Year |
Citation |
Score |
2019 |
Mayo CB, Erlandsen H, Mouser DJ, Feinstein AG, Robinson VL, May ER, Cole JL. Structural Basis of Protein Kinase R Autophosphorylation. Biochemistry. 58: 2967-2977. DOI: 10.2210/Pdb6D3L/Pdb |
0.307 |
|
2015 |
Rutsch F, MacDougall M, Lu C, Buers I, Mamaeva O, Nitschke Y, Rice GI, Erlandsen H, Kehl HG, Thiele H, Nürnberg P, Höhne W, Crow YJ, Feigenbaum A, Hennekam RC. A specific IFIH1 gain-of-function mutation causes Singleton-Merten syndrome. American Journal of Human Genetics. 96: 275-82. PMID 25620204 DOI: 10.1016/J.Ajhg.2014.12.014 |
0.351 |
|
2015 |
Buers I, Nitschke Y, Hennekam R, MacDougall M, Lu C, Mamaeva O, Rice G, Erlandsen H, Kehl H, Thiele H, Nürnberg P, Höhne W, Crow Y, Feigenbaum A, Rutsch F. Singleton-Merten Syndrome: a rare autoimmune disorder caused by a specific IFIH1 mutation Molecular and Cellular Pediatrics. 2: A12. DOI: 10.1186/2194-7791-2-S1-A12 |
0.356 |
|
2014 |
Zhang H, Zhu F, Yang T, Ding L, Zhou M, Li J, Haslam SM, Dell A, Erlandsen H, Wu H. The highly conserved domain of unknown function 1792 has a distinct glycosyltransferase fold. Nature Communications. 5: 4339. PMID 25023666 DOI: 10.1038/Ncomms5339 |
0.368 |
|
2011 |
Zhu F, Erlandsen H, Ding L, Li J, Huang Y, Zhou M, Liang X, Ma J, Wu H. Structural and functional analysis of a new subfamily of glycosyltransferases required for glycosylation of serine-rich streptococcal adhesins. The Journal of Biological Chemistry. 286: 27048-57. PMID 21653318 DOI: 10.1074/Jbc.M110.208629 |
0.45 |
|
2010 |
Gurmu D, Dahlroth SL, Haas J, Nordlund P, Erlandsen H. Expression, purification, crystallization and preliminary X-ray analysis of ORF60, the small subunit (R2) of ribonucleotide reductase from Kaposi's sarcoma-associated herpesvirus (KSHV). Acta Crystallographica. Section F, Structural Biology and Crystallization Communications. 66: 734-7. PMID 20516613 DOI: 10.1107/S1744309110016052 |
0.308 |
|
2009 |
Dahlroth SL, Gurmu D, Schmitzberger F, Engman H, Haas J, Erlandsen H, Nordlund P. Crystal structure of the shutoff and exonuclease protein from the oncogenic Kaposi's sarcoma-associated herpesvirus. The Febs Journal. 276: 6636-45. PMID 19843164 DOI: 10.1111/J.1742-4658.2009.07374.X |
0.389 |
|
2009 |
Gurmu D, Lu J, Johnson KA, Nordlund P, Holmgren A, Erlandsen H. The crystal structure of the protein YhaK from Escherichia coli reveals a new subclass of redox sensitive enterobacterial bicupins. Proteins. 74: 18-31. PMID 18561187 DOI: 10.1002/Prot.22128 |
0.382 |
|
2004 |
Erlandsen H, Pey AL, Gámez A, Pérez B, Desviat LR, Aguado C, Koch R, Surendran S, Tyring S, Matalon R, Scriver CR, Ugarte M, Martínez A, Stevens RC. Correction of kinetic and stability defects by tetrahydrobiopterin in phenylketonuria patients with certain phenylalanine hydroxylase mutations. Proceedings of the National Academy of Sciences of the United States of America. 101: 16903-8. PMID 15557004 DOI: 10.1073/Pnas.0407256101 |
0.458 |
|
2004 |
Pey AL, Pérez B, Desviat LR, Martínez MA, Aguado C, Erlandsen H, Gámez A, Stevens RC, Thórólfsson M, Ugarte M, Martínez A. Mechanisms underlying responsiveness to tetrahydrobiopterin in mild phenylketonuria mutations. Human Mutation. 24: 388-99. PMID 15459954 DOI: 10.1002/Humu.20097 |
0.332 |
|
2004 |
Erlandsen H, Canaves JM, Elsliger MA, von Delft F, Brinen LS, Dai X, Deacon AM, Floyd R, Godzik A, Grittini C, Grzechnik SK, Jaroszewski L, Klock HE, Koesema E, Kovarik JS, et al. Crystal structure of an HEPN domain protein (TM0613) from Thermotoga maritima at 1.75 A resolution. Proteins. 54: 806-9. PMID 14997578 DOI: 10.1002/Prot.10631 |
0.38 |
|
2004 |
Matalon R, Koch R, Michals-Matalon K, Moseley K, Surendran S, Tyring S, Erlandsen H, Gamez A, Stevens RC, Romstad A, Møller LB, Guttler F. Biopterin responsive phenylalanine hydroxylase deficiency. Genetics in Medicine : Official Journal of the American College of Medical Genetics. 6: 27-32. PMID 14726806 DOI: 10.1097/01.Gim.0000108840.17922.A7 |
0.368 |
|
2003 |
Erlandsen H, Patch MG, Gamez A, Straub M, Stevens RC. Structural studies on phenylalanine hydroxylase and implications toward understanding and treating phenylketonuria. Pediatrics. 112: 1557-65. PMID 14654665 |
0.361 |
|
2003 |
Grynberg M, Erlandsen H, Godzik A. HEPN: a common domain in bacterial drug resistance and human neurodegenerative proteins. Trends in Biochemical Sciences. 28: 224-6. PMID 12765831 DOI: 10.1016/S0968-0004(03)00060-4 |
0.356 |
|
2003 |
Scriver CR, Hurtubise M, Konecki D, Phommarinh M, Prevost L, Erlandsen H, Stevens R, Waters PJ, Ryan S, McDonald D, Sarkissian C. PAHdb 2003: what a locus-specific knowledgebase can do. Human Mutation. 21: 333-44. PMID 12655543 DOI: 10.1002/Humu.10200 |
0.371 |
|
2002 |
Wang L, Erlandsen H, Haavik J, Knappskog PM, Stevens RC. Three-dimensional structure of human tryptophan hydroxylase and its implications for the biosynthesis of the neurotransmitters serotonin and melatonin. Biochemistry. 41: 12569-74. PMID 12379098 DOI: 10.1021/Bi026561F |
0.419 |
|
2002 |
Erlandsen H, Kim JY, Patch MG, Han A, Volner A, Abu-Omar MM, Stevens RC. Structural comparison of bacterial and human iron-dependent phenylalanine hydroxylases: similar fold, different stability and reaction rates. Journal of Molecular Biology. 320: 645-61. PMID 12096915 DOI: 10.1016/S0022-2836(02)00496-5 |
0.428 |
|
2001 |
Erlandsen H, Stevens RC. A structural hypothesis for BH4 responsiveness in patients with mild forms of hyperphenylalaninaemia and phenylketonuria. Journal of Inherited Metabolic Disease. 24: 213-30. PMID 11405341 DOI: 10.1023/A:1010371002631 |
0.429 |
|
2000 |
Erlandsen H, Abola EE, Stevens RC. Combining structural genomics and enzymology: completing the picture in metabolic pathways and enzyme active sites. Current Opinion in Structural Biology. 10: 719-30. PMID 11114510 DOI: 10.1016/S0959-440X(00)00154-8 |
0.375 |
|
2000 |
Erlandsen H, Bjørgo E, Flatmark T, Stevens RC. Crystal structure and site-specific mutagenesis of pterin-bound human phenylalanine hydroxylase. Biochemistry. 39: 2208-17. PMID 10694386 DOI: 10.1021/Bi992531+ |
0.393 |
|
1999 |
Erlandsen H, Stevens RC. The structural basis of phenylketonuria. Molecular Genetics and Metabolism. 68: 103-25. PMID 10527663 DOI: 10.1006/Mgme.1999.2922 |
0.418 |
|
1998 |
Erlandsen H, Flatmark T, Stevens RC, Hough E. Crystallographic analysis of the human phenylalanine hydroxylase catalytic domain with bound catechol inhibitors at 2.0 A resolution. Biochemistry. 37: 15638-46. PMID 9843368 DOI: 10.1021/Bi9815290 |
0.426 |
|
1998 |
Fusetti F, Erlandsen H, Flatmark T, Stevens RC. Structure of tetrameric human phenylalanine hydroxylase and its implications for phenylketonuria. The Journal of Biological Chemistry. 273: 16962-7. PMID 9642259 DOI: 10.1074/Jbc.273.27.16962 |
0.497 |
|
1997 |
Erlandsen H, Fusetti F, Martinez A, Hough E, Flatmark T, Stevens RC. Crystal structure of the catalytic domain of human phenylalanine hydroxylase reveals the structural basis for phenylketonuria. Nature Structural Biology. 4: 995-1000. PMID 9406548 DOI: 10.1038/Nsb1297-995 |
0.461 |
|
1997 |
Erlandsen H, Martinez A, Knappskog PM, Haavik J, Hough E, Flatmark T. Crystallization and preliminary diffraction analysis of a truncated homodimer of human phenylalanine hydroxylase. Febs Letters. 406: 171-4. PMID 9109411 DOI: 10.1016/S0014-5793(97)00259-7 |
0.338 |
|
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