Publication

SERF Protein Is a Direct Modifier of Amyloid Fiber Assembly

Falsone, S. F., Meyer, N. H., Schrank, E., Leitinger, G., Pham, C. L. L., Fodero-Tavoletti, M. T., Holmberg, M., Dulle, M., Scicluna, B., Gesslbauer, B., Rueckert, H-M., Wagner, G. E., Merle, D. A., Nollen, E. A., Kungl, A. J., Hill, A. F., Cappai, R. & Zangger, K., Aug-2012, In : Cell reports. 2, 2, p. 358-371 14 p.

Research output: Contribution to journalArticleAcademicpeer-review

APA

Falsone, S. F., Meyer, N. H., Schrank, E., Leitinger, G., Pham, C. L. L., Fodero-Tavoletti, M. T., ... Zangger, K. (2012). SERF Protein Is a Direct Modifier of Amyloid Fiber Assembly. Cell reports, 2(2), 358-371. https://doi.org/10.1016/j.celrep.2012.06.012

Author

Falsone, S. Fabio ; Meyer, N. Helge ; Schrank, Evelyne ; Leitinger, Gerd ; Pham, Chi L. L. ; Fodero-Tavoletti, Michelle T. ; Holmberg, Mats ; Dulle, Martin ; Scicluna, Benjamin ; Gesslbauer, Bernd ; Rueckert, Hanna-Marie ; Wagner, Gabriel E. ; Merle, David A. ; Nollen, Ellen A. ; Kungl, Andreas J. ; Hill, Andrew F. ; Cappai, Roberto ; Zangger, Klaus. / SERF Protein Is a Direct Modifier of Amyloid Fiber Assembly. In: Cell reports. 2012 ; Vol. 2, No. 2. pp. 358-371.

Harvard

Falsone, SF, Meyer, NH, Schrank, E, Leitinger, G, Pham, CLL, Fodero-Tavoletti, MT, Holmberg, M, Dulle, M, Scicluna, B, Gesslbauer, B, Rueckert, H-M, Wagner, GE, Merle, DA, Nollen, EA, Kungl, AJ, Hill, AF, Cappai, R & Zangger, K 2012, 'SERF Protein Is a Direct Modifier of Amyloid Fiber Assembly', Cell reports, vol. 2, no. 2, pp. 358-371. https://doi.org/10.1016/j.celrep.2012.06.012

Standard

SERF Protein Is a Direct Modifier of Amyloid Fiber Assembly. / Falsone, S. Fabio; Meyer, N. Helge; Schrank, Evelyne; Leitinger, Gerd; Pham, Chi L. L.; Fodero-Tavoletti, Michelle T.; Holmberg, Mats; Dulle, Martin; Scicluna, Benjamin; Gesslbauer, Bernd; Rueckert, Hanna-Marie; Wagner, Gabriel E.; Merle, David A.; Nollen, Ellen A.; Kungl, Andreas J.; Hill, Andrew F.; Cappai, Roberto; Zangger, Klaus.

In: Cell reports, Vol. 2, No. 2, 08.2012, p. 358-371.

Research output: Contribution to journalArticleAcademicpeer-review

Vancouver

Falsone SF, Meyer NH, Schrank E, Leitinger G, Pham CLL, Fodero-Tavoletti MT et al. SERF Protein Is a Direct Modifier of Amyloid Fiber Assembly. Cell reports. 2012 Aug;2(2):358-371. https://doi.org/10.1016/j.celrep.2012.06.012


BibTeX

@article{ef21c65dbdb34e2482967bc4ee694149,
title = "SERF Protein Is a Direct Modifier of Amyloid Fiber Assembly",
abstract = "The inherent cytotoxicity of aberrantly folded protein aggregates contributes substantially to the pathogenesis of amyloid diseases. It was recently shown that a class of evolutionary conserved proteins, called MOAG-4/SERF, profoundly alter amyloid toxicity via an autonomous but yet unexplained mode. We show that the biological function of human SERF1a originates from its atypical ability to specifically distinguish between amyloid and nonamyloid aggregation. This inherently unstructured protein directly affected the aggregation kinetics of a broad range of amyloidogenic proteins in vitro, while being inactive against nonamyloid aggregation. A representative biophysical analysis of the SERF1a:alpha-synuclein (aSyn) complex revealed that the amyloid-promoting activity resulted from an early and transient interaction, which was sufficient to provoke a massive increase of soluble aSyn amyloid nucleation templates. Therefore, the autonomous amyloid-modifying activity of SERF1a observed in living organisms relies on a direct and dedicated manipulation of the early stages in the amyloid aggregation pathway.",
keywords = "CIRCULAR-DICHROISM SPECTROSCOPY, ALPHA-SYNUCLEIN AGGREGATION, PARKINSONS-DISEASE, FIBRIL FORMATION, IN-VITRO, OLIGOMERS, PATHWAY, NMR, MECHANISMS, DOPAMINE",
author = "Falsone, {S. Fabio} and Meyer, {N. Helge} and Evelyne Schrank and Gerd Leitinger and Pham, {Chi L. L.} and Fodero-Tavoletti, {Michelle T.} and Mats Holmberg and Martin Dulle and Benjamin Scicluna and Bernd Gesslbauer and Hanna-Marie Rueckert and Wagner, {Gabriel E.} and Merle, {David A.} and Nollen, {Ellen A.} and Kungl, {Andreas J.} and Hill, {Andrew F.} and Roberto Cappai and Klaus Zangger",
year = "2012",
month = "8",
doi = "10.1016/j.celrep.2012.06.012",
language = "English",
volume = "2",
pages = "358--371",
journal = "Cell reports",
issn = "2211-1247",
publisher = "CELL PRESS",
number = "2",

}

RIS

TY - JOUR

T1 - SERF Protein Is a Direct Modifier of Amyloid Fiber Assembly

AU - Falsone, S. Fabio

AU - Meyer, N. Helge

AU - Schrank, Evelyne

AU - Leitinger, Gerd

AU - Pham, Chi L. L.

AU - Fodero-Tavoletti, Michelle T.

AU - Holmberg, Mats

AU - Dulle, Martin

AU - Scicluna, Benjamin

AU - Gesslbauer, Bernd

AU - Rueckert, Hanna-Marie

AU - Wagner, Gabriel E.

AU - Merle, David A.

AU - Nollen, Ellen A.

AU - Kungl, Andreas J.

AU - Hill, Andrew F.

AU - Cappai, Roberto

AU - Zangger, Klaus

PY - 2012/8

Y1 - 2012/8

N2 - The inherent cytotoxicity of aberrantly folded protein aggregates contributes substantially to the pathogenesis of amyloid diseases. It was recently shown that a class of evolutionary conserved proteins, called MOAG-4/SERF, profoundly alter amyloid toxicity via an autonomous but yet unexplained mode. We show that the biological function of human SERF1a originates from its atypical ability to specifically distinguish between amyloid and nonamyloid aggregation. This inherently unstructured protein directly affected the aggregation kinetics of a broad range of amyloidogenic proteins in vitro, while being inactive against nonamyloid aggregation. A representative biophysical analysis of the SERF1a:alpha-synuclein (aSyn) complex revealed that the amyloid-promoting activity resulted from an early and transient interaction, which was sufficient to provoke a massive increase of soluble aSyn amyloid nucleation templates. Therefore, the autonomous amyloid-modifying activity of SERF1a observed in living organisms relies on a direct and dedicated manipulation of the early stages in the amyloid aggregation pathway.

AB - The inherent cytotoxicity of aberrantly folded protein aggregates contributes substantially to the pathogenesis of amyloid diseases. It was recently shown that a class of evolutionary conserved proteins, called MOAG-4/SERF, profoundly alter amyloid toxicity via an autonomous but yet unexplained mode. We show that the biological function of human SERF1a originates from its atypical ability to specifically distinguish between amyloid and nonamyloid aggregation. This inherently unstructured protein directly affected the aggregation kinetics of a broad range of amyloidogenic proteins in vitro, while being inactive against nonamyloid aggregation. A representative biophysical analysis of the SERF1a:alpha-synuclein (aSyn) complex revealed that the amyloid-promoting activity resulted from an early and transient interaction, which was sufficient to provoke a massive increase of soluble aSyn amyloid nucleation templates. Therefore, the autonomous amyloid-modifying activity of SERF1a observed in living organisms relies on a direct and dedicated manipulation of the early stages in the amyloid aggregation pathway.

KW - CIRCULAR-DICHROISM SPECTROSCOPY

KW - ALPHA-SYNUCLEIN AGGREGATION

KW - PARKINSONS-DISEASE

KW - FIBRIL FORMATION

KW - IN-VITRO

KW - OLIGOMERS

KW - PATHWAY

KW - NMR

KW - MECHANISMS

KW - DOPAMINE

U2 - 10.1016/j.celrep.2012.06.012

DO - 10.1016/j.celrep.2012.06.012

M3 - Article

C2 - 22854022

VL - 2

SP - 358

EP - 371

JO - Cell reports

JF - Cell reports

SN - 2211-1247

IS - 2

ER -

ID: 5690736