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Anthony A. Hyman

Anthony Hyman
AnthonyHyman.jpg
Anthony Arie Hyman
Born Anthony Arie Hyman
(1962-05-27) 27 May 1962 (age 54)
Haifa, Israel
Residence Germany
Nationality British
Fields Molecular Cell Biology
Institutions
Alma mater
Thesis Establishment of division axes in the early embryonic divisions of Caenorhabditis Elegans (1987)
Notable awards
Website
hymanlab.mpi-cbg.de

Anthony Arie Hyman (born 27 May 1962) FRS is a British scientist and professor at the Max Planck Institute of Molecular Cell Biology and Genetics.

Hyman was educated at University College London and King's College, Cambridge where he was awarded a PhD in 1987.

Hyman has focused his career on examining microtubules and how these structures of the cytoskeleton control: cell division, mitotic spindle position, and cell polarity. Hyman's research has identified how microtubules are made into cellular structures and how they are broken down.

While at King's College, Cambridge, Hyman worked under the supervision of John White and was a key researcher in Sydney Brenner's C. elegans group. Using microscopy and microsurgery, he examined the placement of cell axes during early cell division of C.elegans embryos. Hyman presented new findings about mechanisms of rotation by cutting microtubules with a laser beam. Hyman demonstrated that pulling forces acting from the posterior cortex on microtubules drives spindle rotation.

At the University of California, San Francisco, Hyman investigated the interaction between chromosomes and microtubules that create the mitotic forces that separate chromosomes in the lab of Tim Mitchison. He also created a number of tools that are used today:

While at the European Molecular Biology Laboratory (EMBL) Hyman along with Rebecca Heald and Eric Karsenti combined their work to create an impact on the current understanding of how the meiotic spindle self assembles. Hyman created his first independent group at EMBL that discovered that the important factors in Xenopus egg extracts were the stabilizing protein, XMAP215 and the destabilizing protein, XKCM1.


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