BAD (タンパク質) (Japanese Wikipedia)

Analysis of information sources in references of the Wikipedia article "BAD (タンパク質)" in Japanese language version.

refsWebsite

Global rank Japanese rank

24nih.gov

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18doi.org

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2ensembl.org

1,626^th place

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2wikipedia.org

low place

2worldcat.org

5^th place

19^th place

1endojournals.org

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1harvard.edu

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doi.org

“The proapoptotic BH3-only protein BAD transduces cell death signals independently of its interaction with Bcl-2”. Cell Death Differ. 9 (11): 1240–7. (2002). doi:10.1038/sj.cdd.4401097. PMID 12404123.
“Interference of BAD (Bcl-xL/Bcl-2-associated death promoter)-induced apoptosis in mammalian cells by 14-3-3 isoforms and P11”. Mol. Endocrinol. 11 (12): 1858–67. (1997). doi:10.1210/me.11.12.1858. PMID 9369453.
Foster, T. C.; Sharrow, K. M.; Masse, J. R.; Norris, C. M.; Kumar, A. (2001-06-01). “Calcineurin links Ca2+ dysregulation with brain aging”. The Journal of Neuroscience: The Official Journal of the Society for Neuroscience 21 (11): 4066–4073. doi:10.1523/JNEUROSCI.21-11-04066.2001. ISSN 1529-2401. PMC 1201477. PMID 11356894.
“Differential targeting of prosurvival Bcl-2 proteins by their BH3-only ligands allows complementary apoptotic function”. Mol. Cell 17 (3): 393–403. (February 2005). doi:10.1016/j.molcel.2004.12.030. PMID 15694340.
“Bad, a heterodimeric partner for Bcl-XL and Bcl-2, displaces Bax and promotes cell death”. Cell 80 (2): 285–91. (January 1995). doi:10.1016/0092-8674(95)90411-5. PMID 7834748.
“Underphosphorylated BAD interacts with diverse antiapoptotic Bcl-2 family proteins to regulate apoptosis”. Apoptosis 6 (5): 319–30. (October 2001). doi:10.1023/A:1011319901057. PMID 11483855.
“Survival function of protein kinase C{iota} as a novel nitrosamine 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone-activated bad kinase”. J. Biol. Chem. 280 (16): 16045–52. (April 2005). doi:10.1074/jbc.M413488200. PMID 15705582.
“BAD partly reverses paclitaxel resistance in human ovarian cancer cells”. Oncogene 17 (19): 2419–27. (November 1998). doi:10.1038/sj.onc.1202180. PMID 9824152.
“Development of a high-throughput fluorescence polarization assay for Bcl-x(L)”. Anal. Biochem. 307 (1): 70–5. (August 2002). doi:10.1016/S0003-2697(02)00028-3. PMID 12137781.
“The anti-apoptotic molecules Bcl-xL and Bcl-w target protein phosphatase 1alpha to Bad”. Eur. J. Immunol. 32 (7): 1847–55. (July 2002). doi:10.1002/1521-4141(200207)32:7<1847::AID-IMMU1847>3.0.CO;2-7. PMID 12115603.
“Human homologue of S. pombe Rad9 interacts with BCL-2/BCL-xL and promotes apoptosis”. Nat. Cell Biol. 2 (1): 1–6. (January 2000). doi:10.1038/71316. PMID 10620799.
“Rationale for Bcl-xL/Bad peptide complex formation from structure, mutagenesis, and biophysical studies”. Protein Sci. 9 (12): 2528–34. (Dec 2000). doi:10.1110/ps.9.12.2528. PMC 2144516. PMID 11206074.
“BAD/BCL-[X(L)] heterodimerization leads to bypass of G0/G1 arrest”. Oncogene 20 (33): 4507–18. (July 2001). doi:10.1038/sj.onc.1204584. PMID 11494146.
“Synergistic anti-apoptotic activity between Bcl-2 and SMN implicated in spinal muscular atrophy”. Nature 390 (6658): 413–7. (November 1997). Bibcode: 1997Natur.390..413I. doi:10.1038/37144. PMID 9389483.
“PCNA interacts with hHus1/hRad9 in response to DNA damage and replication inhibition”. Oncogene 19 (46): 5291–7. (November 2000). doi:10.1038/sj.onc.1203901. PMID 11077446.
“Survival activity of Bcl-2 homologs Bcl-w and A1 only partially correlates with their ability to bind pro-apoptotic family members”. Cell Death Differ. 6 (6): 525–32. (June 1999). doi:10.1038/sj.cdd.4400519. PMID 10381646.
“Interference of BAD (Bcl-xL/Bcl-2-associated death promoter)-induced apoptosis in mammalian cells by 14-3-3 isoforms and P11”. Mol. Endocrinol. 11 (12): 1858–67. (November 1997). doi:10.1210/me.11.12.1858. PMID 9369453.
“The proapoptotic protein Bad binds the amphipathic groove of 14-3-3zeta”. Biochim. Biophys. Acta 1547 (2): 313–9. (June 2001). doi:10.1016/S0167-4838(01)00202-3. PMID 11410287.

endojournals.org

mend.endojournals.org

“Interference of BAD (Bcl-xL/Bcl-2-associated death promoter)-induced apoptosis in mammalian cells by 14-3-3 isoforms and P11”. Mol. Endocrinol. 11 (12): 1858–67. (1997). doi:10.1210/me.11.12.1858. PMID 9369453.

ensembl.org

May2017.archive.ensembl.org

GRCh38: Ensembl release 89: ENSG00000002330 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000024959 - Ensembl, May 2017

harvard.edu

ui.adsabs.harvard.edu

“Synergistic anti-apoptotic activity between Bcl-2 and SMN implicated in spinal muscular atrophy”. Nature 390 (6658): 413–7. (November 1997). Bibcode: 1997Natur.390..413I. doi:10.1038/37144. PMID 9389483.

nih.gov

pubmed.ncbi.nlm.nih.gov

“The proapoptotic BH3-only protein BAD transduces cell death signals independently of its interaction with Bcl-2”. Cell Death Differ. 9 (11): 1240–7. (2002). doi:10.1038/sj.cdd.4401097. PMID 12404123.
“Interference of BAD (Bcl-xL/Bcl-2-associated death promoter)-induced apoptosis in mammalian cells by 14-3-3 isoforms and P11”. Mol. Endocrinol. 11 (12): 1858–67. (1997). doi:10.1210/me.11.12.1858. PMID 9369453.
Foster, T. C.; Sharrow, K. M.; Masse, J. R.; Norris, C. M.; Kumar, A. (2001-06-01). “Calcineurin links Ca2+ dysregulation with brain aging”. The Journal of Neuroscience: The Official Journal of the Society for Neuroscience 21 (11): 4066–4073. doi:10.1523/JNEUROSCI.21-11-04066.2001. ISSN 1529-2401. PMC 1201477. PMID 11356894.
“Differential targeting of prosurvival Bcl-2 proteins by their BH3-only ligands allows complementary apoptotic function”. Mol. Cell 17 (3): 393–403. (February 2005). doi:10.1016/j.molcel.2004.12.030. PMID 15694340.
“Bad, a heterodimeric partner for Bcl-XL and Bcl-2, displaces Bax and promotes cell death”. Cell 80 (2): 285–91. (January 1995). doi:10.1016/0092-8674(95)90411-5. PMID 7834748.
“Underphosphorylated BAD interacts with diverse antiapoptotic Bcl-2 family proteins to regulate apoptosis”. Apoptosis 6 (5): 319–30. (October 2001). doi:10.1023/A:1011319901057. PMID 11483855.
“Survival function of protein kinase C{iota} as a novel nitrosamine 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone-activated bad kinase”. J. Biol. Chem. 280 (16): 16045–52. (April 2005). doi:10.1074/jbc.M413488200. PMID 15705582.
“BAD partly reverses paclitaxel resistance in human ovarian cancer cells”. Oncogene 17 (19): 2419–27. (November 1998). doi:10.1038/sj.onc.1202180. PMID 9824152.
“Development of a high-throughput fluorescence polarization assay for Bcl-x(L)”. Anal. Biochem. 307 (1): 70–5. (August 2002). doi:10.1016/S0003-2697(02)00028-3. PMID 12137781.
“The anti-apoptotic molecules Bcl-xL and Bcl-w target protein phosphatase 1alpha to Bad”. Eur. J. Immunol. 32 (7): 1847–55. (July 2002). doi:10.1002/1521-4141(200207)32:7<1847::AID-IMMU1847>3.0.CO;2-7. PMID 12115603.
“Human homologue of S. pombe Rad9 interacts with BCL-2/BCL-xL and promotes apoptosis”. Nat. Cell Biol. 2 (1): 1–6. (January 2000). doi:10.1038/71316. PMID 10620799.
“Rationale for Bcl-xL/Bad peptide complex formation from structure, mutagenesis, and biophysical studies”. Protein Sci. 9 (12): 2528–34. (Dec 2000). doi:10.1110/ps.9.12.2528. PMC 2144516. PMID 11206074.
“BAD/BCL-[X(L)] heterodimerization leads to bypass of G0/G1 arrest”. Oncogene 20 (33): 4507–18. (July 2001). doi:10.1038/sj.onc.1204584. PMID 11494146.
“Synergistic anti-apoptotic activity between Bcl-2 and SMN implicated in spinal muscular atrophy”. Nature 390 (6658): 413–7. (November 1997). Bibcode: 1997Natur.390..413I. doi:10.1038/37144. PMID 9389483.
“PCNA interacts with hHus1/hRad9 in response to DNA damage and replication inhibition”. Oncogene 19 (46): 5291–7. (November 2000). doi:10.1038/sj.onc.1203901. PMID 11077446.
“Survival activity of Bcl-2 homologs Bcl-w and A1 only partially correlates with their ability to bind pro-apoptotic family members”. Cell Death Differ. 6 (6): 525–32. (June 1999). doi:10.1038/sj.cdd.4400519. PMID 10381646.
“Interference of BAD (Bcl-xL/Bcl-2-associated death promoter)-induced apoptosis in mammalian cells by 14-3-3 isoforms and P11”. Mol. Endocrinol. 11 (12): 1858–67. (November 1997). doi:10.1210/me.11.12.1858. PMID 9369453.
“The proapoptotic protein Bad binds the amphipathic groove of 14-3-3zeta”. Biochim. Biophys. Acta 1547 (2): 313–9. (June 2001). doi:10.1016/S0167-4838(01)00202-3. PMID 11410287.

ncbi.nlm.nih.gov

pmc.ncbi.nlm.nih.gov

Foster, T. C.; Sharrow, K. M.; Masse, J. R.; Norris, C. M.; Kumar, A. (2001-06-01). “Calcineurin links Ca2+ dysregulation with brain aging”. The Journal of Neuroscience: The Official Journal of the Society for Neuroscience 21 (11): 4066–4073. doi:10.1523/JNEUROSCI.21-11-04066.2001. ISSN 1529-2401. PMC 1201477. PMID 11356894.
“Rationale for Bcl-xL/Bad peptide complex formation from structure, mutagenesis, and biophysical studies”. Protein Sci. 9 (12): 2528–34. (Dec 2000). doi:10.1110/ps.9.12.2528. PMC 2144516. PMID 11206074.

wikipedia.org

en.wikipedia.org

GRCh38: Ensembl release 89: ENSG00000002330 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000024959 - Ensembl, May 2017

worldcat.org

Helmreich, E. J. M. (2001). The biochemistry of cell signalling. Oxford: Oxford University Press. pp. 238-243. ISBN 0-19-850820-4. OCLC 45743304

search.worldcat.org

Foster, T. C.; Sharrow, K. M.; Masse, J. R.; Norris, C. M.; Kumar, A. (2001-06-01). “Calcineurin links Ca2+ dysregulation with brain aging”. The Journal of Neuroscience: The Official Journal of the Society for Neuroscience 21 (11): 4066–4073. doi:10.1523/JNEUROSCI.21-11-04066.2001. ISSN 1529-2401. PMC 1201477. PMID 11356894.