Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Lars Kintscher"'
Publikováno v:
Procedia CIRP. 98:318-323
Product recycling will become more important in the future to meet the needs of a growing industry. The challenge is to combine this heterogeneous information flows and establish a way for a holistic life cycle management in the circular economy. The
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::50f1328c204376f04e447946c7c826d5
https://doi.org/10.1016/j.procir.2021.01.110
https://doi.org/10.1016/j.procir.2021.01.110
Publikováno v:
Journal of Communications. :652-660
Recycling will become more and more important in the future. To fulfill the requirements of a more efficient recycling process and thus enable an eco-friendly handling of resources, modern technologies can be used. One of these modern technology stre
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f8c4f674c31af5ef5e2a3938c5130efa
https://doi.org/10.12720/jcm.15.9.652-660
https://doi.org/10.12720/jcm.15.9.652-660
Autor:
Gert Bikker, Christian Scheller, Lars Kintscher, Holger Brüggemann, Mathias Nippraschk, Steffen Blömeke, Thomas Spengler, Priyanka Sharma, Daniel Goldmann, Sebastian Lawrenz, Mark Mennenga, Andreas Rausch, Hendrik Poschmann, Christoph Herrmann
Publikováno v:
ICT4S
Resource scarcity is a global challenge, especially in E-mobility. Currently, Electric vehicles (EVs) are considered as an attractive option on a pathway towards low emission mobility. Nevertheless, due to the increasing sales and acceptance of EVs,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::691f793f2e4b36662e3ffd50c56ede4a
https://doi.org/10.1145/3401335.3401666
https://doi.org/10.1145/3401335.3401666
Autor:
Tim Rasmussen, Benedikt Brors, Hanns Weiss, Dierk Scheide, Thorsten Friedrich, Lars Kintscher
Publikováno v:
Biochemistry. 40:6124-6131
The proton-translocating NADH:ubiquinone oxidoreductase of respiratory chains (complex I) contains one flavin mononucleotide and five EPR-detectable iron-sulfur clusters as redox groups. Because of the number of conserved motifs typical for binding i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fa7120670269ec3b11f5692e08a3086a
https://doi.org/10.1021/bi0026977
https://doi.org/10.1021/bi0026977
Autor:
Tim Rasmussen, Dierk Scheide, Werner Mäntele, Lars Kintscher, Benedikt Brors, Petra Hellwig, Hanns Weiss, Thorsten Friedrich, Ulrich Schulte
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1459(2-3):305-309
The proton-pumping NADH:ubiquinone oxidoreductase is the first of the respiratory chain complexes in many bacteria and mitochondria of most eukaryotes. The bacterial complex consists of 14 different subunits. Seven peripheral subunits bear all known
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::862394a3b990ab22ce9bd5d38c97c291
Autor:
Hanns Weiss, Ulrich Schulte, Dierk Scheide, Kevin Leonard, Tim Rasmussen, Thorsten Friedrich, Angela Schlitt, Anke Abelmann, Vincent Guénebaut, Lars Kintscher, Benedikt Brors
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1365(1-2):215-219
The proton-pumping NADH:ubiquinone oxidoreductase is the first complex in the respiratory chains of many purple bacteria and of mitochondria of most eucaryotes. The bacterial complex consists of 14 different subunits. The mitochondrial complex contai
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::151cfdf607f00912fdbd66d6339e052f
Autor:
Hanns Weiss, Benedikt Brors, Anke Abelmann, Lars Kintscher, Thorsten Friedrich, Ulrich Schulte, Natascha Amling, Tim Rasmussen
Publikováno v:
Scopus-Elsevier
The proton-translocating NADH:ubiquinone oxidoreductase of mitochondria (complex I) is a large L-shaped multisubunit complex. The peripheral matrix arm contains one FMN and a number of iron-sulfur (FeS) clusters and is involved in NADH oxidation and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::05e59a9362b66c71745fca02bb8f2649
https://pubmed.ncbi.nlm.nih.gov/9914816
https://pubmed.ncbi.nlm.nih.gov/9914816