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Best matches for Wälti MA[au]:

Atomic-resolution structure of a disease-relevant Aβ(1-42) amyloid fibril. Wälti MA et al. Proc Natl Acad Sci U S A. (2016)

Binding of Polythiophenes to Amyloids: Structural Mapping of the Pharmacophore. Schütz AK et al. ACS Chem Neurosci. (2018)

Quenched hydrogen-deuterium exchange NMR of a disease-relevant Aβ(1-42) amyloid polymorph. Wälti MA et al. PLoS One. (2017)

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Items: 21


Probing the mechanism of inhibition of amyloid-β(1-42)-induced neurotoxicity by the chaperonin GroEL.

Wälti MA, Steiner J, Meng F, Chung HS, Louis JM, Ghirlando R, Tugarinov V, Nath A, Clore GM.

Proc Natl Acad Sci U S A. 2018 Dec 18;115(51):E11924-E11932. doi: 10.1073/pnas.1817477115. Epub 2018 Dec 3.


Extensive Sampling of the Cavity of the GroEL Nanomachine by Protein Substrates Probed by Paramagnetic Relaxation Enhancement.

Wälti MA, Libich DS, Clore GM.

J Phys Chem Lett. 2018 Jun 21;9(12):3368-3371. doi: 10.1021/acs.jpclett.8b01586. Epub 2018 Jun 7.


Binding of Polythiophenes to Amyloids: Structural Mapping of the Pharmacophore.

Schütz AK, Hornemann S, Wälti MA, Greuter L, Tiberi C, Cadalbert R, Gantner M, Riek R, Hammarström P, Nilsson KPR, Böckmann A, Aguzzi A, Meier BH.

ACS Chem Neurosci. 2018 Mar 21;9(3):475-481. doi: 10.1021/acschemneuro.7b00397. Epub 2017 Dec 4.


Chaperonin GroEL accelerates protofibril formation and decorates fibrils of the Het-s prion protein.

Wälti MA, Schmidt T, Murray DT, Wang H, Hinshaw JE, Clore GM.

Proc Natl Acad Sci U S A. 2017 Aug 22;114(34):9104-9109. doi: 10.1073/pnas.1711645114. Epub 2017 Aug 7.


Fast NMR-Based Determination of the 3D Structure of the Binding Site of Protein-Ligand Complexes with Weak Affinity Binders.

Wälti MA, Riek R, Orts J.

Angew Chem Int Ed Engl. 2017 May 2;56(19):5208-5211. doi: 10.1002/anie.201612304. Epub 2017 Apr 7.


Quenched hydrogen-deuterium exchange NMR of a disease-relevant Aβ(1-42) amyloid polymorph.

Wälti MA, Orts J, Riek R.

PLoS One. 2017 Mar 20;12(3):e0172862. doi: 10.1371/journal.pone.0172862. eCollection 2017.


Long Distance Measurements up to 160 Å in the GroEL Tetradecamer Using Q-Band DEER EPR Spectroscopy.

Schmidt T, Wälti MA, Baber JL, Hustedt EJ, Clore GM.

Angew Chem Int Ed Engl. 2016 Dec 19;55(51):15905-15909. doi: 10.1002/anie.201609617. Epub 2016 Nov 17.


Atomic-resolution structure of a disease-relevant Aβ(1-42) amyloid fibril.

Wälti MA, Ravotti F, Arai H, Glabe CG, Wall JS, Böckmann A, Güntert P, Meier BH, Riek R.

Proc Natl Acad Sci U S A. 2016 Aug 23;113(34):E4976-84. doi: 10.1073/pnas.1600749113. Epub 2016 Jul 28.


Solid-state NMR sequential assignment of an Amyloid-β(1-42) fibril polymorph.

Ravotti F, Wälti MA, Güntert P, Riek R, Böckmann A, Meier BH.

Biomol NMR Assign. 2016 Oct;10(2):269-76. doi: 10.1007/s12104-016-9682-y. Epub 2016 May 10.


NMR-Based Determination of the 3D Structure of the Ligand-Protein Interaction Site without Protein Resonance Assignment.

Orts J, Wälti MA, Marsh M, Vera L, Gossert AD, Güntert P, Riek R.

J Am Chem Soc. 2016 Apr 6;138(13):4393-400. doi: 10.1021/jacs.5b12391. Epub 2016 Mar 23.


Solution NMR studies of recombinant Aβ(1-42): from the presence of a micellar entity to residual β-sheet structure in the soluble species.

Wälti MA, Orts J, Vögeli B, Campioni S, Riek R.

Chembiochem. 2015 Mar 2;16(4):659-69. doi: 10.1002/cbic.201402595. Epub 2015 Feb 11.


Contribution of specific residues of the β-solenoid fold to HET-s prion function, amyloid structure and stability.

Daskalov A, Gantner M, Wälti MA, Schmidlin T, Chi CN, Wasmer C, Schütz A, Ceschin J, Clavé C, Cescau S, Meier B, Riek R, Saupe SJ.

PLoS Pathog. 2014 Jun 12;10(6):e1004158. doi: 10.1371/journal.ppat.1004158. eCollection 2014 Jun.


Towards a true protein movie: a perspective on the potential impact of the ensemble-based structure determination using exact NOEs.

Vögeli B, Orts J, Strotz D, Chi C, Minges M, Wälti MA, Güntert P, Riek R.

J Magn Reson. 2014 Apr;241:53-9. doi: 10.1016/j.jmr.2013.11.016. Review.


Plasticity of the β-trefoil protein fold in the recognition and control of invertebrate predators and parasites by a fungal defence system.

Schubert M, Bleuler-Martinez S, Butschi A, Wälti MA, Egloff P, Stutz K, Yan S, Collot M, Mallet JM, Wilson IB, Hengartner MO, Aebi M, Allain FH, Künzler M.

PLoS Pathog. 2012;8(5):e1002706. doi: 10.1371/journal.ppat.1002706. Epub 2012 May 17. Erratum in: PLoS Pathog. 2012 Aug;8(8). doi: 10.1371/annotation/088ea07b-d578-4586-9707-160143d4f1be. PLoS Pathog. 2012 Aug;8(8). doi: 10.1371/annotation/ed5d46f6-3442-4a89-a505-78befd507436. Collot, Mayeul [added]; Mallet, Jean-Maurice [added].


A lectin-mediated resistance of higher fungi against predators and parasites.

Bleuler-Martínez S, Butschi A, Garbani M, Wälti MA, Wohlschlager T, Potthoff E, Sabotiĉ J, Pohleven J, Lüthy P, Hengartner MO, Aebi M, Künzler M.

Mol Ecol. 2011 Jul;20(14):3056-70. doi: 10.1111/j.1365-294X.2011.05093.x. Epub 2011 Apr 12.


The autoinducer synthase LqsA and putative sensor kinase LqsS regulate phagocyte interactions, extracellular filaments and a genomic island of Legionella pneumophila.

Tiaden A, Spirig T, Sahr T, Wälti MA, Boucke K, Buchrieser C, Hilbi H.

Environ Microbiol. 2010 May;12(5):1243-59. doi: 10.1111/j.1462-2920.2010.02167.x. Epub 2010 Feb 9.


Caenorhabditis elegans N-glycan core beta-galactoside confers sensitivity towards nematotoxic fungal galectin CGL2.

Butschi A, Titz A, Wälti MA, Olieric V, Paschinger K, Nöbauer K, Guo X, Seeberger PH, Wilson IB, Aebi M, Hengartner MO, Künzler M.

PLoS Pathog. 2010 Jan;6(1):e1000717. doi: 10.1371/journal.ppat.1000717. Epub 2010 Jan 8.


Structural basis for chitotetraose coordination by CGL3, a novel galectin-related protein from Coprinopsis cinerea.

Wälti MA, Walser PJ, Thore S, Grünler A, Bednar M, Künzler M, Aebi M.

J Mol Biol. 2008 May 23;379(1):146-59. doi: 10.1016/j.jmb.2008.03.062. Epub 2008 Apr 3.


Crystal structure of the putative carbohydrate recognition domain of human galectin-related protein.

Wälti MA, Thore S, Aebi M, Künzler M.

Proteins. 2008 Aug;72(2):804-8. doi: 10.1002/prot.22078. No abstract available.


Targeted gene silencing in the model mushroom Coprinopsis cinerea (Coprinus cinereus) by expression of homologous hairpin RNAs.

Wälti MA, Villalba C, Buser RM, Grünler A, Aebi M, Künzler M.

Eukaryot Cell. 2006 Apr;5(4):732-44.

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