Results 101 to 110 of about 837,065 (393)

Alterations of the mitochondrial proteome caused by the absence of mitochondrial DNA: A proteomic view [PDF]

, 2006
The proper functioning of mitochondria requires that both the mitochondrial and the nuclear genome are functional. To investigate the importance of the mitochondrial genome, which encodes only 13 subunits of the respiratory complexes, the mitochondrial ...
Abdul, Appleby, Armstrong, Bai, Bourges, Buchet, Chai, Claros, Da Cruz, Dey, Du, Garcia, Gianazza, Joseph, King, King, Lescuyer, Luche, Manjasetty, Martinus, Perkins, Rabilloud, Rabilloud, Rabilloud, Rabilloud, Rabilloud, Santoni, Sharma, Sharp, Sherer, Singh, Sinha, Suzuki, Tastet, Taylor, Tryoen-Toth, Ugalde, Wiedemann, Zamzami, Zischka   +39 more
core   +4 more sources

The role of fibroblast growth factors in cell and cancer metabolism

FEBS Letters, EarlyView.
Fibroblast growth factor (FGF) signaling regulates crucial signaling cascades that promote cell proliferation, survival, and metabolism. Therefore, FGFs and their receptors are often dysregulated in human diseases, including cancer, to sustain proliferation and rewire metabolism.
Jessica Price, Chiara Francavilla
wiley   +1 more source

Human F-ATP synthase as a drug target

Pharmacological Research
Practical and conceptual barriers have kept human F-ATP synthase out of reach as a target for the treatment of human diseases. Although this situation has persisted for decades, it may change in the near future.
Christoph Gerle, Chimari Jiko, Atsuki Nakano, Ken Yokoyama, Chai C. Gopalasingam, Hideki Shigematsu, Kazuhiro Abe   +6 more
doaj   +1 more source

An ancestral interaction module promotes oligomerization in divergent mitochondrial ATP synthases

Nature Communications, 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.
Ondřej Gahura, Alexander Mühleip, Carolina Hierro-Yap, Brian Panicucci, Minal Jain, David Hollaus, Martina Slapničková, Alena Zíková, Alexey Amunts   +8 more
doaj   +1 more source

α-synuclein oligomers interact with ATP synthase and open the permeability transition pore in Parkinson’s disease

Nature Communications, 2018
Protein aggregation causes α-synuclein to switch from its physiological role to a pathological toxic gain of function. Under physiological conditions, monomeric α-synuclein improves ATP synthase efficiency.
M. H. Ludtmann, Plamena R. Angelova, M. Horrocks, Minee L. Choi, M. Rodrigues, Artyom Y. Baev, A. V. Berezhnov, Z. Yao, Daniel Little, B. Banushi, A. Al-Menhali, Rohan T. Ranasinghe, Daniel R. Whiten, Ratsuda Yapom, K. S. Dolt, Michael J. Devine, P. Gissen, T. Kunath, Morana Jaganjac, E. Pavlov, D. Klenerman, A. Abramov, S. Gandhi   +22 more
semanticscholar   +1 more source

Type III ATP synthase is a symmetry-deviated dimer that induces membrane curvature through tetramerization

Nature Communications, 2020
Mitochondrial ATP synthases form functional homodimers to induce cristae curvature that is a universal property of mitochondria. To expand on the understanding of this fundamental phenomenon, we characterized the unique type III mitochondrial ATP ...
R. K. Flygaard, Alexander Mühleip, V. Tobiasson, A. Amunts   +3 more
semanticscholar   +1 more source

The IQ‐compete assay for measuring mitochondrial protein import efficiencies in living yeast cells

FEBS Letters, EarlyView.
The efficiency of mitochondrial protein import depends on the properties of the newly synthesized precursor proteins. The Import and de‐Quenching Competition (IQ‐compete) assay is a novel method to monitor the import efficiency of different proteins by fluorescence in living yeast cells.
Yasmin Hoffman, Annika Egeler, Saskia Rödl, Johannes M. Herrmann   +3 more
wiley   +1 more source

Knock-Out of the Genes Coding for the Rieske Protein and the ATP-Synthase δ-Subunit of Arabidopsis [PDF]

, 2003
In Arabidopsis, the nuclear genes PetC and AtpD code for the Rieske protein of the cytochrome b6/f (cyt b6/f) complex and the δ-subunit of the chloroplast ATP synthase (cpATPase), respectively.
Dietzmann, Angela, Jahns, Peter, Joliot, Anne, Joliot, Pierre, Leister, Dario, Levin, Joshua Z., Maiwald, Daniela, Pesaresi, Paolo, Salamini, Francesco   +8 more
core   +1 more source

Mechanism of ATP hydrolysis dependent rotation of bacterial ATP synthase

Nature Communications, 2023
F1 domain of ATP synthase is a rotary ATPase complex in which rotation of central γ-subunit proceeds in 120° steps against a surrounding α3β3 fueled by ATP hydrolysis. How the ATP hydrolysis reactions occurring in three catalytic αβ dimers are coupled to
Atsuki Nakano, Jun-ichi Kishikawa, Kaoru Mitsuoka, Ken Yokoyama   +3 more
doaj   +1 more source

Rotary substates of mitochondrial ATP synthase reveal the basis of flexible F1-Fo coupling

Science, 2019
Flexible domains in a well-oiled machine Motors convert one form of energy into another. For biological motors, adenosine triphosphate (ATP) serves as chemical energy and its hydrolysis is coupled to conformational changes that exert mechanical force ...
B. J. Murphy, Niklas Klusch, J. Langer, D. Mills, Özkan Yildiz, W. Kühlbrandt   +5 more
semanticscholar   +1 more source