Photo of Haining Zhong, Ph.D.

Haining Zhong Ph.D.

Haining Zhong earned a B.A. in Biological Science and Biotechnology and B.Eng. in Electronics and Computer Science from Tsinghua University in Beijing, China in 1996. He received his Ph.D. in Neuroscience from the Johns Hopkins University School of Medicine in 2002. Zhong did postdoctoral training at the Cold Spring Harbor Laboratory and then at the Janelia Farm Research Campus of the Howard Hughes Medical Institute. In 2009, he was appointed as an assistant scientist at the Vollum Institute and was promoted to scientist in 2015.

The brain is a complex network of billions of neurons which communicate with one another through trillions of very specialized connections called chemical synapses. These synapses and their experience-dependent plasticity are thought to be the fundamental mechanisms underlying an animal’s behavior, adaptation, learning, and memory. The Zhong lab is interested in the mechanisms by which the strength of a synapse is set and regulated at the cellular and molecular level. A current focus of the lab is to systematically characterize the abundance, stoichiometry, localization, and activity of critical synaptic proteins and how they are modulated by neuronal activity.

Areas of interest

  • photoactivated localization microscopy (PALM)
  • two-photon fluorescence lifetime imaging microscopy (2PFLIM)
  • fluorescence resonance energy transfer (FRET) microscopy
  • protein dynamics
  • synaptic signaling

Education

  • B.S., Tsinghua University, Beijing China 1996
  • Ph.D., Johns Hopkins University School of Medicine, Baltimore Maryland 2002

Honors and awards

  • NIH Director’s New Innovator Award (2011-2016)
  • NARSAD Young Investigator Award, The Brain & Behavior Research Foundation (2013-2015)

Publications

  • "A Highly Sensitive A-Kinase Activity Reporter for Imaging Neuromodulatory Events in Awake Mice." Neuron  In: , Vol. 99, No. 4, 22.08.2018, p. 665-679.e5.
  • "Ultrafast neuronal imaging of dopamine dynamics with designed genetically encoded sensors." Science  In: , 31.05.2018, p. 1-14.
  • "Liberated PKA Catalytic Subunits Associate with the Membrane via Myristoylation to Preferentially Phosphorylate Membrane Substrates." Cell Reports  In: , Vol. 19, No. 3, 18.04.2017, p. 617-629.
  • "Ontogenetic establishment of order-specific nuclear organization in the mammalian thalamus." Nature Neuroscience  In: , Vol. 20, No. 4, 29.03.2017, p. 516-528.
  • "A comprehensive excitatory input map of the striatum reveals novel functional organization." eLife  In: , Vol. 5, No. November2016, e19103, 28.11.2016.
  • "Applying superresolution localization-based microscopy to neurons." Synapse  In: , Vol. 69, No. 5, 01.05.2015, p. 283-294.
  • "Live imaging of endogenous PSD-95 using ENABLED : A conditional strategy to fluorescently label endogenous proteins." Journal of Neuroscience  In: , Vol. 34, No. 50, 10.12.2014, p. 16698-16712.
  • "A comprehensive thalamocortical projection map at the mesoscopic level." Nature Neuroscience  In: , Vol. 17, No. 9, 01.09.2014, p. 1276-1285.
  • "Subdiffractive microscopy : Techniques, applications, and challenges." Wiley Interdisciplinary Reviews: Systems Biology and Medicine  In: , Vol. 6, No. 2, 03.2014, p. 151-168.
  • "Photoactivated localization microscopy (PALM) : An optical technique for achieving ~10-nm resolution." Cold Spring Harbor Protocols  In: , Vol. 5, No. 12, 12.2010.
  • "Subcellular Dynamics of Type II PKA in Neurons." Neuron  In: , Vol. 62, No. 3, 14.05.2009, p. 363-374.
  • "Photon capture and signalling by melanopsin retinal ganglion cells." Nature  In: , Vol. 457, No. 7227, 15.01.2009, p. 281-287.
  • "A genetically encoded fluorescent sensor of ERK activity." Proceedings of the National Academy of Sciences of the United States of America  In: , Vol. 105, No. 49, 09.12.2008, p. 19264-19269.
  • "Advances in the speed and resolution of light microscopy." Current Opinion in Neurobiology  In: , Vol. 18, No. 6, 12.2008, p. 605-616.
  • "The spread of Ras activity triggered by activation of a single dendritic spine." Science  In: , Vol. 321, No. 5885, 04.07.2008, p. 136-140.
  • "Erratum : Supersensitive Ras activation in dendrites and spines revealed by two-photon fluorescence lifetime imaging (Nature Neuroscience (2006) 9 (283-291))." Nature Neuroscience  In: , Vol. 9, No. 3, 03.2006, p. 453.
  • "Supersensitive Ras activation in dendrites and spines revealed by two-photon fluorescence lifetime imaging." Nature Neuroscience  In: , Vol. 9, No. 2, 02.2006, p. 283-291.
  • "Intrinsically photosensitive retinal ganglion cells detect light with a vitamin A-based photopigment, melanopsin." Proceedings of the National Academy of Sciences of the United States of America  In: , Vol. 102, No. 29, 19.07.2005, p. 10339-10344.
  • "Selective heteromeric assembly of cyclic nucleotide-gated channels." Proceedings of the National Academy of Sciences of the United States of America  In: , Vol. 100, No. 9, 29.04.2003, p. 5509-5513.
  • "The heteromeric cyclic nucleotide-gated channel adopts a 3A : 1B stoichlometry." Nature  In: , Vol. 420, No. 6912, 14.11.2002, p. 193-198.
  • "Central role of the CNGA4 channel subunit in Ca2+-calmodulin-dependent odor adaptation." Science  In: , Vol. 294, No. 5549, 07.12.2001, p. 2172-2175.
  • "Molecular determinants of the modulation of cyclic nucleotide-activated channels by calmodulin." Proceedings of the National Academy of Sciences of the United States of America  In: , Vol. 96, No. 23, 09.11.1999, p. 13444-13449.
  • "Catalysis of the refolding of urea denatured creatine kinase by peptidyl-prolyl cis-trans isomerase." Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology  In: , Vol. 1338, No. 2, 04.04.1997, p. 147-150.
  • "Salt-induced folding of alkaline denatured creatine kinase under high pH conditions." Biochemistry and Molecular Biology International  In: , Vol. 41, No. 2, 02.1997, p. 257-267.
  • "Alkaline unfolding and salt-induced folding of yeast alcohol dehydrogenase under high pH conditions." International Journal of Peptide and Protein Research  In: , Vol. 47, No. 6, 1996, p. 484-490.

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