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Journal of Molecular Biology|November 5, 1989
Glycera dibranchiata hemoglobin. Structure and refinement at 1.5 A resolutionG Arents, W E LoveJournal of Molecular Biology|April 22, 1994
Glycera dibranchiata hemoglobin. X-ray structure of carbonmonoxide hemoglobin at 1.5 A resolutionB C Braden, G Arents, E A Padlan, et al.Proceedings of the National Academy of Sciences of the United States of America|November 15, 1991
The nucleosomal core histone octamer at 3.1 A resolution: a tripartite protein assembly and a left-handed superhelixG Arents, R W Burlingame, B C Wang, et al.Proceedings of the National Academy of Sciences of the United States of America|November 21, 1995
The histone fold: a ubiquitous architectural motif utilized in DNA compaction and protein dimerizationG Arents, E N MoudrianakisProceedings of the National Academy of Sciences of the United States of America|November 15, 1993
Topography of the histone octamer surface: repeating structural motifs utilized in the docking of nucleosomal DNAG Arents, E N MoudrianakisThe Journal of Biological Chemistry|July 15, 1985
Refined crystal structure of deoxyhemoglobin S. I. Restrained least-squares refinement at 3.0-A resolutionE A Padlan, W E LoveThe Journal of Biological Chemistry|July 15, 1985
Refined crystal structure of deoxyhemoglobin S. II. Molecular interactions in the crystalE A Padlan, W E LoveJournal of Molecular Biology|February 11, 1994
The octameric histone core of the nucleosome. Structural issues resolvedB C Wang, J Rose, G Arents, et al.Nucleic Acids Research|July 25, 1995
A variety of DNA-binding and multimeric proteins contain the histone fold motifA D Baxevanis, G Arents, E N Moudrianakis, et al.The EMBO Journal|May 1, 1997
Histone octamer function in vivo: mutations in the dimer-tetramer interfaces disrupt both gene activation and repressionM S Santisteban, G Arents, E N Moudrianakis, et al.Pageof 2