http://nobelprize.org/chemistry/laureates/2004/press.html
跟生化有關。
Press Release: The Nobel Prize in Chemistry 2004
6 October 2004
The Royal Swedish Academy of Sciences has decided to
award the Nobel Prize in Chemistry for 2004
"for the discovery of ubiquitin-mediated protein degradation" jointly to
Aaron Ciechanover
Technion – Israel Institute of Technology, Haifa, Israel,
Avram Hershko
Technion – Israel Institute of Technology, Haifa, Israel and
Irwin Rose
University of California, Irvine, USA
Proteins labelled for destruction
Proteins build up all living things: plants, animals and therefore
us humans. In the past few decades biochemistry has come a long way
towards explaining how the cell produces all its various proteins.
But as to the breaking down of proteins, not so many researchers
were interested. Aaron Ciechanover, Avram Hershko and Irwin Rose
went against the stream and at the beginning of the 1980s discovered
one of the cell's most important cyclical processes, regulated
protein degradation. For this, they are being rewarded with this
year's Nobel Prize in Chemistry.
Aaron Ciechanover, Avram Hershko and Irwin Rose have brought us to
realise that the cell functions as a highly-efficient checking
station where proteins are built up and broken down at a furious
rate. The degradation is not indiscriminate but takes place through
a process that is controlled in detail so that the proteins to be
broken down at any given moment are given a molecular label, a
‘kiss of death', to be dramatic. The labelled proteins are then
fed into the cells' "waste disposers", the so called proteasomes,
where they are chopped into small pieces and destroyed.
The label consists of a molecule called ubiquitin. This fastens to
the protein to be destroyed, accompanies it to the proteasome where
it is recognised as the key in a lock, and signals that a protein
is on the way for disassembly. Shortly before the protein is squeezed
into the proteasome, its ubiquitin label is disconnected for re-use.
Thanks to the work of the three Laureates it is now possible to
understand at molecular level how the cell controls a number of
central processes by breaking down certain proteins and not others.
Examples of processes governed by ubiquitin-mediated protein
degradation are cell division, DNA repair, quality control of
newly-produced proteins, and important parts of the immune defence.
When the degradation does not work correctly, we fall ill. Cervical
cancer and cystic fibrosis are two examples.
Knowledge of ubiquitin-mediated protein degradation offers an
opportunity to develop drugs against these diseases and others.
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