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Facilitation of NMDA-mediated calcium flux by the HIV-1 protein Tat involves tyrosine kinase-dependent modulation of the zinc site an NMDA receptors.
被引:0
|
作者
:
Haughey, NJ
论文数:
0
引用数:
0
h-index:
0
机构:
NIA, Neurosci Lab, Baltimore, MD 21224 USA
Haughey, NJ
Mattson, MP
论文数:
0
引用数:
0
h-index:
0
机构:
NIA, Neurosci Lab, Baltimore, MD 21224 USA
Mattson, MP
Nath, A
论文数:
0
引用数:
0
h-index:
0
机构:
NIA, Neurosci Lab, Baltimore, MD 21224 USA
Nath, A
Hochman, S
论文数:
0
引用数:
0
h-index:
0
机构:
NIA, Neurosci Lab, Baltimore, MD 21224 USA
Hochman, S
Geiger, JD
论文数:
0
引用数:
0
h-index:
0
机构:
NIA, Neurosci Lab, Baltimore, MD 21224 USA
Geiger, JD
机构
:
[1]
NIA, Neurosci Lab, Baltimore, MD 21224 USA
[2]
Univ Kentucky, Dept Neurol, Lexington, KY 40536 USA
[3]
Emory Univ, Dept Physiol, Atlanta, GA 30322 USA
[4]
Univ Manitoba, Dept Pharmacol, Winnipeg, MB, Canada
来源
:
JOURNAL OF NEUROCHEMISTRY
|
2000年
/ 74卷
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:
D O I
:
暂无
中图分类号
:
Q5 [生物化学];
Q7 [分子生物学];
学科分类号
:
071010 ;
081704 ;
摘要
:
引用
收藏
页码:S19 / S19
页数:1
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Modulation of microtubule assembly by the HIV-1 Tat protein is strongly dependent on zinc binding to Tat
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