Publications Christofer Lendel

The latest publications available at KTH Publication Data Base DiVA

[1]
H. Chaudhary et al., "Intrinsically disordered protein as carbon nanotube dispersant: How dynamic interactions lead to excellent colloidal stability," Journal of Colloid and Interface Science, vol. 556, pp. 172-179, 2019.
[3]
X. Ye et al., "Protein nanofibrils: Preparation, properties, and possible applications in industrial nanomaterials.," in Industrial Applications of Nanomaterials, : Elsevier, 2019, pp. 29-63.
[4]
L. Josefsson et al., "Structural basis for the formation of soy protein nanofibrils," RSC Advances, vol. 9, no. 11, pp. 6310-6319, 2019.
[5]
Y. Hedberg et al., "Synergistic effects of metal-induced aggregation of human serum albumin," Colloids and Surfaces B : Biointerfaces, vol. 173, pp. 751-758, 2019.
[7]
X. Ye et al., "On the role of peptide hydrolysis for fibrillation kinetics and amyloid fibril morphology," RSC Advances, vol. 8, no. 13, pp. 6915-6924, 2018.
[8]
X. Ye et al., "Protein/Protein Nanocomposite Based on Whey Protein Nanofibrils in a Whey Protein Matrix," ACS Sustainable Chemistry and Engineering, vol. 6, no. 4, pp. 5462-5469, 2018.
[9]
A. Kamada et al., "Flow-assisted assembly of nanostructured protein microfibers," Proceedings of the National Academy of Sciences of the United States of America, vol. 114, no. 6, pp. 1232-1237, 2017.
[11]
[12]
A. Kamada et al., "Assembly mechanism of nanostructured whey protein filaments," Abstracts of Papers of the American Chemical Society, vol. 252, 2016.
[13]
[14]
M. M. Rahman et al., "Binding of Human Proteins to Amyloid-beta Protofibrils," ACS Chemical Biology, vol. 10, no. 3, pp. 766-774, 2015.
[15]
Y. Cai et al., "Changes in secondary structure of alpha-synuclein during oligomerization induced by reactive aldehydes," Biochemical and Biophysical Research Communications - BBRC, vol. 464, no. 1, pp. 336-341, 2015.
[16]
C. Lendel et al., "A hexameric peptide barrel as building block of amyloid-β protofibrils.," Angewandte Chemie International Edition, vol. 53, pp. 12756-12760, 2014.
[17]
[18]
[19]
T. Härd and C. Lendel, "Inhibition of amyloid formation.," Journal of Molecular Biology, vol. 421, no. 4-5, pp. 441-65, 2012.
[20]
A. Abelein et al., "Transient small molecule interactions kinetically modulate amyloid β peptide self-assembly.," FEBS Letters, vol. 586, no. 22, pp. 3991-3995, 2012.
[21]
J. Dogan, C. Lendel and T. Härd, "NMR assignments of the free and bound-state protein components of an anti-idiotypic affibody complex," Journal of Biomolecular NMR, vol. 36, pp. (Electronic publication ahead of print Feb. 6; doi:10.1007/s10858-005-5350-8), 2006.
[22]
C. Lendel, J. Dogan and T. Härd, "Structural basis for molecular recognition in an affibody:affibody complex," Asia-Pacific Journal of Molecular Biology and Biotechnology, vol. 359, no. 5, pp. 1293-1304, 2006.
[23]
J. Dogan, C. Lendel and T. Härd, "Thermodynamics of folding and binding in an affibody:affibody complex," Journal of Molecular Biology, vol. 359, no. 5, pp. 1305-1315, 2006.
[24]
[25]
C. Lendel et al., "Biophysical characterization of ZSPA-1-A phage-display selected binder to protein A," Protein Science, vol. 13, no. 8, pp. 2078-2088, 2004.
[26]
V. Dincbas-Renqvist et al., "Thermodynamics of folding, stabilization, and binding in an engineered protein-protein complex," Journal of the American Chemical Society, vol. 126, no. 36, pp. 11220-11230, 2004.
[27]
E. Wahlberg et al., "An affibody in complex with a target protein: Structure and coupled folding.," Proceedings of the National Academy of Sciences of the United States of America, vol. 100, no. 6, pp. 3185-3190, 2003.
[28]
C. Lendel et al., "1H, 13C and 15N resonance assignments of an affibody-target complex," Journal of Biomolecular NMR, vol. 24, no. 3, pp. 271-272, 2002.

Page responsible:Kenneth Carlsson
Belongs to: Department of Chemistry
Last changed: Jun 02, 2017