Taking LSD 1 to a new high.
Histone modifications mediate changes in gene expression by altering the underlying chromatin structure or by serving as a binding platform to recruit other proteins. One such modification, histone methylation, was thought to be irreversible until last year when Shi and co-workers broke new ground w...
| Main Authors: | , , |
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| Format: | Journal article |
| Language: | English |
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2005
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| _version_ | 1797081350408241152 |
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| author | Wysocka, J Milne, T Allis, C |
| author_facet | Wysocka, J Milne, T Allis, C |
| author_sort | Wysocka, J |
| collection | OXFORD |
| description | Histone modifications mediate changes in gene expression by altering the underlying chromatin structure or by serving as a binding platform to recruit other proteins. One such modification, histone methylation, was thought to be irreversible until last year when Shi and co-workers broke new ground with their discovery of a lysine-specific histone demethylase (LSD 1). They showed that LSD 1, a nuclear amine oxidase homolog, is a bona fide histone H3 lysine 4 demethylase (Shi et al., 2004). Now, a new study from published in a recent issue of Molecular Cell, together with two studies recently published by and in Nature, reveal that LSD 1's specificity and activity is in fact regulated by associated protein cofactors. |
| first_indexed | 2024-03-07T01:13:16Z |
| format | Journal article |
| id | oxford-uuid:8dc572e9-657f-474e-8daf-a612ada3978e |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T01:13:16Z |
| publishDate | 2005 |
| record_format | dspace |
| spelling | oxford-uuid:8dc572e9-657f-474e-8daf-a612ada3978e2022-03-26T22:53:20ZTaking LSD 1 to a new high.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:8dc572e9-657f-474e-8daf-a612ada3978eEnglishSymplectic Elements at Oxford2005Wysocka, JMilne, TAllis, CHistone modifications mediate changes in gene expression by altering the underlying chromatin structure or by serving as a binding platform to recruit other proteins. One such modification, histone methylation, was thought to be irreversible until last year when Shi and co-workers broke new ground with their discovery of a lysine-specific histone demethylase (LSD 1). They showed that LSD 1, a nuclear amine oxidase homolog, is a bona fide histone H3 lysine 4 demethylase (Shi et al., 2004). Now, a new study from published in a recent issue of Molecular Cell, together with two studies recently published by and in Nature, reveal that LSD 1's specificity and activity is in fact regulated by associated protein cofactors. |
| spellingShingle | Wysocka, J Milne, T Allis, C Taking LSD 1 to a new high. |
| title | Taking LSD 1 to a new high. |
| title_full | Taking LSD 1 to a new high. |
| title_fullStr | Taking LSD 1 to a new high. |
| title_full_unstemmed | Taking LSD 1 to a new high. |
| title_short | Taking LSD 1 to a new high. |
| title_sort | taking lsd 1 to a new high |
| work_keys_str_mv | AT wysockaj takinglsd1toanewhigh AT milnet takinglsd1toanewhigh AT allisc takinglsd1toanewhigh |