Novel Aspects of Tetramer Assembly and N-terminal Domain Structure and Function Are Revealed by Recombinant Expression of Human AMP Deaminase Isoforms-Reference-Cited by-同舟云学术

Novel Aspects of Tetramer Assembly and N-terminal Domain Structure and Function Are Revealed by Recombinant Expression of Human AMP Deaminase Isoforms

Published:1998-12 Issue:52 Volume:273 Page:35118-35125
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Mahnke-Zizelman Donna K.,Tullson Peter C.,Sabina Richard L.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference41 articles.

1. Isozymes of rat AMP deaminase

2. AMP deaminase isozymes in human tissues

3. Characterization of the human and rat myoadenylate deaminase genes.

4. Adenylate deaminase. A multigene family in humans and rats.

5. Characterization of the human AMPD3 gene reveals that 5′ exon useage is subject to transcriptional control by three tandem promoters and alternative splicing

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