amphipathic Helices, with Similarity to Yeast SIN3. Genomics 26:403-406.

Verhoven, B., R.A. Schlegel, and P. Williamson. Mechanisms of Phosphatidylserine Exposure, a Phagocytic Recognition Signal, on Apoptotic T Lymphocytes. J. Exp. Med. 182-1597-160l.

Williamson, P., E.M. Bevers, E.F. Smeets, P. Comfurius, R.A. Schlegel, and R.F.A. Zwaal. Continuous Analysis of the Mechanisms of Activated Transbilayer Lipid Movement in Platelets. Biochemistry 34:10448-10455.

Patterton, H.-G., and R.T. Simpson. Modified Curved DNA that could Allow Local DNA Underwinding at the Nucleosomal Pseudodyad Fails to Position a Nucleosome in vivo. Nucleic Acids Res. 23:4l70-4l79.

Banci, L., I. Bertini, R. Pierattelli, M. Tien, and A.J. Vila. Factoring of the Hyperfine Shifts in the Cyanide Adduct of Lignin Peroxidase from Phanerochaete Chrysosporium. J. Am. Chem. Soc. ll7:8659-8667.

Koduri, R.S. and M. Tien. Oxidation of Guaiacol by Lignin Peroxidase: Role of Veratryl Alcohol. J. Biol. Chem. 270:22254-22258.

Orth, A.B., M. Rzhetskaya, E.A. Pell, and M. Tien. A Ser(Thr) Protein Kinase Confers Fungicide Resistance in the Phytopathogenic Fungus Ustilago maydis. Appl. Environ. Microbiol. 6l:234l-2345.

Orth, A.B., and M. Tien. Biotechnology of Lignin Degradation (Invited Review). In: The Mycota II Genetics and Biotechnology. (Kuch, ed.), pp. 287-302. Springer-Verlag, Berlin, Heidelberg.

Whitwam, R.E., I.G. Gazarian, and M. Tien. Expression of Fungal Mn Peroxidase in E. coli and Refolding to Yield Active Enzyme. Biochem. Biophys. Res. Commun. 2l6:l0l3-l0l7.

Lee, H.-C., Y.-P.S. Toung, Y.-S.L. Tu, and C.-P.D. Tu. A Molecular Genetic Approach for the Identification of Essential Residues in Human Glutathione S-Transferase Function in Escherichia coli. J. Biol. Chem. 270:99-109.

Lee, H.-C., and C.-P.D. Tu. Drosophila Glutathione S-Transferase D27:Functional Analysis of Two Consecutive Tyrosines Near the N-Terminus. Biochem. Biophys. Res. Comm. 209:327-334.

Reddy, P.M.S., C.-P.D. Tu, and R. Wu. Glutathione S-Transferases in Tracheobrochial Epithelium: Differential Expression and Regulation by Vitamin A, Phorbol Ester, and Collagen Substratum. Am. J. Physiol. 269:L473-L48l.

Tang, A.H., and C.-P.D. Tu. Pentobarbital-Induced Changes in Drosophila Glutathione S-Transferases D2l mRNA Stability. J. Biol. Chem. 270:l38l9-l3825.

Weinander, R., E. Mosialou, J.L. DeJong, C.-P.D. Tu, T. Bergman, H.J. Barnes, J.-O. Hoog and R. Morgenstern. Heterologous Expression of Rat Liver Microsomal Glutathione S-Transferase in Simian COS-Cells and Escherichia coli. Biochem. J. 3ll:86l-866.

Wedler, F.C. Equilibrium Isotope Exchange in Enzyme Catalysis. In: Methods in Enzymology: Enzyme Kinetics and Mechanism -- Part D. (D.L. Purich, ed.), Vol. 249, Chapter 17, pp. 443-479, Academic Press, San Diego, CA.

Adams, C.C., and J.L. Workman. Binding of Disparate Transcriptional Activators to Nucleosomal DNA is Inherently Cooperative. Mol. Cell Biol. l5:l405-l42l.

Cote, J., R.T. Utley, and J.L. Workman. Basic Analysis of Transcription Factor Binding to Nucleosomes. Methods Mol. Genet. 6:108-128.

Vettese-Dadey, M., C.C. Adams, J. Cote, P.P. Walter, and J.L. Workman. Experimental Analysis of Transcription Factor/Nucleosome Interactions. Methods Mol. Genet. 6:129-152.

Walter, P.P., T.A. Owen-Hughes, J. Cote, and J.L. Workman. Stimulation of Transcription Factor Binding and Histone Displacement by Nucleosome Assembly Protein l (NAP-l) and Nucleoplasmin Requires Disruption of the Histone Octamer. Mol. Cell Biol. l5:6l78-6l87.

Walter, P.P., M. Vettese-Dadey, J. Cote, C.C. Adams, L.-J. Juan, R. Utley, and J.L. Workman. Mechanism and Consequences of Transcription Factor Binding to Nucleosomes. In: The Nucleus, Vol. l, (A.P. Wolffe, ed.), pp. 79-l00, JAI Press, Greenwich, NY.