ATF6 (Japanese Wikipedia)

Analysis of information sources in references of the Wikipedia article "ATF6" in Japanese language version.

Last modified: 03:20:48, 2 January 2025 (UTC)

Ref.Un. Ref.Website

Global rank Japanese rank

5^th place

11^th place

2^nd place

3^rd place

11adsabs.harvard.edu

14^th place

60^th place

adsabs.harvard.edu (Global: 14^th place; Japanese: 60^th place)

ui.adsabs.harvard.edu

“Comprehensive identification of human bZIP interactions with coiled-coil arrays”. Science 300 (5628): 2097–101. (2003). Bibcode:2003Sci...300.2097N. doi:10.1126/science.1084648. PMID 12805554.

doi.org (Global: 2^nd place; Japanese: 3^rd place)

“Mammalian Transcription Factor ATF6 Is Synthesized as a Transmembrane Protein and Activated by Proteolysis in Response to Endoplasmic Reticulum Stress”. Mol. Biol. Cell 10 (11): 3787–99. (1999). doi:10.1091/mbc.10.11.3787. PMC 25679. PMID 10564271.
“ER stress regulation of ATF6 localization by dissociation of BiP/GRP78 binding and unmasking of Golgi localization signals”. Dev. Cell 3 (1): 99-111. (2002). doi:10.1016/s1534-5807(02)00203-4. PMID 12110171.
“The luminal domain of ATF6 senses endoplasmic reticulum (ER) stress and causes translocation of ATF6 from the ER to the Golgi”. J. Biol. Chem. 277 (15): 13045–52. (2002). doi:10.1074/jbc.M110636200. PMID 11821395.
“ER stress induces cleavage of membrane-bound ATF6 by the same proteases that process SREBPs”. Mol. Cell 6 (6): 1355–64. (2001). doi:10.1016/S1097-2765(00)00133-7. PMID 11163209.
“A serine protease inhibitor prevents endoplasmic reticulum stress-induced cleavage but not transport of the membrane-bound transcription factor ATF6”. J. Biol. Chem. 278 (33): 31024–32. (2003). doi:10.1074/jbc.M300923200. PMID 12782636.
“Requirement of the p38 mitogen-activated protein kinase signalling pathway for the induction of the 78 kDa glucose-regulated protein/immunoglobulin heavy-chain binding protein by azetidine stress: activating transcription factor 6 as a target for stress-induced phosphorylation”. Biochem. J. 366 (Pt 3): 787–95. (2002). doi:10.1042/BJ20011802. PMC 1222838. PMID 12076252.
“Identification of the cis-acting endoplasmic reticulum stress response element responsible for transcriptional induction of mammalian glucose-regulated proteins. Involvement of basic leucine zipper transcription factors”. J. Biol. Chem. 273 (50): 33741–9. (1999). doi:10.1074/jbc.273.50.33741. PMID 9837962.
“The molecular biology and nomenclature of the activating transcription factor/cAMP responsive element binding family of transcription factors: activating transcription factor proteins and homeostasis”. Gene 273 (1): 1–11. (2001). doi:10.1016/S0378-1119(01)00551-0. PMID 11483355.
“Identification of the G13 (cAMP-response-element-binding protein-related protein) gene product related to activating transcription factor 6 as a transcriptional activator of the mammalian unfolded protein response”. Biochem J. 355 (Pt 1): 19-28. (2001). doi:10.1042/0264-6021:3550019. PMC 1221707. PMID 11256944.
“Nitric oxide-induced apoptosis in RAW 264.7 macrophages is mediated by endoplasmic reticulum stress pathway involving ATF6 and CHOP”. J. Biol. Chem. 277 (14): 12343–50. (2002). doi:10.1074/jbc.M107988200. PMID 11805088.
“XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor”. Cell 107 (7): 881-91. (2001). doi:10.1016/s0092-8674(01)00611-0. PMID 11779464.
“Distinct roles of activating transcription factor 6 (ATF6) and double-stranded RNA-activated protein kinase-like endoplasmic reticulum kinase (PERK) in transcription during the mammalian unfolded protein response”. Biochem. J. 366 (Pt 2): 585–94. (2002). doi:10.1042/BJ20020391. PMC 1222788. PMID 12014989.
“ATF6 is a transcription factor specializing in the regulation of quality control proteins in the endoplasmic reticulum”. Cell Struct Funct 33 (1): 75-89. (2008). doi:10.1247/csf.07044. PMID 18360008.
“Coordination of ATF6-mediated transcription and ATF6 degradation by a domain that is shared with the viral transcription factor, VP16”. J. Biol. Chem. 277 (23): 20734–9. (2002). doi:10.1074/jbc.M201749200. PMID 11909875.
“Transcription factor ATF cDNA clones: an extensive family of leucine zipper proteins able to selectively form DNA-binding heterodimers”. Genes Dev. 3 (12B): 2083–90. (December 1989). doi:10.1101/gad.3.12b.2083. PMID 2516827.
“Activating transcription factor 6 polymorphisms and haplotypes are associated with impaired glucose homeostasis and type 2 diabetes in Dutch Caucasians”. J. Clin. Endocrinol. Metab. 92 (7): 2720–5. (July 2007). doi:10.1210/jc.2006-2280. PMID 17440018.
“Effects of the isoform-specific characteristics of ATF6 alpha and ATF6 beta on endoplasmic reticulum stress response gene expression and cell viability”. J Biol Chem. 282 (31): 22865-78. (2007). doi:10.1074/jbc.M701213200. PMID 17522056.
“Comprehensive identification of human bZIP interactions with coiled-coil arrays”. Science 300 (5628): 2097–101. (2003). Bibcode:2003Sci...300.2097N. doi:10.1126/science.1084648. PMID 12805554.
“ATF6 as a transcription activator of the endoplasmic reticulum stress element: thapsigargin stress-induced changes and synergistic interactions with NF-Y and YY1”. Mol. Cell. Biol. 20 (14): 5096–106. (2000). doi:10.1128/MCB.20.14.5096-5106.2000. PMC 85959. PMID 10866666.
“Endoplasmic Reticulum Stress-Induced Formation of Transcription Factor Complex ERSF Including NF-Y (CBF) and Activating Transcription Factors 6α and 6β That Activates the Mammalian Unfolded Protein Response”. Mol. Cell. Biol. 21 (4): 1239–48. (2001). doi:10.1128/MCB.21.4.1239-1248.2001. PMC 99577. PMID 11158310.
“Identification of TFII-I as the Endoplasmic Reticulum Stress Response Element Binding Factor ERSF: Its Autoregulation by Stress and Interaction with ATF6”. Mol. Cell. Biol. 21 (9): 3220–33. (2001). doi:10.1128/MCB.21.9.3220-3233.2001. PMC 86961. PMID 11287625.
“Interaction of ATF6 and serum response factor”. Mol. Cell. Biol. 17 (9): 4957–66. (September 1997). doi:10.1128/MCB.17.9.4957. PMC 232347. PMID 9271374.
“Activation of the ATF6, XBP1 and grp78 genes in human hepatocellular carcinoma: a possible involvement of the ER stress pathway in hepatocarcinogenesis”. J. Hepatol. 38 (5): 605–14. (2004). doi:10.1016/S0168-8278(03)00029-1. PMID 12713871.
“Hepatitis C Virus Subgenomic Replicons Induce Endoplasmic Reticulum Stress Activating an Intracellular Signaling Pathway”. J. Virol. 76 (15): 7453–9. (2002). doi:10.1128/JVI.76.15.7453-7459.2002. PMC 136367. PMID 12097557.

nih.gov (Global: 5^th place; Japanese: 11^th place)

pubmed.ncbi.nlm.nih.gov

“Mammalian Transcription Factor ATF6 Is Synthesized as a Transmembrane Protein and Activated by Proteolysis in Response to Endoplasmic Reticulum Stress”. Mol. Biol. Cell 10 (11): 3787–99. (1999). doi:10.1091/mbc.10.11.3787. PMC 25679. PMID 10564271.
“ER stress regulation of ATF6 localization by dissociation of BiP/GRP78 binding and unmasking of Golgi localization signals”. Dev. Cell 3 (1): 99-111. (2002). doi:10.1016/s1534-5807(02)00203-4. PMID 12110171.
“The luminal domain of ATF6 senses endoplasmic reticulum (ER) stress and causes translocation of ATF6 from the ER to the Golgi”. J. Biol. Chem. 277 (15): 13045–52. (2002). doi:10.1074/jbc.M110636200. PMID 11821395.
“ER stress induces cleavage of membrane-bound ATF6 by the same proteases that process SREBPs”. Mol. Cell 6 (6): 1355–64. (2001). doi:10.1016/S1097-2765(00)00133-7. PMID 11163209.
“A serine protease inhibitor prevents endoplasmic reticulum stress-induced cleavage but not transport of the membrane-bound transcription factor ATF6”. J. Biol. Chem. 278 (33): 31024–32. (2003). doi:10.1074/jbc.M300923200. PMID 12782636.
“Requirement of the p38 mitogen-activated protein kinase signalling pathway for the induction of the 78 kDa glucose-regulated protein/immunoglobulin heavy-chain binding protein by azetidine stress: activating transcription factor 6 as a target for stress-induced phosphorylation”. Biochem. J. 366 (Pt 3): 787–95. (2002). doi:10.1042/BJ20011802. PMC 1222838. PMID 12076252.
“Identification of the cis-acting endoplasmic reticulum stress response element responsible for transcriptional induction of mammalian glucose-regulated proteins. Involvement of basic leucine zipper transcription factors”. J. Biol. Chem. 273 (50): 33741–9. (1999). doi:10.1074/jbc.273.50.33741. PMID 9837962.
“The molecular biology and nomenclature of the activating transcription factor/cAMP responsive element binding family of transcription factors: activating transcription factor proteins and homeostasis”. Gene 273 (1): 1–11. (2001). doi:10.1016/S0378-1119(01)00551-0. PMID 11483355.
“Identification of the G13 (cAMP-response-element-binding protein-related protein) gene product related to activating transcription factor 6 as a transcriptional activator of the mammalian unfolded protein response”. Biochem J. 355 (Pt 1): 19-28. (2001). doi:10.1042/0264-6021:3550019. PMC 1221707. PMID 11256944.
“Nitric oxide-induced apoptosis in RAW 264.7 macrophages is mediated by endoplasmic reticulum stress pathway involving ATF6 and CHOP”. J. Biol. Chem. 277 (14): 12343–50. (2002). doi:10.1074/jbc.M107988200. PMID 11805088.
“XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor”. Cell 107 (7): 881-91. (2001). doi:10.1016/s0092-8674(01)00611-0. PMID 11779464.
“Distinct roles of activating transcription factor 6 (ATF6) and double-stranded RNA-activated protein kinase-like endoplasmic reticulum kinase (PERK) in transcription during the mammalian unfolded protein response”. Biochem. J. 366 (Pt 2): 585–94. (2002). doi:10.1042/BJ20020391. PMC 1222788. PMID 12014989.
“ATF6 is a transcription factor specializing in the regulation of quality control proteins in the endoplasmic reticulum”. Cell Struct Funct 33 (1): 75-89. (2008). doi:10.1247/csf.07044. PMID 18360008.
“Coordination of ATF6-mediated transcription and ATF6 degradation by a domain that is shared with the viral transcription factor, VP16”. J. Biol. Chem. 277 (23): 20734–9. (2002). doi:10.1074/jbc.M201749200. PMID 11909875.
“Transcription factor ATF cDNA clones: an extensive family of leucine zipper proteins able to selectively form DNA-binding heterodimers”. Genes Dev. 3 (12B): 2083–90. (December 1989). doi:10.1101/gad.3.12b.2083. PMID 2516827.
“Activating transcription factor 6 polymorphisms and haplotypes are associated with impaired glucose homeostasis and type 2 diabetes in Dutch Caucasians”. J. Clin. Endocrinol. Metab. 92 (7): 2720–5. (July 2007). doi:10.1210/jc.2006-2280. PMID 17440018.
“Effects of the isoform-specific characteristics of ATF6 alpha and ATF6 beta on endoplasmic reticulum stress response gene expression and cell viability”. J Biol Chem. 282 (31): 22865-78. (2007). doi:10.1074/jbc.M701213200. PMID 17522056.
“Comprehensive identification of human bZIP interactions with coiled-coil arrays”. Science 300 (5628): 2097–101. (2003). Bibcode:2003Sci...300.2097N. doi:10.1126/science.1084648. PMID 12805554.
“ATF6 as a transcription activator of the endoplasmic reticulum stress element: thapsigargin stress-induced changes and synergistic interactions with NF-Y and YY1”. Mol. Cell. Biol. 20 (14): 5096–106. (2000). doi:10.1128/MCB.20.14.5096-5106.2000. PMC 85959. PMID 10866666.
“Endoplasmic Reticulum Stress-Induced Formation of Transcription Factor Complex ERSF Including NF-Y (CBF) and Activating Transcription Factors 6α and 6β That Activates the Mammalian Unfolded Protein Response”. Mol. Cell. Biol. 21 (4): 1239–48. (2001). doi:10.1128/MCB.21.4.1239-1248.2001. PMC 99577. PMID 11158310.
“Identification of TFII-I as the Endoplasmic Reticulum Stress Response Element Binding Factor ERSF: Its Autoregulation by Stress and Interaction with ATF6”. Mol. Cell. Biol. 21 (9): 3220–33. (2001). doi:10.1128/MCB.21.9.3220-3233.2001. PMC 86961. PMID 11287625.
“Interaction of ATF6 and serum response factor”. Mol. Cell. Biol. 17 (9): 4957–66. (September 1997). doi:10.1128/MCB.17.9.4957. PMC 232347. PMID 9271374.
“Activation of the ATF6, XBP1 and grp78 genes in human hepatocellular carcinoma: a possible involvement of the ER stress pathway in hepatocarcinogenesis”. J. Hepatol. 38 (5): 605–14. (2004). doi:10.1016/S0168-8278(03)00029-1. PMID 12713871.
“Hepatitis C Virus Subgenomic Replicons Induce Endoplasmic Reticulum Stress Activating an Intracellular Signaling Pathway”. J. Virol. 76 (15): 7453–9. (2002). doi:10.1128/JVI.76.15.7453-7459.2002. PMC 136367. PMID 12097557.

pmc.ncbi.nlm.nih.gov

ncbi.nlm.nih.gov