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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
2004
2004
Prior to folding to a native functional structure, many large RNAs form conformationally collapsed states. Formation of the near… Expand
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
Background. Acutevascular xenograft rejection (AVXR), also termed delayed xenograft rejection (DXR), occurs when hyperacute… Expand
1996
1996
A full‐length genomic DNA fragment that codes for a novel EF‐hand protein from Dictyostelium discoideum was cloned and sequenced… Expand
Highly Cited
1995
Highly Cited
1995
The splicing factor CBP2 is required to excise the yeast mitochondrial group I intron bI5 in vivo and at low magnesium ion… Expand
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