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Correction: The viral restriction factor Tetherin prevents leucine-rich pentatricopeptide repeat-containing protein (LRPPRC) from association with Beclin 1 and B-cell CLL/lymphoma 2 (Bcl-2) and enhances autophagy and mitophagy.

08:00 EDT 29th March 2019 | BioPortfolio

Summary of "Correction: The viral restriction factor Tetherin prevents leucine-rich pentatricopeptide repeat-containing protein (LRPPRC) from association with Beclin 1 and B-cell CLL/lymphoma 2 (Bcl-2) and enhances autophagy and mitophagy."

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This article was published in the following journal.

Name: The Journal of biological chemistry
ISSN: 1083-351X
Pages: 5211

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Medical and Biotech [MESH] Definitions

A small leucine-rich proteoglycan that contains 4 KERATAN SULFATE chains within the leucine repeat region. It interacts with COLLAGEN TYPE I and COLLAGEN TYPE II fibrils and may function to control the rate of EXTRACELLULAR MATRIX assembly. It also sequesters TRANSFORMING GROWTH FACTOR BETA in the extracellular matrix.

A small leucine-rich proteoglycan that contains 10 tandem leucine repeats and four N-linked sites within the leucine repeat region that may be substituted with KERATAN SULFATE. These properties and its horseshoe shape allow it to mediate interactions among COLLAGEN molecules within fibrils. It is expressed in most mesenchymal tissues as well as the CORNEA, where it functions to maintain transparency.

A class of proteins that were originally identified by their ability to bind the DNA sequence CCAAT. The typical CCAAT-enhancer binding protein forms dimers and consists of an activation domain, a DNA-binding basic region, and a leucine-rich dimerization domain (LEUCINE ZIPPERS). CCAAT-BINDING FACTOR is structurally distinct type of CCAAT-enhancer binding protein consisting of a trimer of three different subunits.

Activated form of factor IX. This activation can take place via the intrinsic pathway by the action of factor XIa and calcium, or via the extrinsic pathway by the action of factor VIIa, thromboplastin, and calcium. Factor IXa serves to activate factor X to Xa by cleaving the arginyl-leucine peptide bond in factor X.

Intracellular signaling proteins that are defined by the presence of a NUCLEOTIDE-binding region and LEUCINE-rich repeats. Their general structure consists of any of a variety of effector domains at their N-termini such as a caspase recruitment domain (CARD), a central nucleotide-binding domain, and a variable number of C-terminal leucine-rich repeats. They are important for pathogen recognition in the INNATE IMMUNE RESPONSE of animals and plants. Members of the NLR protein family include the NOD SIGNALING ADAPTOR PROTEINS.

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