Calnexin (English Wikipedia)

Analysis of information sources in references of the Wikipedia article "Calnexin" in English language version.

refsWebsite

Global rank English rank

25nih.gov

4^th place

15doi.org

2^nd place

2ensembl.org

1,626^th place

1,007^th place

2harvard.edu

18^th place

17^th place

1semanticscholar.org

11^th place

8^th place

doi.org

Wada I, Rindress D, Cameron PH, Ou WJ, Doherty JJ 2nd, Louvard D, Bell AW, Dignard D, Thomas DY, Bergeron JJ (1991). "SSR alpha and associated calnexin are major calcium binding proteins of the endoplasmic reticulum membrane". J Biol Chem. 226 (29): 19599–610. doi:10.1016/S0021-9258(18)55036-5. PMID 1918067.
Paskevicius T, Farraj RA, Michalak M, Agellon LB (2023). Lim D (ed.). "Calnexin, More Than Just a Molecular Chaperone". Cells. 12 (3): 403. doi:10.3390/cells12030403. PMC 9913998. PMID 36766745. Article No. 403.
Ou WJ, Cameron PH, Thomas DY, Bergeron JJ (1993). "Association of folding intermediates of glycoproteins". Nature. 364 (644): 771–6. doi:10.1038/364771a0. PMID 8102790. S2CID 4340769.
Hammond C, Braakman I, Helenius A (1984). "Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control". Proc Natl Acad Sci USA. 91 (3): 913–7. doi:10.1073/pnas.91.3.913. PMC 521423. PMID 8302866.
Gañán S, Cazzulo JJ, Parodi AJ (1991). "A major proportion of N-glycoproteins are transiently glucosylated in the endoplasmic reticulum". Biochemistry. 30 (12): 3098–104. doi:10.1021/bi00226a017. PMID 1826090.
Jacob CA, Bodmer D, Spirig U, Battig P, Marcil A, Dignard D, Bergeron JJ, Thomas DY, Aebi M (2001). "Htm1p, a mannosidase-like protein, is involved in glycoprotein degradation in yeast". EMBO Rep. 2 (5): 423–30. doi:10.1093/embo-reports/kve089. PMC 1083883. PMID 11375935.
Hosokawa N, Wada I, Hasegawa K, Yorihuzi T, Tremblay LO, Herscovics A, Nagata K (2001). "A novel ER alpha-mannosidase-like protein accelerates ER-associated degradation". EMBO Rep. 2 (5): 415–2. doi:10.1093/embo-reports/kve084. PMC 1083879. PMID 11375934.
Lee AH, Iwakoshi NN, Glimcher LH (2003). "XBP-1 regulates a subset of endoplasmic reticulum chaperone genes in the unfolded protein response". Mol Cell Biol. 23 (21): 5448–59. doi:10.1128/mcb.23.21.7448-7459.2003. PMC 207643. PMID 14559994.
Quan EM, Kamiya D, Denic V, Weibezahn J, Kato K, Weissman JS (2008). "Defining the glycan destruction signal for endoplasmic reticulum-associated degradation". Mol Cell. 32 (6): 870–7. doi:10.1016/j.molcel.2008.11.017. PMC 2873636. PMID 19111666.
Zapun A, Darby NJ, Tessier DC, Michalak M, Bergeron JJ, Thomas DY (1998). "Enhanced catalysis of ribonuclease B folding by the interaction of calnexin or calreticulin with ERp57". J Biol Chem. 273 (211): 6009–12. doi:10.1074/jbc.273.11.6009. PMID 9497314.
Bergeron JJ, Brenner MB, Thomas DY, Williams DB (1994). "Calnexin: a membrane-bound chaperone of the endoplasmic reticulum". Trends Biochem Sci. 19 (3): 124–8. doi:10.1016/0968-0004(94)90205-4. PMID 8203019.
Dickson KM, Bergeron JJ, Shames I, Colby J, Nguyen DT, Chevet E, Thomas DY, Snipes GJ (2002). "Association of calnexin with mutant peripheral myelin protein-22 ex vivo: a basis for "gain-of-function" ER diseases". Proc Natl Acad Sci USA. 99 (15): 9852–7. Bibcode:2002PNAS...99.9852D. doi:10.1073/pnas.152621799. PMC 125041. PMID 12119418.
Hara T, Hashimoto Y, Akuzawa T, Hirai R, Kobayashi H, Sato K (2014). "Rer1 and calnexin regulate endoplasmic reticulum retention of a peripheral myelin protein 22 mutant that causes type 1A Charcot-Marie-Tooth disease". Sci Rep. 4: 1–11. Bibcode:2014NatSR...4E6992H. doi:10.1038/srep06992. PMC 4227013. PMID 25385046.
Schrag JD, Bergeron JJ, Li Y, Borisova S, Hahn M, Thomas DY, Cygler M (2001). "The structure of calnexin, an ER chaperone involved in quality control of protein folding". Mol Cell. 8 (3): 633–44. doi:10.1016/s1097-2765(01)00318-5. PMID 11583625.
Ou WJ, Bergeron JJ, Li Y, Kang CY, Thomas DY (1995). "Conformational changes induced in the endoplasmic reticulum luminal domain of calnexin by Mg-ATP and Ca2+". J Biol Chem. 270 (30): 18051–9. doi:10.1074/jbc.270.30.18051. PMID 7629114.

ensembl.org

May2017.archive.ensembl.org

ENSG00000127022 GRCh38: Ensembl release 89: ENSG00000283777, ENSG00000127022 – Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000020368 – Ensembl, May 2017

harvard.edu

ui.adsabs.harvard.edu

Dickson KM, Bergeron JJ, Shames I, Colby J, Nguyen DT, Chevet E, Thomas DY, Snipes GJ (2002). "Association of calnexin with mutant peripheral myelin protein-22 ex vivo: a basis for "gain-of-function" ER diseases". Proc Natl Acad Sci USA. 99 (15): 9852–7. Bibcode:2002PNAS...99.9852D. doi:10.1073/pnas.152621799. PMC 125041. PMID 12119418.
Hara T, Hashimoto Y, Akuzawa T, Hirai R, Kobayashi H, Sato K (2014). "Rer1 and calnexin regulate endoplasmic reticulum retention of a peripheral myelin protein 22 mutant that causes type 1A Charcot-Marie-Tooth disease". Sci Rep. 4: 1–11. Bibcode:2014NatSR...4E6992H. doi:10.1038/srep06992. PMC 4227013. PMID 25385046.

nih.gov

pubmed.ncbi.nlm.nih.gov

Wada I, Rindress D, Cameron PH, Ou WJ, Doherty JJ 2nd, Louvard D, Bell AW, Dignard D, Thomas DY, Bergeron JJ (1991). "SSR alpha and associated calnexin are major calcium binding proteins of the endoplasmic reticulum membrane". J Biol Chem. 226 (29): 19599–610. doi:10.1016/S0021-9258(18)55036-5. PMID 1918067.
Paskevicius T, Farraj RA, Michalak M, Agellon LB (2023). Lim D (ed.). "Calnexin, More Than Just a Molecular Chaperone". Cells. 12 (3): 403. doi:10.3390/cells12030403. PMC 9913998. PMID 36766745. Article No. 403.
Ou WJ, Cameron PH, Thomas DY, Bergeron JJ (1993). "Association of folding intermediates of glycoproteins". Nature. 364 (644): 771–6. doi:10.1038/364771a0. PMID 8102790. S2CID 4340769.
Hammond C, Braakman I, Helenius A (1984). "Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control". Proc Natl Acad Sci USA. 91 (3): 913–7. doi:10.1073/pnas.91.3.913. PMC 521423. PMID 8302866.
Gañán S, Cazzulo JJ, Parodi AJ (1991). "A major proportion of N-glycoproteins are transiently glucosylated in the endoplasmic reticulum". Biochemistry. 30 (12): 3098–104. doi:10.1021/bi00226a017. PMID 1826090.
Jacob CA, Bodmer D, Spirig U, Battig P, Marcil A, Dignard D, Bergeron JJ, Thomas DY, Aebi M (2001). "Htm1p, a mannosidase-like protein, is involved in glycoprotein degradation in yeast". EMBO Rep. 2 (5): 423–30. doi:10.1093/embo-reports/kve089. PMC 1083883. PMID 11375935.
Hosokawa N, Wada I, Hasegawa K, Yorihuzi T, Tremblay LO, Herscovics A, Nagata K (2001). "A novel ER alpha-mannosidase-like protein accelerates ER-associated degradation". EMBO Rep. 2 (5): 415–2. doi:10.1093/embo-reports/kve084. PMC 1083879. PMID 11375934.
Lee AH, Iwakoshi NN, Glimcher LH (2003). "XBP-1 regulates a subset of endoplasmic reticulum chaperone genes in the unfolded protein response". Mol Cell Biol. 23 (21): 5448–59. doi:10.1128/mcb.23.21.7448-7459.2003. PMC 207643. PMID 14559994.
Quan EM, Kamiya D, Denic V, Weibezahn J, Kato K, Weissman JS (2008). "Defining the glycan destruction signal for endoplasmic reticulum-associated degradation". Mol Cell. 32 (6): 870–7. doi:10.1016/j.molcel.2008.11.017. PMC 2873636. PMID 19111666.
Zapun A, Darby NJ, Tessier DC, Michalak M, Bergeron JJ, Thomas DY (1998). "Enhanced catalysis of ribonuclease B folding by the interaction of calnexin or calreticulin with ERp57". J Biol Chem. 273 (211): 6009–12. doi:10.1074/jbc.273.11.6009. PMID 9497314.
Bergeron JJ, Brenner MB, Thomas DY, Williams DB (1994). "Calnexin: a membrane-bound chaperone of the endoplasmic reticulum". Trends Biochem Sci. 19 (3): 124–8. doi:10.1016/0968-0004(94)90205-4. PMID 8203019.
Dickson KM, Bergeron JJ, Shames I, Colby J, Nguyen DT, Chevet E, Thomas DY, Snipes GJ (2002). "Association of calnexin with mutant peripheral myelin protein-22 ex vivo: a basis for "gain-of-function" ER diseases". Proc Natl Acad Sci USA. 99 (15): 9852–7. Bibcode:2002PNAS...99.9852D. doi:10.1073/pnas.152621799. PMC 125041. PMID 12119418.
Hara T, Hashimoto Y, Akuzawa T, Hirai R, Kobayashi H, Sato K (2014). "Rer1 and calnexin regulate endoplasmic reticulum retention of a peripheral myelin protein 22 mutant that causes type 1A Charcot-Marie-Tooth disease". Sci Rep. 4: 1–11. Bibcode:2014NatSR...4E6992H. doi:10.1038/srep06992. PMC 4227013. PMID 25385046.
Schrag JD, Bergeron JJ, Li Y, Borisova S, Hahn M, Thomas DY, Cygler M (2001). "The structure of calnexin, an ER chaperone involved in quality control of protein folding". Mol Cell. 8 (3): 633–44. doi:10.1016/s1097-2765(01)00318-5. PMID 11583625.
Ou WJ, Bergeron JJ, Li Y, Kang CY, Thomas DY (1995). "Conformational changes induced in the endoplasmic reticulum luminal domain of calnexin by Mg-ATP and Ca2+". J Biol Chem. 270 (30): 18051–9. doi:10.1074/jbc.270.30.18051. PMID 7629114.

ncbi.nlm.nih.gov

"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
Paskevicius T, Farraj RA, Michalak M, Agellon LB (2023). Lim D (ed.). "Calnexin, More Than Just a Molecular Chaperone". Cells. 12 (3): 403. doi:10.3390/cells12030403. PMC 9913998. PMID 36766745. Article No. 403.
Hammond C, Braakman I, Helenius A (1984). "Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control". Proc Natl Acad Sci USA. 91 (3): 913–7. doi:10.1073/pnas.91.3.913. PMC 521423. PMID 8302866.
Jacob CA, Bodmer D, Spirig U, Battig P, Marcil A, Dignard D, Bergeron JJ, Thomas DY, Aebi M (2001). "Htm1p, a mannosidase-like protein, is involved in glycoprotein degradation in yeast". EMBO Rep. 2 (5): 423–30. doi:10.1093/embo-reports/kve089. PMC 1083883. PMID 11375935.
Hosokawa N, Wada I, Hasegawa K, Yorihuzi T, Tremblay LO, Herscovics A, Nagata K (2001). "A novel ER alpha-mannosidase-like protein accelerates ER-associated degradation". EMBO Rep. 2 (5): 415–2. doi:10.1093/embo-reports/kve084. PMC 1083879. PMID 11375934.
Lee AH, Iwakoshi NN, Glimcher LH (2003). "XBP-1 regulates a subset of endoplasmic reticulum chaperone genes in the unfolded protein response". Mol Cell Biol. 23 (21): 5448–59. doi:10.1128/mcb.23.21.7448-7459.2003. PMC 207643. PMID 14559994.
Quan EM, Kamiya D, Denic V, Weibezahn J, Kato K, Weissman JS (2008). "Defining the glycan destruction signal for endoplasmic reticulum-associated degradation". Mol Cell. 32 (6): 870–7. doi:10.1016/j.molcel.2008.11.017. PMC 2873636. PMID 19111666.
Dickson KM, Bergeron JJ, Shames I, Colby J, Nguyen DT, Chevet E, Thomas DY, Snipes GJ (2002). "Association of calnexin with mutant peripheral myelin protein-22 ex vivo: a basis for "gain-of-function" ER diseases". Proc Natl Acad Sci USA. 99 (15): 9852–7. Bibcode:2002PNAS...99.9852D. doi:10.1073/pnas.152621799. PMC 125041. PMID 12119418.
Hara T, Hashimoto Y, Akuzawa T, Hirai R, Kobayashi H, Sato K (2014). "Rer1 and calnexin regulate endoplasmic reticulum retention of a peripheral myelin protein 22 mutant that causes type 1A Charcot-Marie-Tooth disease". Sci Rep. 4: 1–11. Bibcode:2014NatSR...4E6992H. doi:10.1038/srep06992. PMC 4227013. PMID 25385046.

semanticscholar.org

api.semanticscholar.org

Ou WJ, Cameron PH, Thomas DY, Bergeron JJ (1993). "Association of folding intermediates of glycoproteins". Nature. 364 (644): 771–6. doi:10.1038/364771a0. PMID 8102790. S2CID 4340769.