TY  - JOUR
A1  - Arnison, Paul G.
A1  - Bibb, Mervyn J.
A1  - Bierbaum, Gabriele
A1  - Bowers, Albert A.
A1  - Bugni, Tim S.
A1  - Bulaj, Grzegorz
A1  - Camarero, Julio A.
A1  - Campopiano, Dominic J.
A1  - Challis, Gregory L.
A1  - Clardy, Jon
A1  - Cotter, Paul D.
A1  - Craik, David J.
A1  - Dawson, Michael
A1  - Dittmann-Thünemann, Elke
A1  - Donadio, Stefano
A1  - Dorrestein, Pieter C.
A1  - Entian, Karl-Dieter
A1  - Fischbach, Michael A.
A1  - Garavelli, John S.
A1  - Goeransson, Ulf
A1  - Gruber, Christian W.
A1  - Haft, Daniel H.
A1  - Hemscheidt, Thomas K.
A1  - Hertweck, Christian
A1  - Hill, Colin
A1  - Horswill, Alexander R.
A1  - Jaspars, Marcel
A1  - Kelly, Wendy L.
A1  - Klinman, Judith P.
A1  - Kuipers, Oscar P.
A1  - Link, A. James
A1  - Liu, Wen
A1  - Marahiel, Mohamed A.
A1  - Mitchell, Douglas A.
A1  - Moll, Gert N.
A1  - Moore, Bradley S.
A1  - Mueller, Rolf
A1  - Nair, Satish K.
A1  - Nes, Ingolf F.
A1  - Norris, Gillian E.
A1  - Olivera, Baldomero M.
A1  - Onaka, Hiroyasu
A1  - Patchett, Mark L.
A1  - Piel, Jörn
A1  - Reaney, Martin J. T.
A1  - Rebuffat, Sylvie
A1  - Ross, R. Paul
A1  - Sahl, Hans-Georg
A1  - Schmidt, Eric W.
A1  - Selsted, Michael E.
A1  - Severinov, Konstantin
A1  - Shen, Ben
A1  - Sivonen, Kaarina
A1  - Smith, Leif
A1  - Stein, Torsten
A1  - Suessmuth, Roderich D.
A1  - Tagg, John R.
A1  - Tang, Gong-Li
A1  - Truman, Andrew W.
A1  - Vederas, John C.
A1  - Walsh, Christopher T.
A1  - Walton, Jonathan D.
A1  - Wenzel, Silke C.
A1  - Willey, Joanne M.
A1  - van der Donk, Wilfred A.
T1  - Ribosomally synthesized and post-translationally modified peptide natural products overview and recommendations for a universal nomenclature
JF  - Natural product reports : a journal of current developments in bio-organic chemistry
N2  - This review presents recommended nomenclature for the biosynthesis of ribosomally synthesized and post-translationally modified peptides (RiPPs), a rapidly growing class of natural products. The current knowledge regarding the biosynthesis of the >20 distinct compound classes is also reviewed, and commonalities are discussed.
Y1  - 2013
U6  - https://doi.org/10.1039/c2np20085f
SN  - 0265-0568
VL  - 30
IS  - 1
SP  - 108
EP  - 160
PB  - Royal Society of Chemistry
CY  - Cambridge
ER  - 
TY  - JOUR
A1  - Henze, Andrea
A1  - Homann, Thomas
A1  - Rohn, Isabelle
A1  - Aschner, Michael A.
A1  - Link, Christopher D.
A1  - Kleuser, Burkhard
A1  - Schweigert, Florian J.
A1  - Schwerdtle, Tanja
A1  - Bornhorst, Julia
T1  - Caenorhabditis elegans as a model system to study post-translational modifications of human transthyretin
JF  - Scientific reports
N2  - The visceral protein transthyretin (TTR) is frequently affected by oxidative post-translational protein modifications (PTPMs) in various diseases. Thus, better insight into structure-function relationships due to oxidative PTPMs of TTR should contribute to the understanding of pathophysiologic mechanisms. While the in vivo analysis of TTR in mammalian models is complex, time-and resource-consuming, transgenic Caenorhabditis elegans expressing hTTR provide an optimal model for the in vivo identification and characterization of drug-mediated oxidative PTPMs of hTTR by means of matrix assisted laser desorption/ionization - time of flight - mass spectrometry (MALDI-TOF-MS). Herein, we demonstrated that hTTR is expressed in all developmental stages of Caenorhabditis elegans, enabling the analysis of hTTR metabolism during the whole life-cycle. The suitability of the applied model was verified by exposing worms to D-penicillamine and menadione. Both drugs induced substantial changes in the oxidative PTPM pattern of hTTR. Additionally, for the first time a covalent binding of both drugs with hTTR was identified and verified by molecular modelling.
Y1  - 2016
U6  - https://doi.org/10.1038/srep37346
SN  - 2045-2322
VL  - 6
PB  - Nature Publ. Group
CY  - London
ER  - 
TY  - GEN
A1  - Henze, Andrea
A1  - Homann, Thomas
A1  - Rohn, Isabelle
A1  - Aschner, Michael A.
A1  - Link, Christopher D.
A1  - Kleuser, Burkhard
A1  - Schweigert, Florian J.
A1  - Schwerdtle, Tanja
A1  - Bornhorst, Julia
T1  - Caenorhabditis elegans as a model system to study post-translational modifications of human transthyretin
N2  - The visceral protein transthyretin (TTR) is frequently affected by oxidative post-translational protein modifications (PTPMs) in various diseases. Thus, better insight into structure-function relationships due to oxidative PTPMs of TTR should contribute to the understanding of pathophysiologic mechanisms. While the in vivo analysis of TTR in mammalian models is complex, time- and resource-consuming, transgenic Caenorhabditis elegans expressing hTTR provide an optimal model for the in vivo identification and characterization of drug-mediated oxidative PTPMs of hTTR by means of matrix assisted laser desorption/ionization – time of flight – mass spectrometry (MALDI-TOF-MS). Herein, we demonstrated that hTTR is expressed in all developmental stages of Caenorhabditis elegans, enabling the analysis of hTTR metabolism during the whole life-cycle. The suitability of the applied model was verified by exposing worms to D-penicillamine and menadione. Both drugs induced substantial changes in the oxidative PTPM pattern of hTTR. Additionally, for the first time a covalent binding of both drugs with hTTR was identified and verified by molecular modelling.
T3  - Zweitveröffentlichungen der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe - 312 
KW  - binding
KW  - c. elegans
KW  - cells
KW  - disease
KW  - force-field
KW  - life-span
KW  - menadione
KW  - n-acetyl-cysteine
KW  - protein
KW  - s-glutathionylation
Y1  - 2016
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:kobv:517-opus4-103674
ER  - 
TY  - JOUR
A1  - Henze, Andrea
A1  - Homann, Thomas
A1  - Rohn, Isabelle
A1  - Aschner, Michael A.
A1  - Link, Christopher D.
A1  - Kleuser, Burkhard
A1  - Schweigert, Florian J.
A1  - Schwerdtle, Tanja
A1  - Bornhorst, Julia
T1  - Caenorhabditis elegans as a model system to study post-translational modifications of human transthyretin
JF  - Scientific reports
N2  - The visceral protein transthyretin (TTR) is frequently affected by oxidative post-translational protein modifications (PTPMs) in various diseases. Thus, better insight into structure-function relationships due to oxidative PTPMs of TTR should contribute to the understanding of pathophysiologic mechanisms. While the in vivo analysis of TTR in mammalian models is complex, time- and resource-consuming, transgenic Caenorhabditis elegans expressing hTTR provide an optimal model for the in vivo identification and characterization of drug-mediated oxidative PTPMs of hTTR by means of matrix assisted laser desorption/ionization – time of flight – mass spectrometry (MALDI-TOF-MS). Herein, we demonstrated that hTTR is expressed in all developmental stages of Caenorhabditis elegans, enabling the analysis of hTTR metabolism during the whole life-cycle. The suitability of the applied model was verified by exposing worms to D-penicillamine and menadione. Both drugs induced substantial changes in the oxidative PTPM pattern of hTTR. Additionally, for the first time a covalent binding of both drugs with hTTR was identified and verified by molecular modelling.
KW  - n-acetyl-cysteine
KW  - s-glutathionylation
KW  - force-field
KW  - c. elegans
KW  - life-span
KW  - protein
KW  - cells
KW  - menadione
KW  - disease
KW  - binding
Y1  - 2016
U6  - https://doi.org/10.1038/srep37346
SN  - 2045-2322
VL  - 6
PB  - Nature Publishing Group
CY  - London
ER  -