CoChat
Sign Up
Cited by 31

The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.

Activating Transcription Factor 1 and Cyclic AMP Response Element Modulator Can Modulate the Activity of the Immunoglobulin κ 3′ Enhancer

Pongubala, Jagan M.R., Atchison, Michael L.·1995·Journal of Biological Chemistry
DOI 10.1074/jbc.270.17.10304
Open this paper in CoChat — free account

Overview

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1074/jbc.270.17.10304

Cites

2 of 2 references verified0 citation errors · 0 not checkable

Statistics

Figures

Image 1
CC-BY · From the PDF
Image 2
CC-BY · From the PDF
Image 3
CC-BY · From the PDF
Image 4
CC-BY · From the PDF
Image 5
CC-BY · From the PDF
Image 6
CC-BY · From the PDF
FiG. 5 Identification of protein-DNA contact sites. Panel A, the 25-bp oligonucleotide 2 sequence (see panelB) was used in dimethylsulfate methylation interference assays. Lanes containing free (F), complex1(1), or complex 2 (2) are indicated. The positions of the G residues that inhibited protein binding when methylated are indicated by arrows. Panel B, summary of the footprint and EMSAs. The oligonucleotide 2 sequence (nucleotides 400-424) is shown at the top, and the positions of linker scan mutants B, C, and D are indicated. Asterisks show protein contact sites identified by dimethyl sulfate methylation interference assays. Below are shown the CRE-like motifs in the sequence and the sequences of mutants M.1-M.6. The binding activity of each mutant as measured by EMSA is summarized in the lower right. Panel C, the protein contact sites of the mouse enhancer are compared with the contact sites of the human 3' enhancer determined by in vivo footprinting (27).
FiG. 5 Identification of protein-DNA contact sites. Panel A, the 25-bp oligonucleotide 2 sequence (see panelB) was used in dimethylsulfate methylation interference assays. Lanes containing free (F), complex1(1), or complex 2 (2) are indicated. The positions of the G residues that inhibited protein binding when methylated are indicated by arrows. Panel B, summary of the footprint and EMSAs. The oligonucleotide 2 sequence (nucleotides 400-424) is shown at the top, and the positions of linker scan mutants B, C, and D are indicated. Asterisks show protein contact sites identified by dimethyl sulfate methylation interference assays. Below are shown the CRE-like motifs in the sequence and the sequences of mutants M.1-M.6. The binding activity of each mutant as measured by EMSA is summarized in the lower right. Panel C, the protein contact sites of the mouse enhancer are compared with the contact sites of the human 3' enhancer determined by in vivo footprinting (27).CC-BY · From the PDF
FiG. 6 ATF-1 and CREM bind to the κE3'-CRE. Radiolabeled κE3'-CRE oligonucleotide (oligonucleotide 2) was incubated with S194 nuclear extract proteins. Samples were either untreated (lane 1), treated with preimmune sera (lane 2), or treated with antibodies against CREM (lane 3), ATF-1 (lane 4), c-fos (lane 5), or CREB (lane 6).
FiG. 6 ATF-1 and CREM bind to the κE3'-CRE. Radiolabeled κE3'-CRE oligonucleotide (oligonucleotide 2) was incubated with S194 nuclear extract proteins. Samples were either untreated (lane 1), treated with preimmune sera (lane 2), or treated with antibodies against CREM (lane 3), ATF-1 (lane 4), c-fos (lane 5), or CREB (lane 6).CC-BY · From the PDF
FIG. 7 ATF-1enhances the binding ability of nuclear factors tothe κE3'CRE. Various amounts of nuclear extract proteins (from 3-1 pre-B cells) were assayed alone, in the presence of 2 µl of ATF-1 prepared by in vitro translation, or in the presence of control translation lysate (RRL). The amount of nuclear extract protein and the presence of ATF-1 or control lysate (RRL) are indicated above each lane. Arrows indicate the positions of complexes1,2, and 3.
FIG. 7 ATF-1enhances the binding ability of nuclear factors tothe κE3'CRE. Various amounts of nuclear extract proteins (from 3-1 pre-B cells) were assayed alone, in the presence of 2 µl of ATF-1 prepared by in vitro translation, or in the presence of control translation lysate (RRL). The amount of nuclear extract protein and the presence of ATF-1 or control lysate (RRL) are indicated above each lane. Arrows indicate the positions of complexes1,2, and 3.CC-BY · From the PDF
Image 10
CC-BY · From the PDF
Image 11
CC-BY · From the PDF
Image 12
CC-BY · From the PDF
FIG. 10 ATF-1 and CREM expression inB cells. Poly(A)⁺ RNAsisolated from 3-1, 1-8, MPC11, orS194cells were subjected to Northern blot analyses and probed with ATF-1 sequences (panel A). The same blot was stripped and rehybridized with CREM sequences (panel B). Panel C, a diagram of the various CREM isoforms and reverse transcriptase PCR primers. In.1 and In.2 represent glutamine-rich domains, P-BOX represents a phosphorylation domain, and DNA binding domains are represented as DBDI and DBDII.
FIG. 10 ATF-1 and CREM expression inB cells. Poly(A)⁺ RNAsisolated from 3-1, 1-8, MPC11, orS194cells were subjected to Northern blot analyses and probed with ATF-1 sequences (panel A). The same blot was stripped and rehybridized with CREM sequences (panel B). Panel C, a diagram of the various CREM isoforms and reverse transcriptase PCR primers. In.1 and In.2 represent glutamine-rich domains, P-BOX represents a phosphorylation domain, and DNA binding domains are represented as DBDI and DBDII.CC-BY · From the PDF
Image 14
CC-BY · From the PDF
FIG. 11 The κE3'-CRE sequence functions synergistically with the PU.1/NF-EM5 binding sites in the 3' enhancer. S194 cells were transfected with 4 µg of the reporter plasmids indicated above each lane. Transfection efficiencies were normalized by the level of β-galactosidase produced by the cotransfected plasmid pCH110. The activity of the reporter construct containing the PU.1 binding site (PU.1TKCAT) was considered as 1, and the relative activity of the κE3'-CRE+PU.1TKCAT reporter construct was determined relative to this value.
FIG. 11 The κE3'-CRE sequence functions synergistically with the PU.1/NF-EM5 binding sites in the 3' enhancer. S194 cells were transfected with 4 µg of the reporter plasmids indicated above each lane. Transfection efficiencies were normalized by the level of β-galactosidase produced by the cotransfected plasmid pCH110. The activity of the reporter construct containing the PU.1 binding site (PU.1TKCAT) was considered as 1, and the relative activity of the κE3'-CRE+PU.1TKCAT reporter construct was determined relative to this value.CC-BY · From the PDF

Verification

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cites

Show all 2 references

Research works printed but not linked: 41

  1. Pongubala, 1991, Mol. Cell. Biol., 11, 1041
  2. Park, 1991, Proc. Natl. Acad. Sci. U. S. A., 88, 9804, 10.1073/pnas.88.21.9804 · DOI
  3. Pongubala, 1992, Mol. Cell. Biol., 12, 368
  4. Briskin, 1988, Science, 242, 1036, 10.1126/science.3143155 · DOI
  5. Giri, 1984, J. Immunol., 132, 223, 10.4049/jimmunol.132.1.223 · DOI
  6. McGillis, 1993, Cell. Immunol., 150, 405, 10.1006/cimm.1993.1208 · DOI
  7. Sen, 1986, Cell, 47, 921, 10.1016/0092-8674(86)90807-X · DOI
  8. Shirakawa, 1989, Mol. Cell. Biol., 9, 959
  9. Weeks, 1988, J. Immunol., 140, 1312, 10.4049/jimmunol.140.4.1312 · DOI
  10. Atchison, 1987, Cell, 48, 121, 10.1016/0092-8674(87)90362-X · DOI
  11. Atchison, 1988, EMBO J., 7, 4213, 10.1002/j.1460-2075.1988.tb03318.x · DOI
  12. Gosh, 1990, Nature, 344, 678, 10.1038/344678a0 · DOI
  13. Lenardo, 1987, Science, 236, 1573, 10.1126/science.3109035 · DOI
  14. Hagman, 1990, Genes & Dev., 4, 978, 10.1101/gad.4.6.978 · DOI · Paper page
  15. Bomsztky, 1990, J. Biol. Chem., 265, 9413, 10.1016/S0021-9258(19)38864-7 · DOI
  16. Zaret, 1990, Proc. Natl. Acad. Sci. U. S. A., 87, 5469, 10.1073/pnas.87.14.5469 · DOI
  17. Kunkel, 1985, Proc. Natl. Acad. Sci. U. S. A., 82, 488, 10.1073/pnas.82.2.488 · DOI
  18. Sanger, 1977, Proc. Natl. Acad. Sci. U. S. A., 74, 5463, 10.1073/pnas.74.12.5463 · DOI · Paper page
  19. Hall, 1983, J. Mol. Appl. Genet., 2, 101
  20. Gorman, 1982, Mol. Cell. Biol., 2, 1044
  21. Dignam, 1983, Nucleic Acids Res., 11, 1475, 10.1093/nar/11.5.1475 · DOI
  22. Atchison, 1990, EMBO J., 9, 3109, 10.1002/j.1460-2075.1990.tb07508.x · DOI
  23. Vinson, 1988, Genes & Dev., 2, 801, 10.1101/gad.2.7.801 · DOI
  24. Meyer, 1989, EMBO J., 8, 1959, 10.1002/j.1460-2075.1989.tb03601.x · DOI
  25. Judde, 1992, Mol. Cell. Biol., 12, 5206
  26. Hai, 1989, Genes & Dev., 3, 2083, 10.1101/gad.3.12b.2083 · DOI
  27. Yoshimura, 1990, EMBO J., 9, 2537, 10.1002/j.1460-2075.1990.tb07434.x · DOI
  28. Foulkes, 1991, Cell, 64, 739, 10.1016/0092-8674(91)90503-Q · DOI
  29. Fink, 1988, Proc. Natl. Acad. Sci. U. S. A., 85, 6662, 10.1073/pnas.85.18.6662 · DOI
  30. Rehfuss, 1991, J. Biol. Chem., 266, 18431, 10.1016/S0021-9258(18)55078-X · DOI
  31. Foulkes, 1992, Cell, 68, 411, 10.1016/0092-8674(92)90178-F · DOI
  32. Foulkes, 1991, Proc. Natl. Acad. Sci. U. S. A., 88, 5448, 10.1073/pnas.88.12.5448 · DOI
  33. Foulkes, 1992, Nature, 355, 80, 10.1038/355080a0 · DOI
  34. Delmas, 1992, Proc. Natl. Acad. Sci. U. S. A., 89, 4226, 10.1073/pnas.89.10.4226 · DOI
  35. Molina, 1993, Cell, 75, 875, 10.1016/0092-8674(93)90532-U · DOI
  36. Hurst, 1991, Nucleic Acids Res., 19, 4601, 10.1093/nar/19.17.4601 · DOI
  37. Wagner, 1993, Science, 262, 395, 10.1126/science.8211160 · DOI
  38. Hai, 1991, Proc. Natl. Acad. Sci. U. S. A., 88, 3720, 10.1073/pnas.88.9.3720 · DOI
  39. Ziff, 1990, Trends Genet., 6, 69, 10.1016/0168-9525(90)90081-G · DOI
  40. Nakajima, 1993, Mol. Cell. Biol., 13, 3027
  41. Klemsz, 1990, Cell, 61, 113, 10.1016/0092-8674(90)90219-5 · DOI · Paper page

Cited by

Sorted by citations

See all 31

Metadata

Authors
Pongubala, J. M. R., & Atchison, M. L.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1995-04
Volume
270
Issue
17
Pages
10304-10313
ISSN
0021-9258
DOI
10.1074/jbc.270.17.10304
Cited by
31
References
2
Language
en
Licence

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

How to cite

Cite CoChat for the checks on this page, and the paper for its own findings.

This page
CoChat. (2026). Citation check: Activating Transcription Factor 1 and Cyclic AMP Response Element Modulator Can Modulate the Activity of the Immunoglobulin κ 3′ Enhancer. https://app.cochat.ai/papers/10.1074/jbc.270.17.10304
The paper
Pongubala, J. M. R., & Atchison, M. L. (1995). Activating Transcription Factor 1 and Cyclic AMP Response Element Modulator Can Modulate the Activity of the Immunoglobulin κ 3′ Enhancer. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.270.17.10304