La is involved in diverse aspects of RNA metabolism, including binding and protecting 3-prime UUU (OH) elements of newly RNA polymerase III-transcribed RNA, processing 5-prime and 3-prime ends of pre-tRNA precursors, acting as an RNA chaperone, and binding viral RNAs associated with hepatitis C virus. La protein was originally defined by its reactivity with autoantibodies from patients with Sjögren's syndrome and systemic lupus erythematosus.[5][6]
^Fouraux MA, Bouvet P, Verkaart S, van Venrooij WJ, Pruijn GJ (July 2002). "Nucleolin associates with a subset of the human Ro ribonucleoprotein complexes". Journal of Molecular Biology. 320 (3): 475–88. doi:10.1016/S0022-2836(02)00518-1. hdl:2066/121576. PMID12096904.
Rauh AJ, Hornig H, Lührmann R (December 1988). "At least three distinct B cell epitopes reside in the C-terminal half of La protein, as determined by a recombinant DNA approach". European Journal of Immunology. 18 (12): 2049–57. doi:10.1002/eji.1830181227. PMID2464497. S2CID7014818.
Helsloot J, Sturgess A (December 1997). "T cell reactivity to Sjögren's syndrome related antigen La(SSB)". The Journal of Rheumatology. 24 (12): 2340–7. PMID9415639.
Broekhuis CH, Neubauer G, van der Heijden A, Mann M, Proud CG, van Venrooij WJ, Pruijn GJ (March 2000). "Detailed analysis of the phosphorylation of the human La (SS-B) autoantigen. (De)phosphorylation does not affect its subcellular distribution". Biochemistry. 39 (11): 3023–33. doi:10.1021/bi992308c. hdl:2066/187036. PMID10715123.
Nashimoto M, Nashimoto C, Tamura M, Kaspar RL, Ochi K (October 2001). "The inhibitory effect of the autoantigen La on in vitro 3' processing of mammalian precursor tRNAs". Journal of Molecular Biology. 312 (5): 975–84. doi:10.1006/jmbi.2001.5026. PMID11580243.
Fouraux MA, Bouvet P, Verkaart S, van Venrooij WJ, Pruijn GJ (July 2002). "Nucleolin associates with a subset of the human Ro ribonucleoprotein complexes". Journal of Molecular Biology. 320 (3): 475–88. doi:10.1016/S0022-2836(02)00518-1. hdl:2066/121576. PMID12096904.