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Mark Gerstein

Researcher at Yale University

Publications -  802
Citations -  172183

Mark Gerstein is an academic researcher from Yale University. The author has contributed to research in topics: Genome & Gene. The author has an hindex of 168, co-authored 751 publications receiving 149578 citations. Previous affiliations of Mark Gerstein include Rutgers University & Structural Genomics Consortium.

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Analyzing Cellular Biochemistry in Terms of Molecular Networks

TL;DR: From perspectives on how network analysis represents a preliminary step toward a systems approach for modeling cells, approaches for characterizing the topology of networks, such as finding hubs and analyzing subnets in terms of common motifs are discussed.
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A Bayesian system integrating expression data with sequence patterns for localizing proteins: comprehensive application to the yeast genome

TL;DR: A probabilistic system for predicting the subcellular localization of proteins and estimating the relative population of the various compartments in yeast, based on a Bayesian approach, which gives better accuracy in determining relative compartment populations than that obtained by simply tallying the localization predictions for individual proteins.
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Analysis of copy number variants and segmental duplications in the human genome: Evidence for a change in the process of formation in recent evolutionary history

TL;DR: The results imply that a shift in predominant formation mechanism occurred in recent history: approximately 40 million years ago, during the "Alu burst" in retrotransposition activity, non-allelic homologous recombination was the main driver of genome rearrangements.
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The Database of Macromolecular Motions: new features added at the decade mark

TL;DR: The database of molecular motions, MolMovDB (), has been in existence for the past decade and provides tools to interpolate between two conformations (the Morph Server) and predict possible motions in a single structure and developed tools to relate points of flexibility in a structure to particular key residue positions.
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Domain Closure in Lactoferrin: Two Hinges Produce a See-saw Motion Between Alternative Close-packed Interfaces

TL;DR: The structural mechanism underlying Lactoferrin's domain closure is analyzed here in detail and is compared to other instances of hinged domain closure and contrasted with instances of shear domain closure, where the overall motion is a summation of many small sliding motions between close-packed segments of polypeptide.