In situ, Reversible Gating of a Mechanosensitive Ion Channel through Protein-Lipid Interactions

Autor: Anna Dimitrova, Martin Walko, Maryam Hashemi Shabestari, Pravin Kumar, Martina Huber, Armagan Kocer

Publikováno v: Frontiers in Physiology, Vol 7 (2016)

Understanding the functioning of ion channels, as well as utilizing their properties for biochemical applications requires control over channel activity. Herein we report a reversible control over the functioning of a mechanosensitive ion channel by

Externí odkaz: https://doaj.org/article/74a6d26dbe644475a4091808e2d63fe1

Acetylation and phosphorylation of human TFAM regulate TFAM-DNA interactions via contrasting mechanisms

Autor: Kees-Karel H. Taris, Graeme A. King, Wouter H. Roos, Kamalendra Singh, Maryam Hashemi Shabestari, Ashutosh K. Pandey, J. Thilagavathi, Dmitry Temiakov, Carolyn K. Suzuki, Sundararajan Venkatesh, Gijs J.L. Wuite, Rama K. Koppisetti

Publikováno v: Nucleic Acids Research, 46(7), 3633-3642. Oxford University Press
Shabestari, M H, King, G A, Taris, K-K H, Pandey, A K, Venkatesh, S, Thilagavathi, J, Singh, K, Koppisetti, R K, Temiakov, D, Roos, W H, Suzuki, C K & Wuite, G J L 2018, ' Acetylation and phosphorylation of human TFAM regulate TFAM-DNA interactions via contrasting mechanisms ', Nucleic Acids Research, vol. 46, no. 7, pp. 3633-3642 . https://doi.org/10.1093/nar/gky204
Nucleic Acids Research

Mitochondrial transcription factor A (TFAM) is essential for the maintenance, expression and transmission of mitochondrial DNA (mtDNA). However, mechanisms for the post-translational regulation of TFAM are poorly understood. Here, we show that TFAM i

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::16ed721ba6395e64fdeebf694a3d29e3
https://research.rug.nl/en/publications/4f281a9e-c8dd-4be1-81c0-d455d8deebec

Conformation and EPR characterization of rigid, 310-helical peptides with TOAC spin labels: Models for short distances

Autor: Alessandro Moretto, Claudio Toniolo, Maryam Hashemi Shabestari, Martin van Son, Martina Huber, Marco Crisma

Publikováno v: Biopolymers. 102:244-251

For 3D-structure determination in biophysical systems EPR is rapidly gaining ground. Proteins labeled specifically with two nitroxide spin labels can be prepared, and several EPR methods are available for distance determination, which makes it possib

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::575c2c5106c63f38b1361247e3ba6e25
https://doi.org/10.1002/bip.22467

The Aggregation Potential of the 1-15-and 1-16-Fragments of the Amyloid beta Peptide and Their Influence on the Aggregation of A beta 40

Autor: T. Plug, Martina Huber, J. C. M. Meijers, Nico J. Meeuwenoord, Dmitri V. Filippov, M. M. Motazacker, Maryam Hashemi Shabestari

Publikováno v: Applied magnetic resonance, 44(10), 1167-1179. Springer Wien

The aggregation of amyloid beta (A beta) peptide is important in Alzheimer's disease. Shorter A beta fragments may reduce A beta's cytotoxicity and are used in diagnostics. The aggregation of A beta 16 is controversial; Liu et al. (J. Neurosci. Res.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::70a41f8420b00ce5015769692d2563a0
https://doi.org/10.1007/s00723-013-0469-3

Mechanical Unfolding of an Autotransporter Passenger Protein Reveals the Secretion Starting Point and Processive Transport Intermediates

Autor: Peter van Ulsen, Wouter H. Roos, Marian Baclayon, Timo Verzijden, Maryam Hashemi Shabestari, Halima Mouhib, Sanne Abeln, Gijs J.L. Wuite

Publikováno v: ACS Nano, 10(6), 5710-5719. American Chemical Society
Europe PubMed Central
Baclayon, M, van Ulsen, P, Mouhib, H, Hashemi Shabestari, M, Verzijden, T, Abeln, S, Roos, W H & Wuite, G J L 2016, ' Mechanical Unfolding of an Autotransporter Passenger Protein Reveals the Secretion Starting Point and Processive Transport Intermediates ', ACS Nano, vol. 10, no. 6, pp. 5710-5719 . https://doi.org/10.1021/acsnano.5b07072
Acs Nano, 10(6), 5710-5719. AMER CHEMICAL SOC

The backbone of secreted autotransporter passenger proteins generally attains a stable β-helical structure. The secretion of passengers across the outer membrane was proposed to be driven by sequential folding of this structure at the cell surface.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6a8b2387c055265b09e092ab2d89783a
https://research.vu.nl/en/publications/cb8be87b-3c02-4a3b-b5d6-fcda68c9386a