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Monomeric fluorescent proteins that change their emission characteristics as they mature have been successfully used to study the spatial and temporal dynamics of lysosome-associated membrane protein type 2A.
Lysosome-associated membrane protein type 2A.
Chaperone-mediated autophagy (CMA) involves direct translocation of unfolded substrate proteins across the lysosome membrane through the action of a cytosolic and lysosomal chaperone hsc70, and the integral membrane receptor lysosome-associated membrane protein type 2A (LAMP-2A).
This membrane protein type is evolutionarily conserved and includes proteins essential to intracellular trafficking and mitochondrial architecture/function.
Because such coding treatments have been successfully used to improve the quality in predicting many other protein attributes, such as membrane protein type [28], protein subcellular locations [29], and protein complexes [30].
AGM is known to bind the basement membrane protein type IV collagen with high affinity 15.
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The elucidation of membrane protein types provides clues for understanding the structure and function of proteins.
These results indicate that our method is effective and valuable for predicting membrane protein types.
Knowledge of membrane protein types often provides useful clues in deducing the functions of uncharacterized membrane proteins.
In addition, the performance of the proposed approach is complementary to the functional-domain-based method for different membrane protein types.
The results of jackknife cross-validation test show that our method achieves an overall accuracy of 93.0% in discriminating between mycobacterial membrane proteins and mycobacterial non-membrane proteins and an overall accuracy of 93.1% in classifying mycobacterial membrane protein types.
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