Zobrazeno 1 - 10
of 66
pro vyhledávání: '"Karthikeyan Annamalai"'
Autor:
Desiree Schütz, Clarissa Read, Rüdiger Groß, Annika Röcker, Sascha Rode, Karthikeyan Annamalai, Marcus Fändrich, Jan Münch
Publikováno v:
ACS Omega, Vol 6, Iss 11, Pp 7731-7738 (2021)
Externí odkaz:
https://doaj.org/article/cb26c81941e6490a9a3a3cf6ab5f3ef2
Autor:
Lynn Radamaker, Yin-Hsi Lin, Karthikeyan Annamalai, Stefanie Huhn, Ute Hegenbart, Stefan O. Schönland, Günter Fritz, Matthias Schmidt, Marcus Fändrich
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-8 (2019)
Systemic AL amyloidosis is caused by misfolding of immunoglobulin light chains and is one of the most frequently occurring forms of systemic amyloidosis. Here the authors present the 3.3 Å cryo-EM structure of a λ1 AL amyloid fibril that was isolat
Externí odkaz:
https://doaj.org/article/b4de0969a221446794222489fd2110f9
Autor:
William Close, Matthias Neumann, Andreas Schmidt, Manuel Hora, Karthikeyan Annamalai, Matthias Schmidt, Bernd Reif, Volker Schmidt, Nikolaus Grigorieff, Marcus Fändrich
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-7 (2018)
Amyloid fibril structures can display polymorphism. Here the authors reveal the cryo-EM structures of several different fibril morphologies of a peptide derived from an amyloidogenic immunoglobulin light chain and present a mathematical analysis of p
Externí odkaz:
https://doaj.org/article/0e804c5e89db443289443ff9451e6c39
Publikováno v:
PLoS ONE, Vol 6, Iss 3, p e16850 (2011)
The cell envelope of Mycobacterium tuberculosis (M. tuberculosis) is composed of a variety of lipids including mycolic acids, sulpholipids, lipoarabinomannans, etc., which impart rigidity crucial for its survival and pathogenesis. Acyl CoA carboxylas
Externí odkaz:
https://doaj.org/article/7d1e4b22e11a49eab7a6d92a432db135
Autor:
Rüdiger Groß, Desiree Schütz, Marcus Fändrich, Annika Röcker, Karthikeyan Annamalai, Clarissa Read, Sascha Rode, Jan Münch
Publikováno v:
ACS Omega
ACS Omega, Vol 6, Iss 11, Pp 7731-7738 (2021)
ACS Omega, Vol 6, Iss 11, Pp 7731-7738 (2021)
Positively charged naturally occurring or engineered peptide nanofibrils (PNF) are effective enhancers of lentiviral and retroviral transduction, an often rate limiting step in gene transfer and gene therapy approaches. These polycationic PNF are tho
Autor:
Stefan Schönland, Karthikeyan Annamalai, Yin-Hsi Lin, Lynn Radamaker, Matthias Schmidt, Stefanie Huhn, Günter Fritz, Marcus Fändrich, Ute Hegenbart
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-8 (2019)
Nature Communications
Nature Communications
Amyloid fibrils derived from antibody light chains are key pathogenic agents in systemic AL amyloidosis. They can be deposited in multiple organs but cardiac amyloid is the major risk factor of mortality. Here we report the structure of a λ1 AL amyl
Autor:
Stefan Schönland, Karthikeyan Annamalai, Marcus Fändrich, Ute Hegenbart, Bernd Reif, Riddhiman Sarkar, Tejaswini Pradhan
Publikováno v:
Biomol. NMR Assign. 15, 9-16 (2021)
Biomolecular Nmr Assignments
Biomolecular Nmr Assignments
The aggregation of antibody light chains is linked to systemic light chain (AL) amyloidosis, a disease where amyloid deposits frequently affect the heart and the kidney. We here investigate fibrils from the λ-III FOR005 light chain (LC), which is de
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c3ac7968014d16059c2f5e6f14725858
https://push-zb.helmholtz-muenchen.de/frontdoor.php?source_opus=60078
https://push-zb.helmholtz-muenchen.de/frontdoor.php?source_opus=60078
Publikováno v:
In Solid State Ionics 2008 179(21):1234-1237
Autor:
S. Schoenland, Bernd Reif, Stefanie Huhn, Riddhiman Sarkar, Tejaswini Pradhan, Ute Hegenbart, Karthikeyan Annamalai, M. Faendrich
Systemic antibody light chains (AL) amyloidosis is characterized by deposition of amyloid fibrils derived from a particular antibody light chain. Cardiac involvement is a major risk factor for mortality. Using MAS solid-state NMR, we study the fibril
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c2a3b7706ea96f74df41edf9b84e5249
https://doi.org/10.1101/2020.10.02.323303
https://doi.org/10.1101/2020.10.02.323303
Autor:
Stefanie Huhn, Marcus Fändrich, Bernd Reif, Ute Hegenbart, Riddhiman Sarkar, Tejaswini Pradhan, Stefan Schönland, Karthikeyan Annamalai
Publikováno v:
The Journal of Biological Chemistry
J. Biol. Chem. 295, 18474-18484 (2020)
J. Biol. Chem. 295, 18474-18484 (2020)
Systemic antibody light chains (AL) amyloidosis is characterized by deposition of amyloid fibrils derived from a particular antibody light chain. Cardiac involvement is a major risk factor for mortality. Using MAS solid-state NMR, we studied the fibr