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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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miR-122, a mammalian liver-specific microRNA, is processed from hcr mRNA and may downregulate the high affinity cationic amino acid transporter CAT-1.

TL;DR: These studies show that miR-122, a 22-nucleotide microRNA, is derived from a liver-specific non-coding polyadenylated RNA transcribed from the gene hcr, which may be a specific mRNA target, CAT-1, which is expressed in all mammaliantissues but with lower levels in adult liver.
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Enlarged representative set of protein structures

Uwe Hobohm, +1 more
- 01 Mar 1994 - 
TL;DR: To reduce redundancy in the Protein Data Bank of 3D protein structures, which is caused by many homologous proteins in the data bank, a representative set of structures is selected to reduce time and effort in statistical analyses.
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The Immunoglobulin Fold: Structural Classification, Sequence Patterns and Common Core

TL;DR: A systematic comparison of 23 Ig domain structures with less than 25% pairwise residue identity was performed using automatic structural alignment and analysis of beta-sheet and loop topology, revealing a common structural core of only four beta-strands and four different topological subtypes that correlate with the length of the intervening sequence between strands c and e, the most variable region in sequence.
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Genomic and transcriptomic hallmarks of poorly differentiated and anaplastic thyroid cancers

TL;DR: These data support a model of tumorigenesis whereby PDTCs and ATCs arise from well-differentiated tumors through the accumulation of key additional genetic abnormalities, many of which have prognostic and possible therapeutic relevance.
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Protein normal-mode dynamics: trypsin inhibitor, crambin, ribonuclease and lysozyme.

TL;DR: A new method for modelling protein dynamics using normal-mode analysis in internal co-ordinates, particularly well suited for modelling collective motion, makes possible direct visualization of biologically interesting modes, and is complementary to the more time-consuming simulation of molecular dynamics trajectories.