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The structural basis of ZMPSTE24-dependent laminopathies

Abstract:: Mutations in the nuclear membrane zinc metalloprotease ZMPSTE24 lead to diseases of lamin processing (laminopathies), such as the premature aging disease progeria and metabolic disorders. ZMPSTE24 processes prelamin A, a component of the nuclear lamina intermediate filaments, by cleaving it at two sites. Failure of this processing results in accumulation of farnesylated, membrane-associated prelamin A. The 3.4 angstrom crystal structure of human ZMPSTE24 has a seven transmembrane α-helical ba...
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APA Style

Quigley, A., Dong, Y., Pike, A., Dong, L., Shrestha, L., Berridge, G., Stansfeld, P., Sansom, M., Edwards, A., Bountra, C., Von Delft, F., Bullock, A., Burgess-Brown, N., & Carpenter, E. (2013). The structural basis of ZMPSTE24-dependent laminopathies. Science, 340(6127), 1604–1607.

MLA Style

Quigley, A., et al. “The Structural Basis of ZMPSTE24-Dependent Laminopathies.” Science, vol. 340, no. 6127, 2013, pp. 1604–07.

Chicago Style

Quigley, A, Y Dong, A Pike, L Dong, L Shrestha, G Berridge, P Stansfeld, et al. 2013. “The Structural Basis of ZMPSTE24-Dependent Laminopathies.” Science 340 (6127): 1604–7.
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Publisher copy:: 10.1126/science.1231513

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+ Dong, Y More by this author

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+ Pike, A More by this author

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+ Dong, L More by this author

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+ Shrestha, L More by this author

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Bibliographic Details

Journal:: Science
Volume:: 340
Issue:: 6127
Pages:: 1604-1607
Publication date:: 2013-03-29
DOI:: 10.1126/science.1231513
EISSN:: 1095-9203
ISSN:: 0036-8075

Item Description

Language:: English
Pubs id:: pubs:395221
UUID:: uuid:064f9553-0aec-4ab9-a5ea-979ec4f82394
Local pid:: pubs:395221
Source identifiers:: 395221
Deposit date:: 2013-11-17

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Copyright date:: 2013

Licence:: Terms and Conditions of Use for Oxford University Research Archive

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