Drummond

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(Original Drummond Lab entry)
Current revision (12:02, 15 June 2012) (view source)
 
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[[Drummond|  '''Home''' ]]
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To carry out biological functions, a typical protein must fold into a complex structure encoded by its amino-acid sequence. Alterations of that sequence often cause misfolding, disrupting function and also creating toxic, aggregation-prone molecules.
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[[Drummond:Contact |  '''Contact''' ]]
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[[Drummond:Back Door | '''Internal''' ]]
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[[Drummond:Lab Members | '''Lab Members''' ]]
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[[Drummond:Reprints | '''Publications''' ]]  
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[[Drummond:Research |  '''Research''' ]]
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[[Drummond:Talks |  '''Talks''' ]]
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Protein misfolding causes major age-related human neurodegenerative diseases, shapes quality control mechanisms inside the cell, and influences how rapidly protein-coding genes accumulate sequence changes over evolutionary time. Yet strikingly little is known about the major causes, amounts, or consequences of protein misfolding. Key open questions include: What are the dominant causes of protein misfolding in normal, disease-afflicted and aging cells? What fraction of newly synthesized proteins misfold, and why? What is the error rate of protein synthesis? Why are misfolded proteins toxic, and how do cells detect and respond to them?
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== General ==
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[[Drummond Lab:Lab Supplies|Lab Supplies]]
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[[Drummond Lab:Lab Chores|Lab Chores]]
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We seek answers to these questions, taking an integrated biochemical, genetic, and evolutionary approach.
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[[Drummond Lab:Safety|Lab Safety]]
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<strong>We are [[Drummond:Employment|hiring]]!</strong>
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== Group Meetings ==
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<small>Congratulations to Dr. Kerry Samerotte, winner of the [http://www.smbe.org/awards/the-walter-m-fitch-award/ 2011 Walter M. Fitch Award].<br/>
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[[Drummond Lab:Group Meeting Snack Schedule|Snack Schedule]]
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Read our [http://www.pnas.org/content/early/2010/12/22/1017570108.full.pdf+html most recent paper in PNAS].<br/>
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[[Drummond Lab:Lab Meetings|Notes for Meetings]]
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== Other ==
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Current revision

the drummond lab

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To carry out biological functions, a typical protein must fold into a complex structure encoded by its amino-acid sequence. Alterations of that sequence often cause misfolding, disrupting function and also creating toxic, aggregation-prone molecules.

Protein misfolding causes major age-related human neurodegenerative diseases, shapes quality control mechanisms inside the cell, and influences how rapidly protein-coding genes accumulate sequence changes over evolutionary time. Yet strikingly little is known about the major causes, amounts, or consequences of protein misfolding. Key open questions include: What are the dominant causes of protein misfolding in normal, disease-afflicted and aging cells? What fraction of newly synthesized proteins misfold, and why? What is the error rate of protein synthesis? Why are misfolded proteins toxic, and how do cells detect and respond to them?

We seek answers to these questions, taking an integrated biochemical, genetic, and evolutionary approach.


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