Journal article
Complement C1q is hydroxylated by collagen prolyl 4 hydroxylase, and is sensitive to off target inhibition by prolyl hydroxylase domain inhibitors that stabilise Hypoxia Inducible Factor
- Abstract:
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C1q is part of the C1 macromolecular complex that mediates the classical complement activation pathway, a major arm of innate immune defence. C1q is composed of A, B, and C chains that require post-translational prolyl-4-hydroxylation of their N-terminal collagen-like domain to enable formation of the functional triple helical multimers. The prolyl-4-hydroxylase(s) that hydroxylate C1q have not previously been identified. Recognised prolyl-4-hydroxylases include collagen prolyl- 4-hydroxylase...
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- Publication status:
- Published
- Peer review status:
- Peer reviewed
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(Preview, Version of record, pdf, 969.0KB, Terms of use)
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- Publisher copy:
- 10.1016/j.kint.2017.03.008
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Bibliographic Details
- Publisher:
- Elsevier
- Journal:
- Kidney International More from this journal
- Volume:
- 92
- Issue:
- 4
- Pages:
- 900–908
- Publication date:
- 2017-05-12
- Acceptance date:
- 2017-03-06
- DOI:
- EISSN:
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1523-1755
- ISSN:
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0085-2538
Item Description
- Keywords:
- Pubs id:
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pubs:684149
- UUID:
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uuid:04b6cb9c-ef1b-4569-b5b4-0aaba4762379
- Local pid:
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pubs:684149
- Source identifiers:
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684149
- Deposit date:
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2017-03-07
Terms of use
- Copyright holder:
- International Society of Nephrology
- Copyright date:
- 2017
- Notes:
- © 2017, International Society of Nephrology. Published by Elsevier Inc. Open access, funded by Wellcome Trust.
- Licence:
- CC Attribution (CC BY)
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