Lindorff-Larsen K - Search Results

1

Insight into Calcium-Binding Motifs of Intrinsically Disordered Proteins.

Newcombe EA, Fernandes CB, Lundsgaard JE, Brakti I, Lindorff-Larsen K, Langkilde AE, Skriver K, Kragelund BB. Newcombe EA, et al. Biomolecules. 2021 Aug 9;11(8):1173. doi: 10.3390/biom11081173. Biomolecules. 2021. PMID: 34439840 Free PMC article.

2

A Two-step Protein Quality Control Pathway for a Misfolded DJ-1 Variant in Fission Yeast.

Mathiassen SG, Larsen IB, Poulsen EG, Madsen CT, Papaleo E, Lindorff-Larsen K, Kragelund BB, Nielsen ML, Kriegenburg F, Hartmann-Petersen R. Mathiassen SG, et al. J Biol Chem. 2015 Aug 21;290(34):21141-21153. doi: 10.1074/jbc.M115.662312. Epub 2015 Jul 7. J Biol Chem. 2015. PMID: 26152728 Free PMC article.

3

Exploiting hydrophobicity for efficient production of transmembrane helices for structure determination by NMR spectroscopy.

Bugge K, Steinocher H, Brooks AJ, Lindorff-Larsen K, Kragelund BB. Bugge K, et al. Anal Chem. 2015 Sep 15;87(18):9126-31. doi: 10.1021/acs.analchem.5b02365. Epub 2015 Sep 2. Anal Chem. 2015. PMID: 26309151

4

A combined computational and structural model of the full-length human prolactin receptor.

Bugge K, Papaleo E, Haxholm GW, Hopper JT, Robinson CV, Olsen JG, Lindorff-Larsen K, Kragelund BB. Bugge K, et al. Nat Commun. 2016 May 13;7:11578. doi: 10.1038/ncomms11578. Nat Commun. 2016. PMID: 27174498 Free PMC article.

5

Understanding single-pass transmembrane receptor signaling from a structural viewpoint-what are we missing?

Bugge K, Lindorff-Larsen K, Kragelund BB. Bugge K, et al. FEBS J. 2016 Dec;283(24):4424-4451. doi: 10.1111/febs.13793. Epub 2016 Jul 18. FEBS J. 2016. PMID: 27350538 Free article. Review.

6

A phosphorylation-motif for tuneable helix stabilisation in intrinsically disordered proteins - Lessons from the sodium proton exchanger 1 (NHE1).

Hendus-Altenburger R, Lambrughi M, Terkelsen T, Pedersen SF, Papaleo E, Lindorff-Larsen K, Kragelund BB. Hendus-Altenburger R, et al. Cell Signal. 2017 Sep;37:40-51. doi: 10.1016/j.cellsig.2017.05.015. Epub 2017 May 26. Cell Signal. 2017. PMID: 28554535 Free article.

7

An Efficient Method for Estimating the Hydrodynamic Radius of Disordered Protein Conformations.

Nygaard M, Kragelund BB, Papaleo E, Lindorff-Larsen K. Nygaard M, et al. Biophys J. 2017 Aug 8;113(3):550-557. doi: 10.1016/j.bpj.2017.06.042. Biophys J. 2017. PMID: 28793210 Free PMC article.

8

Role of protein dynamics in transmembrane receptor signalling.

Wang Y, Bugge K, Kragelund BB, Lindorff-Larsen K. Wang Y, et al. Curr Opin Struct Biol. 2018 Feb;48:74-82. doi: 10.1016/j.sbi.2017.10.017. Epub 2017 Nov 11. Curr Opin Struct Biol. 2018. PMID: 29136528 Review.

9

On the Calculation of SAXS Profiles of Folded and Intrinsically Disordered Proteins from Computer Simulations.

Henriques J, Arleth L, Lindorff-Larsen K, Skepö M. Henriques J, et al. J Mol Biol. 2018 Aug 3;430(16):2521-2539. doi: 10.1016/j.jmb.2018.03.002. Epub 2018 Mar 14. J Mol Biol. 2018. PMID: 29548755

10

Computing, Analyzing, and Comparing the Radius of Gyration and Hydrodynamic Radius in Conformational Ensembles of Intrinsically Disordered Proteins.

Ahmed MC, Crehuet R, Lindorff-Larsen K. Ahmed MC, et al. Methods Mol Biol. 2020;2141:429-445. doi: 10.1007/978-1-0716-0524-0_21. Methods Mol Biol. 2020. PMID: 32696370

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