Abstract
Cyclophilins (CyPs) are binding proteins for the immunosuppressive drug cyclosporin A (CsA). CyPs are evolutionarily highly conserved proteins present in both pro- and eukaryotes as well as in different subcellular locations. CyPs possess enzymatic activity, namely peptidyl-prolyl cis-trans isomerase (PPIase) activity; CyPs are involved in cellular protein folding and protein interactions. To date, only cyclosporins and proteins are known to interact with CyPs. Here we describe a novel nuclear cyclophilin (hCyP33) from human T cells with an additional RNA-binding domain. This combines for the first time RNA binding and protein folding in one protein.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Isomerases / chemistry*
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Amino Acid Isomerases / metabolism
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Amino Acid Sequence
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Carrier Proteins / chemistry*
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Carrier Proteins / metabolism
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Cloning, Molecular
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Cyclophilins*
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DNA, Complementary
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Humans
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Molecular Sequence Data
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Nuclear Proteins / chemistry*
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Nuclear Proteins / metabolism
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Peptidylprolyl Isomerase
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Protein Folding
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RNA / metabolism*
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RNA-Binding Proteins / chemistry*
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RNA-Binding Proteins / metabolism
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Recombinant Fusion Proteins / chemistry
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Recombinant Fusion Proteins / metabolism
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Sequence Alignment
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T-Lymphocytes / chemistry*
Substances
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Carrier Proteins
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DNA, Complementary
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Nuclear Proteins
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RNA-Binding Proteins
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Recombinant Fusion Proteins
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RNA
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Amino Acid Isomerases
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Cyclophilins
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PPIE protein, human
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Peptidylprolyl Isomerase