2003
DOI: 10.1016/s0378-1119(02)01210-6
|View full text |Cite
|
Sign up to set email alerts
|

Molecular cloning and characterization of a novel gene family of four ancient conserved domain proteins (ACDP)

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1
1
1

Citation Types

2
122
1

Year Published

2003
2003
2024
2024

Publication Types

Select...
7
2

Relationship

1
8

Authors

Journals

citations
Cited by 99 publications
(125 citation statements)
references
References 17 publications
2
122
1
Order By: Relevance
“…7B). This interaction is specific, as evi- denced by the fact that CNNM2a and CNNM2b hardly dimerize with CNNM4, which shares the highest sequence homology with CNNM2 (96.7% similarity and 81.4% identity at the protein level) (5).…”
Section: Discussionmentioning
confidence: 99%
See 1 more Smart Citation
“…7B). This interaction is specific, as evi- denced by the fact that CNNM2a and CNNM2b hardly dimerize with CNNM4, which shares the highest sequence homology with CNNM2 (96.7% similarity and 81.4% identity at the protein level) (5).…”
Section: Discussionmentioning
confidence: 99%
“…Interestingly, no other electrolyte disturbance was detected (3). CNNM2, formerly known as ancient conserved domain protein 2 (ACDP2), belongs to the CNNM family consisting of four proteins (CNNM1-4) that share homology to cyclins, although no cyclin-related function has been described (5). Two predicted CNNM2 protein isoforms are conserved between humans and mouse.…”
mentioning
confidence: 99%
“…Members of the Cyclin M (CNNM) family have been proposed to function as Mg 2ϩ transporters (184,545).…”
Section: Cnnm3mentioning
confidence: 99%
“…Thus, correlating with the enhanced BAT thermogenesis observed, the overall increase in energy dissipation can explain the reason PRL2-KO mice are underweight, even though they exhibited increased food intake and O 2 consumption, especially in female mice. Mg 2+ transporter CNNMs contain tandem pairs of cystathionine-β-synthase (CBS) domains that are conserved in all living cells from prokaryotes to eukaryotes (48,49). CBS domains act as energy-sensing modules; for instance, the γ subunit of AMPK possesses 4 CBS domains with allosteric binding sites for AMP as well as ATP, allowing AMPK activity to vary according to the intracellular ATP:AMP ratio (50).…”
Section: +mentioning
confidence: 99%