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Guillermo A. Calero, Ph.D.

Affiliations: 
2003 Cornell University, Ithaca, NY, United States 
Area:
natural products
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"Guillermo Calero"
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Jon C. Clardy grad student 2003 Cornell
 (X-ray crystallographic studies of signaling regulators.)

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Publications

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Vergara S, Zhou X, Santiago U, et al. (2023) Structures of kinetic intermediate states of HIV-1 reverse transcriptase DNA synthesis. Biorxiv : the Preprint Server For Biology
Lin G, Barnes CO, Weiss S, et al. (2023) Structural basis of transcription: RNA Polymerase II substrate binding and metal coordination at 3.0 Å using a free-electron laser. Biorxiv : the Preprint Server For Biology
Sarkar S, Runge B, Russell RW, et al. (2022) Atomic-Resolution Structure of SARS-CoV-2 Nucleocapsid Protein N-Terminal Domain. Journal of the American Chemical Society. 144: 10543-10555
Byeon IL, Calero G, Wu Y, et al. (2021) Structure of HIV-1 Vpr in complex with the human nucleotide excision repair protein hHR23A. Nature Communications. 12: 6864
Barnes CO, Wu Y, Song J, et al. (2019) The crystal structure of dGTPase reveals the molecular basis of dGTP selectivity. Proceedings of the National Academy of Sciences of the United States of America
de la Cruz MJ, Hattne J, Shi D, et al. (2017) Atomic-resolution structures from fragmented protein crystals with the cryoEM method MicroED. Nature Methods
Wu Y, Zhou X, Barnes CO, et al. (2016) The DDB1-DCAF1-Vpr-UNG2 crystal structure reveals how HIV-1 Vpr steers human UNG2 toward destruction. Nature Structural & Molecular Biology
Barnes CO, Calero M, Malik I, et al. (2015) Crystal Structure of a Transcribing RNA Polymerase II Complex Reveals a Complete Transcription Bubble. Molecular Cell. 59: 258-69
Wu Y, Koharudin LM, Mehrens J, et al. (2015) Structural Basis of Clade-specific Engagement of SAMHD1 (Sterile α Motif and Histidine/Aspartate-containing Protein 1) Restriction Factors by Lentiviral Viral Protein X (Vpx) Virulence Factors. The Journal of Biological Chemistry. 290: 17935-45
Arjunan P, Wang J, Nemeria NS, et al. (2014) Novel binding motif and new flexibility revealed by structural analyses of a pyruvate dehydrogenase-dihydrolipoyl acetyltransferase subcomplex from the Escherichia coli pyruvate dehydrogenase multienzyme complex. The Journal of Biological Chemistry. 289: 30161-76
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