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Daniel H. Ramirez
Researcher at Harvard University
Publications - 6
Citations - 136
Daniel H. Ramirez is an academic researcher from Harvard University. The author has contributed to research in topics: Target protein & Tetratricopeptide. The author has an hindex of 3, co-authored 6 publications receiving 51 citations. Previous affiliations of Daniel H. Ramirez include Carnegie Institution for Science & University of Texas at El Paso.
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Journal ArticleDOI
Engineering a Proximity-Directed O-GlcNAc Transferase for Selective Protein O-GlcNAcylation in Cells.
Daniel H. Ramirez,Chanat Aonbangkhen,Hung-Yi Wu,Jeffrey A. Naftaly,Stephanie Tang,Timothy R. O’Meara,Christina M. Woo +6 more
TL;DR: These first proximity-directed OGT constructs provide a flexible strategy for targeting additional proteins and a template for further engineering of OGT and the O-GlcNAc proteome in the future.
Journal ArticleDOI
Target protein deglycosylation in living cells by a nanobody-fused split O-GlcNAcase.
Yun Ge,Daniel H. Ramirez,Bo Yang,Alexandria K. D’Souza,Chanat Aonbangkhen,Stephanie M. Wong,Christina M. Woo +6 more
TL;DR: In this article, a nanobody-fused split O-GlcNAcase (OGA) was used as an eraser for selective deglycosylation of a target protein in cells.
Journal ArticleDOI
Truncation of the TPR domain of OGT alters substrate and glycosite selection
Daniel H. Ramirez,Daniel H. Ramirez,Bo Yang,Alexandria K. D’Souza,Dacheng Shen,Christina M. Woo +5 more
TL;DR: In this article, the effects of iterative truncations to the TPR domain of OGT on substrate and glycosite selection with the model protein GFP-JunB and the surrounding O-GlcNAc proteome in U2OS cells were investigated.
Journal ArticleDOI
O-GlcNAc Engineering on a Target Protein in Cells with Nanobody-OGT and Nanobody-splitOGA.
TL;DR: In this article, the role of O-GlcNAc on a target protein is investigated using nanobody-OGT/nanobody split O-glcNAcase (OGA) fused to a nano-body.
Journal ArticleDOI
Expression and in vitro functional analyses of recombinant Gam1 protein
Gustavo A. Avila,Daniel H. Ramirez,Zacariah L. Hildenbrand,Pedro Jacquez,Susanna Chiocca,Jianjun Sun,Germán Rosas-Acosta,Chuan Xiao +7 more
TL;DR: Careful optimization indicates that both low temperature induction and the chaperone function of TF play critical roles in increasing Gam1 solubility and built the foundation for further structural investigations that will broaden the understanding of Gam1's roles in viral replication.