Multiple nuclear factors interact with the immunoglobulin enhancer sequences

@article{Sen1986MultipleNF,
  title={Multiple nuclear factors interact with the immunoglobulin enhancer sequences},
  author={Ranjan Sen and David Baltimore},
  journal={Cell},
  year={1986},
  volume={46},
  pages={705-716}
}

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References

SHOWING 1-10 OF 56 REFERENCES
A nuclear factor that binds to a conserved sequence motif in transcriptional control elements of immunoglobulin genes
TLDR
It is reported here the identification of a human B-cell nuclear factor (IgNF-A) that binds to DNA sequences in the upstream regions of both the mouse heavy and κ light-chain gene promoters and also to the mouseHeavychain gene enhancer.
Distinct factors bind to apparently homolgous sequences in the immunoglobulin heavy-chain enhancer
TLDR
A mouse B-cell nuclear factor (NF-μE1) which binds specifically to one such motif within the mouse heavy-chain gene enhancer is identified, which seems to be present in both lym-phoid and non-lymphoid cell lines.
Cell-type-specific contacts to immunoglobulin enhancers in nuclei
TLDR
DMS strategy is applied in experiments involving single-copy genes within intact mammalian nuclei using genomic sequencing27, and it is found that a region of as few as 140 base pairs is sufficient for the enhancement effect of the enhancer.
Immunoglobulin heavy-chain enhancer requires one or more tissue-specific factors.
TLDR
In lymphoid cells, the heavy-chain and SV40 enhancers bind a common factor essential for enhancer function, in contrast, fibroblast cells contain a functionally distinct factor that is used by the SV40 but not by theheavy-chain enhancer.
A lymphocyte-specific enhancer in the mouse immunoglobulin kappa gene.
TLDR
Direct evidence is shown for a functionally similar enhancer within the large kappa gene intron of the mouse which is, however, less active than the heavy-chain gene enhancer.
B lineage--specific interactions of an immunoglobulin enhancer with cellular factors in vivo.
TLDR
There are changes in the reactivity of guanine residues to dimethyl sulfate within the enhancer sequence in myeloma, B, and early B cells, whereas virtually no alterations appear in cells of non-B lineage.
Specific interaction of cellular factors with the B enhancer of polyoma virus.
TLDR
Specific interactions between proteins from mouse 3T6 cells and the enhancer sequence of polyoma virus were detected using the method of band shifting on polyacrylamide gels, and it was confirmed that similar sequences are required for the formation of the complex.
Structure of the 5' ends of immunoglobulin genes: a novel conserved sequence.
TLDR
Comparison of the sequence of the 70Z/3 kappa light chain gene with those encoding other immunoglobulin heavy and light chains has revealed that a distinctive promoter region structure is characteristic of this multigene family.
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