The mitochondrial permeability transition: Recent progress and open questions
P Bernardi, M Carraro, G Lippe - The FEBS journal, 2022 - Wiley Online Library
Major progress has been made in defining the basis of the mitochondrial permeability
transition, a Ca2+‐dependent permeability increase of the inner membrane that has puzzled …
transition, a Ca2+‐dependent permeability increase of the inner membrane that has puzzled …
Structure and function of mitochondrial membrane protein complexes
W Kühlbrandt - BMC biology, 2015 - Springer
Biological energy conversion in mitochondria is carried out by the membrane protein
complexes of the respiratory chain and the mitochondrial ATP synthase in the inner …
complexes of the respiratory chain and the mitochondrial ATP synthase in the inner …
Multiscale simulations of biological membranes: the challenge to understand biological phenomena in a living substance
Biological membranes are tricky to investigate. They are complex in terms of molecular
composition and structure, functional over a wide range of time scales, and characterized by …
composition and structure, functional over a wide range of time scales, and characterized by …
The mitochondrial permeability transition pore: channel formation by F-ATP synthase, integration in signal transduction, and role in pathophysiology
P Bernardi, A Rasola, M Forte… - Physiological …, 2015 - journals.physiology.org
The mitochondrial permeability transition (PT) is a permeability increase of the inner
mitochondrial membrane mediated by a channel, the permeability transition pore (PTP) …
mitochondrial membrane mediated by a channel, the permeability transition pore (PTP) …
Mitochondrial ATP generation is more proteome efficient than glycolysis
Metabolic efficiency profoundly influences organismal fitness. Nonphotosynthetic organisms,
from yeast to mammals, derive usable energy primarily through glycolysis and respiration …
from yeast to mammals, derive usable energy primarily through glycolysis and respiration …
Structure of a complete ATP synthase dimer reveals the molecular basis of inner mitochondrial membrane morphology
We determined the structure of a complete, dimeric F 1 F o-ATP synthase from yeast
Yarrowia lipolytica mitochondria by a combination of cryo-EM and X-ray crystallography. The …
Yarrowia lipolytica mitochondria by a combination of cryo-EM and X-ray crystallography. The …
Atomic model for the dimeric FO region of mitochondrial ATP synthase
H Guo, SA Bueler, JL Rubinstein - Science, 2017 - science.org
Mitochondrial adenosine triphosphate (ATP) synthase produces the majority of ATP in
eukaryotic cells, and its dimerization is necessary to create the inner membrane folds, or …
eukaryotic cells, and its dimerization is necessary to create the inner membrane folds, or …
[图书][B] Bioenergetics
DG Nicholls - 2013 - books.google.com
Extensively revised, the fourth edition of this highly successful book takes into account the
many newly determined protein structures that provide molecular insight into chemiosmotic …
many newly determined protein structures that provide molecular insight into chemiosmotic …
Cryo-EM structure of the mammalian ATP synthase tetramer bound with inhibitory protein IF1
The mitochondrial adenosine triphosphate (ATP) synthase produces most of the ATP
required by mammalian cells. We isolated porcine tetrameric ATP synthase and solved its …
required by mammalian cells. We isolated porcine tetrameric ATP synthase and solved its …
High-resolution cryo-EM analysis of the yeast ATP synthase in a lipid membrane
INTRODUCTION The mitochondrial adenosine triphosphate (ATP) synthase is the enzyme
responsible for the synthesis of more than 90% of the ATP produced by mammalian cells …
responsible for the synthesis of more than 90% of the ATP produced by mammalian cells …