Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Alexander Mühleip"'
Autor:
Pradeep Kumar Sheokand, Sabyasachi Pradhan, Andrew E. Maclean, Alexander Mühleip, Lilach Sheiner
Publikováno v:
International Journal of Molecular Sciences, Vol 25, Iss 17, p 9239 (2024)
The Plasmodium falciparum mitochondrial electron transport chain (mETC) is responsible for essential metabolic pathways such as de novo pyrimidine synthesis and ATP synthesis. The mETC complex III (cytochrome bc1 complex) is responsible for transferr
Externí odkaz:
https://doaj.org/article/f405f4da43294a7da06c117f62fe1cec
Autor:
Ondřej Gahura, Alexander Mühleip, Carolina Hierro-Yap, Brian Panicucci, Minal Jain, David Hollaus, Martina Slapničková, Alena Zíková, Alexey Amunts
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-13 (2022)
Mitochondrial ATP synthase assemble into oligomers. Here, authors resolve the structure of trypanosomal ATP synthase, showing that its dimerization is essential for function and evolutionary conserved.
Externí odkaz:
https://doaj.org/article/033e79272bfa4cdc9ca0a33a7abdda7a
Autor:
Alexander Mühleip, Rasmus Kock Flygaard, Jana Ovciarikova, Alice Lacombe, Paula Fernandes, Lilach Sheiner, Alexey Amunts
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-13 (2021)
Structural and functional analysis of mitochondria from the human parasite Toxoplasma gondii reveals that its ATP synthase assembles into cyclic hexamers, arranged together in a form of pentagonal pyramids required for maintenance of cristae morpholo
Externí odkaz:
https://doaj.org/article/56947c119cc747a6b15d66b6a2139440
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-11 (2020)
Mitochondrial ATP synthases are involved in shaping the mitochondrial cristae. The cryo-EM structure of type III ATP synthase reveals the architecture of the unusual, asymmetrical, U-shaped dimer and offers insights into the interaction with the natu
Externí odkaz:
https://doaj.org/article/7d4c0874d55a42c7ab5f4fe8e73119c5
Publikováno v:
eLife, Vol 8 (2019)
The mitochondrial ATP synthase fuels eukaryotic cells with chemical energy. Here we report the cryo-EM structure of a divergent ATP synthase dimer from mitochondria of Euglena gracilis, a member of the phylum Euglenozoa that also includes human paras
Externí odkaz:
https://doaj.org/article/bd25ca45bbff4e43806ee2359013987e
Autor:
Alexander Mühleip, Rasmus Kock Flygaard, Rozbeh Baradaran, Outi Haapanen, Thomas Gruhl, Victor Tobiasson, Amandine Maréchal, Vivek Sharma, Alexey Amunts
Publikováno v:
Mühleip, A, Flygaard, R K, Baradaran, R, Haapanen, O, Gruhl, T, Tobiasson, V, Marechal, A, Sharma, V & Amunts, A 2023, ' Structural basis of mitochondrial membrane bending by the I-II-III2-IV2 supercomplex ', Nature, vol. 615, pp. 934-938 . < https://www.nature.com/articles/s41586-023-05817-y#Abs1 >
Mitochondrial energy conversion requires an intricate architecture of the inner mitochondrial membrane1. Here we show that a supercomplex containing all four respiratory chain components contributes to membrane curvature induction in ciliates. We rep
Autor:
Alexander Mühleip
Publikováno v:
BIOspektrum. 28:590-593
Mitochondrial energy conversion depends on an intricately folded membrane structure, generated by oligomerisation of ATP synthase dimers. However, morphology of cristae membranes varies greatly between different organisms. Recent studies have reveale
Autor:
Alexander Mühleip, Rasmus Kock Flygaard, Outi Haapanen, Rozbeh Baradaran, Thomas Gruhl, Victor Tobiasson, Amandine Maréchal, Vivek Sharma, Alexey Amunts
Mitochondrial energy conversion requires an intricate architecture of the inner mitochondrial membrane1. Here we show that in ciliates, the membrane curvature is provided by a supercomplex containing all four respiratory chain components. We report c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::36c185fe1ba3109cf7266063a3ddb16f
https://doi.org/10.1101/2022.06.26.497646
https://doi.org/10.1101/2022.06.26.497646
Autor:
Ondřej Gahura, Alexander Mühleip, Carolina Hierro-Yap, Brian Panicucci, Minal Jain, David Hollaus, Martina Slapničková, Alena Zíková, Alexey Amunts
Mitochondrial ATP synthase forms stable dimers arranged into oligomeric assemblies that generate the inner-membrane curvature essential for efficient energy conversion. Here, we report cryo-EM structures of the intact ATP synthase dimer from Trypanos
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::671a89a38a993f237284a851793b3dda
https://doi.org/10.21203/rs.3.rs-1196040/v1
https://doi.org/10.21203/rs.3.rs-1196040/v1
Autor:
Ondřej Gahura, Alexander Mühleip, Carolina Hierro-Yap, Brian Panicucci, Minal Jain, David Hollaus, Martina Slapničková, Alena Zíková, Alexey Amunts
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1863:148628