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Chris Sander

Researcher at Harvard University

Publications -  730
Citations -  273726

Chris Sander is an academic researcher from Harvard University. The author has contributed to research in topics: Large Hadron Collider & Protein structure. The author has an hindex of 178, co-authored 713 publications receiving 233287 citations. Previous affiliations of Chris Sander include Purdue University & University of Leeds.

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Characterization of small RNAs in Aplysia reveals a role for miR-124 in constraining synaptic plasticity through CREB.

TL;DR: Direct evidence is presented that a modulatory neurotransmitter important for learning can regulate the levels of small RNAs and a role for miR-124 in long-term plasticity of synapses in the mature nervous system is presented.
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Convergent Evolution of Similar Enzymatic Function on Different Protein Folds: The Hexokinase, Ribokinase, and Galactokinase Families of Sugar Kinases

TL;DR: The three‐dimensional structure of hexokinase is known and can be used to build models of functionally important regions of other kinases in this family, which contains many prokaryotic and eukaryotic sugar kinases with diverse specificities, including a new member, rhamnokinase from Salmonella typhimurium.
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Pattern discovery and cancer gene identification in integrated cancer genomic data

TL;DR: This work proposes a framework for joint modeling of discrete and continuous variables that arise from integrated genomic, epigenomic, and transcriptomic profiling, motivated by the hypothesis that diverse molecular phenotypes can be predicted by a set of orthogonal latent variables that represent distinct molecular drivers, and thus can reveal tumor subgroups of biological and clinical importance.
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On the use of sequence homologies to predict protein structure: identical pentapeptides can have completely different conformations

TL;DR: In 62 proteins with 10,000 residues, it is found that the longest isolated homologies between unrelated proteins are five residues long, which shows quantitatively that pentapeptide structure within a protein is strongly dependent on sequence context.