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colligin-2

Known as: CBP2 
 
National Institutes of Health

Papers overview

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2006
2006
Like most cellular RNA enzymes, the bI5 group I intron requires binding by a protein cofactor to fold correctly. Here, we use… Expand
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2005
2005
Human squamous cell carcinoma of the head and neck (SCCHN) is characterized by over expression of a tumor cell surface-specific… Expand
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2004
2004
Prior to folding to a native functional structure, many large RNAs form conformationally collapsed states. Formation of the near… Expand
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2001
2001
Native folding and splicing by the Saccharomyces cerevisiae mitochondrial bI5 group I intron RNA is facilitated by both the S… Expand
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2001
2001
Most large RNAs achieve their active, native structures only as complexes with one or more cofactor proteins. By varying the Mg2… Expand
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2000
2000
To study the signal transduction of cytokinins, we characterized cytokinin-binding proteins (CBPs) isolated from tobacco callus… Expand
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2000
2000
Abstract We previously isolated RA-A47, which is recognized as an antigen of rheumatoid arthritis (RA), from a human… Expand
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1996
1996
A full-length genomic DNA fragment that codes for a novel EF-hand protein Dictyostelium discoideum was cloned and sequenced. The… Expand
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1995
1995
The splicing factor CBP2 is required to excise the yeast mitochondrial group I intron bI5 in vivo and at low magnesium ion… Expand
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1991
1991
The yeast CBP2 gene product is required for the splicing of the terminal intron (bI5) of the mitochondrial cytochrome b pre-mRNA… Expand
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