Janne
Molnes
Senior Engineer
Visit Address:
Children's clinic, 3. etg.
Room:
3008
Postal Address:
Postboks 7804
5021 Bergen
Phone:
+47 55 97 52 77
E-mail:
Journal articles
- 2014. GCK-MODY diabetes as a protein misfolding disease: The mutation R275C promotes protein misfolding, self-association and cellular degradation. Molecular and Cellular Endocrinology. 382: 55-65. doi: 10.1016/j.mce.2013.08.020
- 2013. SUMOylation of pancreatic glucokinase regulates its cellular stability and activity. Journal of Biological Chemistry. 288: 5951-5962. doi: 10.1074/jbc.M112.393769
- 2013. A novel GATA6 mutation in a child with congenital heart malformation and neonatal diabetes. Clinical Case Reports. 1: 86-90. doi: 10.1002/ccr3.33
- 2013. An Egyptian family with H syndrome due to a novel mutation in SLC29A3 illustrating overlapping features with pigmented hypertrichotic dermatosis with insulin-dependent diabetes and Faisalabad histiocytosis. Pediatric Diabetes. 14: 466-472. doi: 10.1111/j.1399-5448.2012.00925.x
- 2013. Assessing the phenotypic effects in the general population of rare variants in genes for a dominant Mendelian form of diabetes. Nature Genetics. 45: 1380-1385. doi: 10.1038/ng.2794
- 2013. Prevalence of monogenic diabetes in the population-based Norwegian Childhood Diabetes Registry. Diabetologia. 56: 1512-1519. doi: 10.1007/s00125-013-2916-y
- 2013. Clinical and molecular characterization of neonatal diabetes and monogenic syndromic diabetes in Asian Indian children. Clinical Genetics. 83: 439-445. doi: 10.1111/j.1399-0004.2012.01939.x
- 2013. Monogenetic diabetes mellitus in Norway :. Norsk Epidemiologi. 23: 55-60.
- 2012. HNF1B mutation in a Turkish child with renal and exocrine pancreas insufficiency, diabetes and liver disease. Pediatric Diabetes. 13: e1-e5. doi: 10.1111/j.1399-5448.2011.00773.x
- 2012. Exome sequencing and genetic testing for MODY. PLoS ONE. 7. 8 pages. doi: 10.1371/journal.pone.0038050
- 2012. GCK-MODY diabetes associated with protein misfolding, cellular self-association and degradation. Biochimica et Biophysica Acta - Molecular Basis of Disease. 1822: 1705-1715. doi: 10.1016/j.bbadis.2012.07.005
- 2011. Binding of ATP at the active site of human pancreatic glucokinase - nucleotide-induced conformational changes with possible implications for its kinetic cooperativity. The FEBS Journal. 278: 2372-2386. doi: 10.1111/j.1742-4658.2011.08160.x
- 2008. Catalytic activation of human glucokinase by substrate binding - residue contacts involved in the binding of D-glucose to the super-open form and conformational transitions. The FEBS Journal. 275: 2467-2481. doi: 10.1111/j.1742-4658.2008.06391.x
- 2008. Diagnostic screening of MODY2/GCK mutations in the Norwegian MODY Registry. Pediatric Diabetes. 9: 442-449. doi: 10.1111/j.1399-5448.2008.00399.x
- 2007. Allosteric activation of human glucokinase by free polyubiquitin chains and its ubiquitin-dependent cotranslational proteasomal degradation. Journal of Biological Chemistry. 282: 22757-22764. doi: 10.1074/jbc.M700517200
- 2005. Two novel Kir6.2 mutations affecting the ATP sensitivity of the K-ATP channel are the cause of Permanent Neonatal Diabetes. Biophysical Journal. 88: 285A-285A.
- 2005. Kir6.2 mutations causing neonatal diabetes provide new insights into Kir6.2-SUR1 interactions. EMBO Journal. 24: 2318-2330.
- 2004. Activating mutations in the gene encoding the ATP-sensitive potassium-channel subunit Kir6.2 and permanent neonatal diabetes. New England Journal of Medicine. 350: 1838-1849.
- 2004. Permanent neonatal diabetes due to mutations in KCNJ11 encoding Kir6.2 - Patient characteristics and initial response to sulfonylurea therapy. Diabetes. 53: 2713-2718.
- 2003. Permanent neonatal diabetes caused by glucokinase deficiency; inborn error of the glucose-insulin signaling pathway. Diabetes. 52: 2854-2860.
- 2003. Permanent neonatal diabetes mellitus due to glucokinase deficiency- an inborn error of the glucose-insulin signalling pathway. Diabetes. 52: 2854-2860.
Reports and theses
- 2012. Human pancreatic glucokinase; Structural and physico-chemical studies related to catalytic activation, kinetic cooperativity and GCK-diabetes. University of Bergen.
- 1998. Antigenic drift in the HA1 domain of influenza A(H3N2) strains isolated in Norway in 1992-6 and relationship to vaccine and reference viruses. Cand.scient. thesis.. [Mangler utgivernavn].
- 1997. Antigenic drift in the HA<SUB>1</SUB> domain of influenza A(H3N2) strains isolated in Norway in 1992-6 and relationship to vaccine and reference viruses. [Mangler utgivernavn]. 95 pages.
More information in national current research information system (CRIStin)
