J
James M. Berger
Researcher at Johns Hopkins University
Publications - 215
Citations - 21480
James M. Berger is an academic researcher from Johns Hopkins University. The author has contributed to research in topics: DNA & Topoisomerase. The author has an hindex of 75, co-authored 204 publications receiving 19688 citations. Previous affiliations of James M. Berger include Massachusetts Institute of Technology & University of California, Berkeley.
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Core structure of GP41 from the HIV envelope glycoprotein
TL;DR: The crystal structure of this complex, composed of the peptides N36 and C34, is a six-helical bundle that shows striking similarity to the low-pH-induced conformation of influenza hemagglutinin and likely represents the core of fusion-active gp41.
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Structure and mechanism of DNA topoisomerase II
TL;DR: The crystal structure of a large fragment of yeast type II DNA topoisomerase reveals a heart-shaped dimeric protein with a large central hole that provides a molecular model of the enzyme as an ATP-modulated clamp with two sets of jaws at opposite ends, connected by multiple joints.
Journal ArticleDOI
Evolutionary relationships and structural mechanisms of AAA+ proteins.
Jan P. Erzberger,James M. Berger +1 more
TL;DR: The critical features of theAAA+ domain are described, current knowledge of how this versatile element is incorporated into larger assemblies is summarized, and specific adaptations of the AAA+ fold are discussed that allow complex molecular manipulations to be carried out for a highly diverse set of macromolecular targets.
Journal ArticleDOI
Neurexin mediates the assembly of presynaptic terminals.
Camin Dean,Francisco G. Scholl,Jenny Choih,Shannon DeMaria,James M. Berger,Ehud Y. Isacoff,Peter Scheiffele +6 more
TL;DR: It is reported that neurexins are concentrated at synapses and that purified neuroligin is sufficient to cluster neURExin and to induce presynaptic differentiation and it is found that beta-neurexin clustering is necessary to trigger the recruitment of synaptic vesicles through interactions that require the cytoplasmic domain of neureXin.
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A robust and scalable microfluidic metering method that allows protein crystal growth by free interface diffusion.
TL;DR: This work developed a scheme for metering fluids on the picoliter scale that is scalable to highly integrated parallel architectures and is independent of the properties of the working fluid, and demonstrates that diffraction-quality crystals may be grown and harvested from such nanoliter-volume reactions.