Výsledky vyhledávání - "Biophysics/Protein Folding"

Multi-Scaled Explorations of Binding-Induced Folding of Intrinsically Disordered Protein Inhibitor IA3 to its Target Enzyme

Autor: Wei Han, Yong Wang, Xiakun Chu, Stephen J. Hagen, Jin Wang, Erkang Wang

Publikováno v: PLoS Computational Biology
PLoS Computational Biology, Vol 7, Iss 4, p e1001118 (2011)

Biomolecular function is realized by recognition, and increasing evidence shows that recognition is determined not only by structure but also by flexibility and dynamics. We explored a biomolecular recognition process that involves a major conformati

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8c06205a98e592b3d1fca890903ae078
http://europepmc.org/articles/PMC3072359

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Apolipoprotein E: Isoform Specific Differences in Tertiary Structure and Interaction with Amyloid-β in Human Alzheimer Brain

Autor: Brian J. Bacskai, Tadafumi Hashimoto, Anete Rozkalne, Christine A. F. von Armin, Mathew Mielke, Bradley T. Hyman, Tara L. Spires-Jones, Tammy T. Hshieh, Phillip B. Jones, Kenneth W. Adams

Publikováno v: PLoS ONE
PLoS ONE, Vol 6, Iss 1, p e14586 (2011)
Jones, P B, Adams, K W, Rozkalne, A, Spires-Jones, T L, Hshieh, T T, Hashimoto, T, von Armin, C A F, Mielke, M, Bacskai, B J & Hyman, B T 2011, ' Apolipoprotein E: isoform specific differences in tertiary structure and interaction with amyloid-β in human Alzheimer brain ', PLoS ONE, vol. 6, no. 1, pp. e14586 . https://doi.org/10.1371/journal.pone.0014586

We applied a novel application of FLIM-FRET to in situ measurement and quantification of protein interactions to explore isoform specific differences in Aβ-ApoE interaction and ApoE tertiary conformation in senile plaques in human Alzheimer brain. A

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c923337a7dcfd41ac229f0ab114a19ce
http://europepmc.org/articles/PMC3031506

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Membrane Permeabilization by Oligomeric α-Synuclein: In Search of the Mechanism

Autor: Mireille Maria Anna Elisabeth Claessens, Vinod Subramaniam, Bart D. van Rooijen

Publikováno v: PLoS ONE, 5(12). Public Library of Science
van Rooijen, B D, Claessens, M M A E & Subramaniam, V 2010, ' Membrane Permeabilization by Oligomeric α-Synuclein : In Search of the Mechanism ', PLoS ONE, vol. 5, no. 12, pp. e14292 . https://doi.org/10.1371/journal.pone.0014292
PLoS ONE, Vol 5, Iss 12, p e14292 (2010)
PLoS ONE

BACKGROUND: The question of how the aggregation of the neuronal protein α-synuclein contributes to neuronal toxicity in Parkinson's disease has been the subject of intensive research over the past decade. Recently, attention has shifted from the amy

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::11f346c4ba1c7ca8b6134d652634489a
https://research.vu.nl/en/publications/1653345f-fd80-4e66-a836-99e220cb5285

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Molecular interactions between prions as seeds and recombinant prion proteins as substrates resemble the biological interspecies barrier in vitro

Autor: Lars Luers, Detlev Riesner, Luitgard Nagel-Steger, Jürgen Weiβ, Jan Stöhr, Giannantonio Panza, Dieter Willbold, Eva Birkmann

Publikováno v: PLoS ONE, Vol 5, Iss 12, p e14283 (2010)
PLoS one 5, e14283 (2010). doi:10.1371/journal.pone.0014283
PLoS ONE

Prion diseases like Creutzfeldt-Jakob disease in humans, Scrapie in sheep or bovine spongiform encephalopathy are fatal neurodegenerative diseases, which can be of sporadic, genetic, or infectious origin. Prion diseases are transmissible between diff

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4fa5b084d643b58d5951596a465f87d0
https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/21151607/?tool=EBI

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Structure of a Burkholderia pseudomallei Trimeric Autotransporter Adhesin Head

Autor: Amir Masoudi, Wenjin Guo, Thomas E. Edwards, Stephen N. Hewitt, Isabelle Phan, David J. Leibly, Shellie H. Dieterich, Wesley C. Van Voorhis, Jan Abendroth, Bart L. Staker, Samuel I. Miller, Angela Kelley, Peter J. Myler, Mitch Brittnacher, Lance Stewart

Publikováno v: PLoS ONE
PLoS ONE, Vol 5, Iss 9 (2010)

Background Pathogenic bacteria adhere to the host cell surface using a family of outer membrane proteins called Trimeric Autotransporter Adhesins (TAAs). Although TAAs are highly divergent in sequence and domain structure, they are all conceptually c

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::622b37665a0c12e75107046b0e04f83b
http://europepmc.org/articles/PMC2942831

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FliO regulation of FliP in the formation of the Salmonella enterica flagellum

Autor: Irina V. Meshcheryakova, Clive S. Barker, Fadel A. Samatey, Alla S. Kostyukova

Publikováno v: PLoS Genetics, Vol 6, Iss 9, p e1001143 (2010)
PLoS Genetics

The type III secretion system of the Salmonella flagellum consists of 6 integral membrane proteins: FlhA, FlhB, FliO, FliP, FliQ, and FliR. However, in some other type III secretion systems, a homologue of FliO is apparently absent, suggesting it has

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::65cf905275133948ef5606cd4b16daca
http://europepmc.org/articles/PMC2947984?pdf=render

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Amyloid-Like Aggregates of the Yeast Prion Protein Ure2 Enter Vertebrate Cells by Specific Endocytotic Pathways and Induce Apoptosis

Autor: Zai-Rong Zhang, Antony P. Jackson, Chen Zhang, Shun Yu, Yan Han, Sarah Perrett, Rongqiao He

Publikováno v: PLoS ONE
PLoS ONE, Vol 5, Iss 9, p e12489 (2010)

BACKGROUND: A number of amyloid diseases involve deposition of extracellular protein aggregates, which are implicated in mechanisms of cell damage and death. However, the mechanisms involved remain poorly understood. METHODOLOGY/PRINCIPAL FINDINGS: H

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9c04880af1ac436cd63e0a8f4a2a0235
http://europepmc.org/articles/PMC2932714

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Reduction in structural disorder and functional complexity in the thermal adaptation of prokaryotes

Autor: Peter Tompa, Prasad Burra, Lajos Kalmar

Publikováno v: PLoS ONE, Vol 5, Iss 8, p e12069 (2010)
PLoS ONE

Genomic correlates of evolutionary adaptation to very low or very high optimal growth temperature (OGT) values have been the subject of many studies. Whereas these provided a protein-structural rationale of the activity and stability of globular prot

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5411d5ce033fdb6709744950c48fef1f
https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/20711457/pdf/?tool=EBI

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Symmetric key structural residues in symmetric proteins with beta-trefoil fold

Autor: Yanzhao Huang, Jianhui Feng, Yi Xiao, Mingfeng Li

Publikováno v: PLoS ONE
PLoS ONE, Vol 5, Iss 11, p e14138 (2010)

To understand how symmetric structures of many proteins are formed from asymmetric sequences, the proteins with two repeated beta-trefoil domains in Plant Cytotoxin B-chain family and all presently known beta-trefoil proteins are analyzed by structur

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::04e45a80ea1a176153d4a7279a24d083
https://pubmed.ncbi.nlm.nih.gov/21152439

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The Energy Landscape, Folding Pathways and the Kinetics of a Knotted Protein

Autor: Peter G. Wolynes, Michael C. Prentiss, David J. Wales

Publikováno v: PLoS Computational Biology, Vol 6, p e1000835 (2010)
PLoS Computational Biology

The folding pathway and rate coefficients of the folding of a knotted protein are calculated for a potential energy function with minimal energetic frustration. A kinetic transition network is constructed using the discrete path sampling approach, an

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::08e26851cdcc8c1d587848f7c88cd1a5
http://arxiv.org/abs/1007.0300

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