Interdisciplinary Nanoscience Center

Aarhus University Seal / Aarhus Universitets segl
You are here: » Daniel Otzen » Research outputs » Polymorphic Fibrillation of the Destabilized Fourth Fasci...

About

Daniel Otzen

Polymorphic Fibrillation of the Destabilized Fourth Fasciclin-1 Domain Mutant A546T of the Transforming Growth Factor-β-induced Protein (TGFBIp) Occurs through Multiple Pathways with Different Oligomeric Intermediates

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review

Standard

Polymorphic Fibrillation of the Destabilized Fourth Fasciclin-1 Domain Mutant A546T of the Transforming Growth Factor-β-induced Protein (TGFBIp) Occurs through Multiple Pathways with Different Oligomeric Intermediates. / Andreasen, Maria; Nielsen, Søren Bang; Runager, Kasper; Christiansen, Gunna; Nielsen, Niels Christian; Enghild, Jan J; Otzen, Daniel.

In: Journal of Biological Chemistry, Vol. 287, No. 41, 05.10.2012, p. 34730-34742.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review

Harvard

Andreasen, M, Nielsen, SB, Runager, K, Christiansen, G, Nielsen, NC, Enghild, JJ & Otzen, D 2012, 'Polymorphic Fibrillation of the Destabilized Fourth Fasciclin-1 Domain Mutant A546T of the Transforming Growth Factor-β-induced Protein (TGFBIp) Occurs through Multiple Pathways with Different Oligomeric Intermediates', Journal of Biological Chemistry, vol. 287, no. 41, pp. 34730-34742. https://doi.org/10.1074/jbc.M112.379552

APA

Andreasen, M., Nielsen, S. B., Runager, K., Christiansen, G., Nielsen, N. C., Enghild, J. J., & Otzen, D. (2012). Polymorphic Fibrillation of the Destabilized Fourth Fasciclin-1 Domain Mutant A546T of the Transforming Growth Factor-β-induced Protein (TGFBIp) Occurs through Multiple Pathways with Different Oligomeric Intermediates. Journal of Biological Chemistry, 287(41), 34730-34742. https://doi.org/10.1074/jbc.M112.379552

CBE

Andreasen M, Nielsen SB, Runager K, Christiansen G, Nielsen NC, Enghild JJ, Otzen D. 2012. Polymorphic Fibrillation of the Destabilized Fourth Fasciclin-1 Domain Mutant A546T of the Transforming Growth Factor-β-induced Protein (TGFBIp) Occurs through Multiple Pathways with Different Oligomeric Intermediates. Journal of Biological Chemistry. 287(41):34730-34742. https://doi.org/10.1074/jbc.M112.379552

MLA

Andreasen, Maria et al. "Polymorphic Fibrillation of the Destabilized Fourth Fasciclin-1 Domain Mutant A546T of the Transforming Growth Factor-β-induced Protein (TGFBIp) Occurs through Multiple Pathways with Different Oligomeric Intermediates". Journal of Biological Chemistry. 2012, 287(41). 34730-34742. https://doi.org/10.1074/jbc.M112.379552

Vancouver

Andreasen M, Nielsen SB, Runager K, Christiansen G, Nielsen NC, Enghild JJ et al. Polymorphic Fibrillation of the Destabilized Fourth Fasciclin-1 Domain Mutant A546T of the Transforming Growth Factor-β-induced Protein (TGFBIp) Occurs through Multiple Pathways with Different Oligomeric Intermediates. Journal of Biological Chemistry. 2012 Oct 5;287(41):34730-34742. https://doi.org/10.1074/jbc.M112.379552

Author

Andreasen, Maria ; Nielsen, Søren Bang ; Runager, Kasper ; Christiansen, Gunna ; Nielsen, Niels Christian ; Enghild, Jan J ; Otzen, Daniel. / Polymorphic Fibrillation of the Destabilized Fourth Fasciclin-1 Domain Mutant A546T of the Transforming Growth Factor-β-induced Protein (TGFBIp) Occurs through Multiple Pathways with Different Oligomeric Intermediates. In: Journal of Biological Chemistry. 2012 ; Vol. 287, No. 41. pp. 34730-34742.

Bibtex

@article{d59486ba84e34cc5ba73f91183d18cd6,
title = "Polymorphic Fibrillation of the Destabilized Fourth Fasciclin-1 Domain Mutant A546T of the Transforming Growth Factor-β-induced Protein (TGFBIp) Occurs through Multiple Pathways with Different Oligomeric Intermediates",
abstract = "Mutations in the transforming growth factor β induced protein (TGFBIp) are linked to the development of corneal dystrophies, in which abnormal protein deposition in the cornea leads to a loss of corneal transparency and ultimately blindness. Different mutations give rise to phenotypically distinct corneal dystrophies. Most mutations are located in the 4th fasciclin-1 domain (FAS1-4). The amino acid substitution A546T in the FAS1-4 domain is linked to the development of lattice corneal dystrophy with amyloid deposits in.",
author = "Maria Andreasen and Nielsen, {S{\o}ren Bang} and Kasper Runager and Gunna Christiansen and Nielsen, {Niels Christian} and Enghild, {Jan J} and Daniel Otzen",
year = "2012",
month = oct,
day = "5",
doi = "10.1074/jbc.M112.379552",
language = "English",
volume = "287",
pages = "34730--34742",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology, Inc.",
number = "41",

}

RIS

TY - JOUR

T1 - Polymorphic Fibrillation of the Destabilized Fourth Fasciclin-1 Domain Mutant A546T of the Transforming Growth Factor-β-induced Protein (TGFBIp) Occurs through Multiple Pathways with Different Oligomeric Intermediates

AU - Andreasen, Maria

AU - Nielsen, Søren Bang

AU - Runager, Kasper

AU - Christiansen, Gunna

AU - Nielsen, Niels Christian

AU - Enghild, Jan J

AU - Otzen, Daniel

PY - 2012/10/5

Y1 - 2012/10/5

N2 - Mutations in the transforming growth factor β induced protein (TGFBIp) are linked to the development of corneal dystrophies, in which abnormal protein deposition in the cornea leads to a loss of corneal transparency and ultimately blindness. Different mutations give rise to phenotypically distinct corneal dystrophies. Most mutations are located in the 4th fasciclin-1 domain (FAS1-4). The amino acid substitution A546T in the FAS1-4 domain is linked to the development of lattice corneal dystrophy with amyloid deposits in.

AB - Mutations in the transforming growth factor β induced protein (TGFBIp) are linked to the development of corneal dystrophies, in which abnormal protein deposition in the cornea leads to a loss of corneal transparency and ultimately blindness. Different mutations give rise to phenotypically distinct corneal dystrophies. Most mutations are located in the 4th fasciclin-1 domain (FAS1-4). The amino acid substitution A546T in the FAS1-4 domain is linked to the development of lattice corneal dystrophy with amyloid deposits in.

U2 - 10.1074/jbc.M112.379552

DO - 10.1074/jbc.M112.379552

M3 - Journal article

C2 - 22893702

VL - 287

SP - 34730

EP - 34742

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 41

ER -