Ionic factors affecting the association of tyrosine hydroxylase with chromaffin granules in the adrenal medullary cell
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Cellular and Molecular Neuroscience
Cited by 7 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. Subcellular distribution of human tyrosine hydroxylase isoforms 1 and 4 in SH‐SY5Y cells;Journal of Cellular Biochemistry;2019-07-11
2. The N-Terminal Sequence of Tyrosine Hydroxylase Is a Conformationally Versatile Motif That Binds 14-3-3 Proteins and Membranes;Journal of Molecular Biology;2014-01
3. Three-way Interaction between 14-3-3 Proteins, the N-terminal Region of Tyrosine Hydroxylase, and Negatively Charged Membranes;Journal of Biological Chemistry;2009-11
4. The binding of tyrosine hydroxylase to negatively charged lipid bilayers involves the N-terminal region of the enzyme;FEBS Letters;2002-04-30
5. The N-Terminus of Human Tyrosine Hydroxylase is Responsible for its Association with Phospholipid Bilayers;Chemistry and Biology of Pteridines and Folates;2002
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