Tomas Kirchhausen, Ph.D.

Tomas Kirchhausen, Ph.D.

Senior Investigator, Program in Cellular and Molecular Medicine (Boston Children's Hospital)
Springer Family Professor of Pediatrics (HMS)
Professor of Cell Biology (HMS)

The Kirchhausen Lab focuses on understanding processes that mediate and regulate cellular membrane remodeling, the biogenesis of organelles, and the ways by which viruses, biologicals and oligonucleotides are delivered to the cell interior. 

By direct observation of molecular events obtained using Lattice Light Sheet Microscopy and Lattice Light Sheet Microscopy optimized with Adaptive Optics (AO-LLSM), frontier optical-imaging modalities with high temporal resolution and spatial precision, we aim to bridge the gap between molecules and cells, either as independent entities in culture, as components of organoids, or as constituents of living tissues. The richness and magnitude of the big-data obtained over periods ranging from seconds to hours create new challenges for obtaining quantitative representations of the observed dynamics and for deriving accurate and comprehensive models for the underlying developmental mechanisms. With these type of dynamic studies we expect to integrate molecular snapshots obtained at molecular and atomic resolution using cryoEM with live-cell processes, in an effort to generate ‘molecular movies' allowing us to obtain frameworks for analyzing some of the molecular contacts and switches that participate in the regulation, availability, and intracellular traffic of the many molecules involved in signal transduction, immune responsiveness, lipid homeostasis, cell-cell recognition and organelle biogenesis. Such biological phenomena have importance for our understanding of many diseases including cancer, viral infection and pathogen invasion, Alzheimer's, as well as other neurological diseases.

Harvard Medical School

Dept. of Cell Biology, WAB-133

200 Longwood Avenue

Boston, MA 02115

Lab telephone: 617-713-8888

Lab fax: 617-713-8898

Identification of a putative yeast homolog of the mammalian beta chains of the clathrin-associated protein complexes.
Authors: Authors: Kirchhausen T.
Mol Cell Biol
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Sequence of the rat alpha c large chain of the clathrin associated protein complex AP-2.
Authors: Authors: Tucker KL, Nathanson K, Kirchhausen T.
Nucleic Acids Res
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Analysis of clathrin light chain-heavy chain interactions using truncated mutants of rat liver light chain LCB3.
Authors: Authors: Scarmato P, Kirchhausen T.
J Biol Chem
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Structural and functional division into two domains of the large (100- to 115-kDa) chains of the clathrin-associated protein complex AP-2.
Authors: Authors: Kirchhausen T, Nathanson KL, Matsui W, Vaisberg A, Chow EP, Burne C, Keen JH, Davis AE.
Proc Natl Acad Sci U S A
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Molecular cloning and complete amino acid sequence of AP50, an assembly protein associated with clathrin-coated vesicles.
Authors: Authors: Thurieau C, Brosius J, Burne C, Jolles P, Keen JH, Mattaliano RJ, Chow EP, Ramachandran KL, Kirchhausen T.
DNA
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Clathrin heavy chain: molecular cloning and complete primary structure.
Authors: Authors: Kirchhausen T, Harrison SC, Chow EP, Mattaliano RJ, Ramachandran KL, Smart J, Brosius J.
Proc Natl Acad Sci U S A
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Clathrin light chains LCA and LCB are similar, polymorphic, and share repeated heptad motifs.
Authors: Authors: Kirchhausen T, Scarmato P, Harrison SC, Monroe JJ, Chow EP, Mattaliano RJ, Ramachandran KL, Smart JE, Ahn AH, Brosius J.
Science
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Configuration of clathrin trimers: evidence from electron microscopy.
Authors: Authors: Kirchhausen T, Harrison SC, Heuser J.
J Ultrastruct Mol Struct Res
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DNA gyrase and its complexes with DNA: direct observation by electron microscopy.
Authors: Authors: Kirchhausen T, Wang JC, Harrison SC.
Cell
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Deep-etch views of clathrin assemblies.
Authors: Authors: Heuser J, Kirchhausen T.
J Ultrastruct Res
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