Zobrazeno 1 - 10
of 109
pro vyhledávání: '"Parvesh Wadhwani"'
Autor:
Imke Rudnik-Jansen, Jie Du, Nina Karssemakers-Degen, Anna R. Tellegen, Parvesh Wadhwani, Daniele Zuncheddu, Björn P. Meij, Jens Thies, Pieter Emans, Fetullah C. Öner, George Mihov, Joao Pedro Garcia, Anne S. Ulrich, Sibylle Grad, Marianna A. Tryfonidou, Hugo van Ingen, Laura B. Creemers
Publikováno v:
Drug Delivery, Vol 31, Iss 1 (2024)
Intradiscal drug delivery is a promising strategy for treating intervertebral disk degeneration (IVDD). Local degenerative processes and intrinsically low fluid exchange are likely to influence drug retention. Understanding their connection will enab
Externí odkaz:
https://doaj.org/article/e74ff26b3ae344bf99b69a5fc7b3d7c3
Autor:
Fabian Schweigardt, Erik Strandberg, Parvesh Wadhwani, Johannes Reichert, Jochen Bürck, Haroldo L. P. Cravo, Luisa Burger, Anne S. Ulrich
Publikováno v:
Biomedicines, Vol 10, Iss 9, p 2071 (2022)
Amphipathic peptides can act as antibiotics due to membrane permeabilization. KL peptides with the repetitive sequence [Lys-Leu]n-NH2 form amphipathic β-strands in the presence of lipid bilayers. As they are known to kill bacteria in a peculiar leng
Externí odkaz:
https://doaj.org/article/d471007a46f74fb1bd185601d55a85fa
Autor:
Christian Mink, Erik Strandberg, Parvesh Wadhwani, Manuel N. Melo, Johannes Reichert, Irene Wacker, Miguel A. R. B. Castanho, Anne S. Ulrich
Publikováno v:
Frontiers in Cellular and Infection Microbiology, Vol 11 (2021)
BP100 is a short, designer-made membrane-active peptide with multiple functionalities: antimicrobial, cell-penetrating, and fusogenic. Consisting of five lysines and 6 hydrophobic residues, BP100 was shown to bind to lipid bilayers as an amphipathic
Externí odkaz:
https://doaj.org/article/de90319e98544420a3c6e113fcfc7d28
Autor:
Giorgia Manzo, Mariano A Scorciapino, Parvesh Wadhwani, Jochen Bürck, Nicola Pietro Montaldo, Manuela Pintus, Roberta Sanna, Mariano Casu, Andrea Giuliani, Giovanna Pirri, Vincenzo Luca, Anne S Ulrich, Andrea C Rinaldi
Publikováno v:
PLoS ONE, Vol 10, Iss 1, p e0116379 (2015)
SB056 is a novel semi-synthetic antimicrobial peptide with a dimeric dendrimer scaffold. Active against both Gram-negative and -positive bacteria, its mechanism has been attributed to a disruption of bacterial membranes. The branched peptide was show
Externí odkaz:
https://doaj.org/article/a6fe04b2444d41f58ed022ffe06c5f48
Autor:
Susanne Fanghänel, Parvesh Wadhwani, Erik Strandberg, Wouter P R Verdurmen, Jochen Bürck, Sebastian Ehni, Pavel K Mykhailiuk, Sergii Afonin, Dagmar Gerthsen, Igor V Komarov, Roland Brock, Anne S Ulrich
Publikováno v:
PLoS ONE, Vol 9, Iss 6, p e99653 (2014)
Structure analysis of the cell-penetrating peptide transportan 10 (TP10) revealed an exemplary range of different conformations in the membrane-bound state. The bipartite peptide (derived N-terminally from galanin and C-terminally from mastoparan) wa
Externí odkaz:
https://doaj.org/article/7f4a4fcd052149528fd741085e206de6
Autor:
Hannah G. Abernathy, Jhinuk Saha, Lisa K. Kemp, Parvesh Wadhwani, Tristan D. Clemons, Sarah E. Morgan, Vijayaraghavan Rangachari
Proteinaceous amyloids are well known for their widespread pathological roles but lately have emerged also as key components in several biological functions. The remarkable ability of amyloid fibers to form tightly packed conformations in a cross β-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ea63efd123bb6bd91fe6e9fe877fec63
https://doi.org/10.1101/2023.05.08.539858
https://doi.org/10.1101/2023.05.08.539858
Autor:
Erik Strandberg, Parvesh Wadhwani, Jochen Bürck, Patrick Anders, Christian Mink, Jonas van den Berg, Raffaele A. M. Ciriello, Manuel N. Melo, Miguel A. R. B. Castanho, Eduard Bardají, Jakob P. Ulmschneider, Anne S. Ulrich
Publikováno v:
ChemBioChem
© 2022 The Authors. ChemBioChem published by Wiley-VCH GmbH. This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is pr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9856200324c5f00efaf92d71305d562e
https://doi.org/10.1002/cbic.202200602
https://doi.org/10.1002/cbic.202200602
Autor:
Regina Leibe, Susanne Fritsch‐Decker, Florian Gussmann, Ane Marit Wagbo, Parvesh Wadhwani, Silvia Diabaté, Wolfgang Wenzel, Anne S. Ulrich, Carsten Weiss
Publikováno v:
Small
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::00fd65cae1e9bab0a5b31871f743f66f
Publikováno v:
Biophysical Journal. 122:154a-155a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f80146b86958db71c466e034f3752d45
https://doi.org/10.1016/j.bpj.2022.11.982
https://doi.org/10.1016/j.bpj.2022.11.982
Autor:
Ulrich, Fabian Schweigardt, Erik Strandberg, Parvesh Wadhwani, Johannes Reichert, Jochen Bürck, Haroldo L. P. Cravo, Luisa Burger, Anne S.
Publikováno v:
Biomedicines; Volume 10; Issue 9; Pages: 2071
Amphipathic peptides can act as antibiotics due to membrane permeabilization. KL peptides with the repetitive sequence [Lys-Leu]n-NH2 form amphipathic β-strands in the presence of lipid bilayers. As they are known to kill bacteria in a peculiar leng
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=multidiscipl::6a98776684c16a605244c20f474d34d4