Journal
CURRENT PHARMACEUTICAL DESIGN
Volume 21, Issue 14, Pages 1862-1865Publisher
BENTHAM SCIENCE PUBL LTD
DOI: 10.2174/1381612821666150302115025
Keywords
Human serum albumin
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Funding
- NIGMS NIH HHS [T32 GM007183] Funding Source: Medline
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [T32GM007183] Funding Source: NIH RePORTER
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Human serum albumin (HSA) regulates the transport and availability of numerous chemical compounds and molecules in the blood vascular system. While previous HSA research has found that HSA interacts with specific varieties of ligands, new research efforts aim to expand HSA's ability to interact with more different drugs in order to improve the delivery of various pharmacological drugs. This review will cover fatty acid chain and post-translational modifications of HSA that potentially modulate how HSA interacts with various pharmacological drugs, including glycation, cysteinylation, S-nitrosylation, S-transnitrosation and S-guanylation.
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