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Cell Reports|October 13, 2021
RAG2 abolishes RAG1 aggregation to facilitate V(D)J recombinationTingting Gan, Yuhong Wang, Yang Liu, et al.
The EMBO Journal|October 1, 1990
Protein import into yeast mitochondria is accelerated by the outer membrane protein MAS70V Hines, A Brandt, G Griffiths, et al.
American Journal of Preventive Medicine|July 4, 1998
Immunogenicity of hepatitis B Vaccines. Implications for persons at occupational risk of hepatitis B virus infectionF Averhoff, F Mahoney, P Coleman, et al.
The EMBO Journal|August 1, 1985
The first twelve amino acids (less than half of the pre-sequence) of an imported mitochondrial protein can direct mouse cytosolic dihydrofolate reductase into the yeast mitochondrial matrixE C Hurt, B Pesold-Hurt, K Suda, et al.
The EMBO Journal|February 1, 1991
Inner membrane protease I, an enzyme mediating intramitochondrial protein sorting in yeastA Schneider, M Behrens, P Scherer, et al.
Nucleic Acids Research|July 21, 2016
RAG1 targeting in the genome is dominated by chromatin interactions mediated by the non-core regions of RAG1 and RAG2Yaakov Maman, Grace Teng, Rashu Seth, et al.
Molecular Cell|March 11, 2000
Identification of two catalytic residues in RAG1 that define a single active site within the RAG1/RAG2 protein complexS D Fugmann, I J Villey, L M Ptaszek, et al.
Proceedings of the National Academy of Sciences of the United States of America|July 1, 1980
Cytoplasmically made subunits of yeast mitochondrial F1-ATPase and cytochrome c oxidase are synthesized as individual precursors, not as polyproteinsA S Lewin, I Gregor, T L Mason, et al.
The Journal of Biological Chemistry|July 7, 2007
Activation-induced cytidine deaminase-mediated sequence diversification is transiently targeted to newly integrated DNA substratesShu Yuan Yang, Sebastian D Fugmann, Hillary S Gramlich, et al.
The EMBO Journal|July 22, 1998
Interaction of mitochondrial targeting signals with acidic receptor domains along the protein import pathway: evidence for the 'acid chain' hypothesisT Komiya, S Rospert, C Koehler, et al.
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