sameAs
P1889
Antamanide, a derivative of Amanita phalloides, is a novel inhibitor of the mitochondrial permeability transition poreThe mitochondrial chaperone TRAP1 promotes neoplastic growth by inhibiting succinate dehydrogenaseHexokinase II detachment from mitochondria triggers apoptosis through the permeability transition pore independent of voltage-dependent anion channelsDevelopmental shift of cyclophilin D contribution to hypoxic-ischemic brain injuryCyclosporin A corrects mitochondrial dysfunction and muscle apoptosis in patients with collagen VI myopathiesFrom ATP to PTP and Back: A Dual Function for the Mitochondrial ATP SynthaseThe mitochondrial permeability transition pore: molecular nature and role as a target in cardioprotectionThe mitochondrial permeability transition from yeast to mammalsDimers of mitochondrial ATP synthase form the permeability transition poreRegulation of the inner membrane mitochondrial permeability transition by the outer membrane translocator protein (peripheral benzodiazepine receptor)Cyclophilin D modulates mitochondrial F0F1-ATP synthase by interacting with the lateral stalk of the complexPhosphate is essential for inhibition of the mitochondrial permeability transition pore by cyclosporin A and by cyclophilin D ablationMyotonic dystrophy protein kinase (DMPK) prevents ROS-induced cell death by assembling a hexokinase II-Src complex on the mitochondrial surfaceLigand-selective modulation of the permeability transition pore by arginine modification. Opposing effects of p-hydroxyphenylglyoxal and phenylglyoxal.Opening of the mitochondrial permeability transition pore causes depletion of mitochondrial and cytosolic NAD+ and is a causative event in the death of myocytes in postischemic reperfusion of the heart.The mitochondrial permeability transition, release of cytochrome c and cell death. Correlation with the duration of pore openings in situ.Modification of permeability transition pore arginine(s) by phenylglyoxal derivatives in isolated mitochondria and mammalian cells. Structure-function relationship of arginine ligands.The mitochondrial effects of small organic ligands of BCL-2: sensitization of BCL-2-overexpressing cells to apoptosis by a pyrimidine-2,4,6-trione derivative.Properties of the permeability transition in VDAC1(-/-) mitochondria.Regulation of the mitochondrial permeability transition pore by the outer membrane does not involve the peripheral benzodiazepine receptor (Translocator Protein of 18 kDa (TSPO)).Channel formation by yeast F-ATP synthase and the role of dimerization in the mitochondrial permeability transition.Mitochondria and cell death. Mechanistic aspects and methodological issues.Mitochondrial transport of cations: channels, exchangers, and permeability transition.Progress on the mitochondrial permeability transition pore: regulation by complex I and ubiquinone analogs.The effects of idebenone on mitochondrial bioenergeticsDestabilization of the outer and inner mitochondrial membranes by core and linker histones.Monoamine oxidase inhibition prevents mitochondrial dysfunction and apoptosis in myoblasts from patients with collagen VI myopathies.Mitochondrial dysfunction and defective autophagy in the pathogenesis of collagen VI muscular dystrophies.p66Shc, mitochondria, and the generation of reactive oxygen species.Properties of the permeability transition pore in mitochondria devoid of Cyclophilin D.Melanocytes from Patients Affected by Ullrich Congenital Muscular Dystrophy and Bethlem Myopathy have Dysfunctional Mitochondria That Can be Rescued with Cyclophilin Inhibitors.Changes in muscle cell metabolism and mechanotransduction are associated with myopathic phenotype in a mouse model of collagen VI deficiency.Assessing the molecular basis for rat-selective induction of the mitochondrial permeability transition by norbormide.Enhancement of anxiety, facilitation of avoidance behavior, and occurrence of adult-onset obesity in mice lacking mitochondrial cyclophilin DTherapy of collagen VI-related myopathies (Bethlem and Ullrich).Peptide-based carbon nanotubes for mitochondrial targeting.Mitochondrial energy dissipation by fatty acids. Mechanisms and implications for cell death.Hepatic progenitor cells express SerpinB3F-ATPase of Drosophila melanogaster forms 53-picosiemen (53-pS) channels responsible for mitochondrial Ca2+-induced Ca2+ release.Mitochondria and reperfusion injury. The role of permeability transition.
P50
Q21562115-6E342E81-4E3A-4A03-ADEB-96CF9C93932CQ24294745-51942C31-B6C9-4992-965B-8222404C543CQ24312702-C6ACD37F-D16F-4128-8329-6BE4118E06B3Q24607913-54BC618E-E621-4413-978B-B841F039D9F8Q24647603-97A151CB-04DF-410D-BB55-AD7FB0597C22Q27004110-4692495A-0605-4695-B417-852FDF48F7E1Q28248925-902C3BC9-FD39-404D-9801-4ECC1730BD98Q28279895-E6446165-0EE2-450F-A381-E6F6D2CCA129Q28287824-A3D65832-94B6-45E1-9CA1-00D9D8901321Q28297948-693C1C49-9FB7-4A85-B958-C6B09CA4004BQ28507223-58AEB27D-A02F-4CB6-8EAA-6B5E2718A5DAQ28594159-5FAE7FE0-1029-4A5C-969F-5AF00C9B8840Q30009539-6EA2F991-768C-41C0-BDEE-B03C761CD48EQ31028811-373F859F-31BD-4E14-B75E-E6B0C3FC0ACBQ31552541-818FC98D-61AD-4E79-BE68-5AB018ECA203Q31779663-7D57134A-E9DC-4416-B934-1286B4C8776EQ33211203-D52FC53B-21BE-464E-B2C5-C667C4D79958Q33234059-E7C4C499-F015-483A-A120-2EFC46A799A1Q33240486-85682BD2-03AB-4786-B3BA-7BB1298EE671Q33619335-A02566A1-A28E-4863-803C-2951572A8847Q33718426-23B1015B-D41D-4693-A425-60CBF99E2D0CQ33734610-F636AE9B-4AA0-4ADD-9664-214A631EC1A3Q33744633-3E556919-6741-4706-A29F-F807271E8925Q33832698-FD293B07-CD08-4BCB-8585-5C67B4C2282CQ34075134-D04ACD86-D594-4336-9EE5-91DD2C6076D0Q34241828-AA213875-1ACE-4E31-88FC-0C1DEDE69759Q34266732-CDE76AC3-FEFB-4CB9-918D-EAC584F4A42BQ34338854-D34AE986-0225-4887-BA78-1599EC6D4772Q34357221-92057DD5-330D-4466-8114-9F0DE9349DD5Q34406704-5B13520D-D4EA-4095-992A-8A46F2B97DA3Q34547398-A2CC0564-11AD-407E-B67F-A5D88277027BQ34599342-ED04C93A-BBF4-45A2-8FF3-E07E77FA3B1DQ34629293-BD392B4E-F4AB-4411-8308-EFE2D6F2C593Q34671714-6AD452F8-15FC-4A82-A64F-4A08047A3568Q34883830-351DD234-8618-4327-9C24-15D728F148E9Q34884970-CC6A5BA8-AC69-4EF2-A532-35F29DA4C977Q35025248-15D48019-C9D5-4FAA-9651-83BDB402736EQ35092061-49261922-46D0-4739-B13B-E1D36C19D19DQ35103850-B4253FDC-91E0-4608-BCAF-D5AD67780AB2Q35166967-1F28F9EC-478C-419E-926A-36F3BE48FD5A
P50
description
Italian pathologist
@en
Italian pathologist
@en-ca
Italian pathologist
@en-gb
médecin italien
@fr
patólogo italiano
@es
wetenschapper
@nl
عالم أمراض إيطالي
@ar
name
Paolo Bernardi
@ast
Paolo Bernardi
@de
Paolo Bernardi
@en
Paolo Bernardi
@es
Paolo Bernardi
@fr
Paolo Bernardi
@nl
Paolo Bernardi
@sl
type
label
Paolo Bernardi
@ast
Paolo Bernardi
@de
Paolo Bernardi
@en
Paolo Bernardi
@es
Paolo Bernardi
@fr
Paolo Bernardi
@nl
Paolo Bernardi
@sl
prefLabel
Paolo Bernardi
@ast
Paolo Bernardi
@de
Paolo Bernardi
@en
Paolo Bernardi
@es
Paolo Bernardi
@fr
Paolo Bernardi
@nl
Paolo Bernardi
@sl
P1053
C-3656-2008
P1889
P1960
OIumVrsAAAAJ
P21
P2798
P31
P3829
P496
0000-0001-9187-3736
P5463
Bernardi_Paolo
P569
1953-01-01T00:00:00Z