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Refinado por: Base de dados/Biblioteca: JSTOR (Journal Storage) remover Base de dados/Biblioteca: Single Journals remover
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1
Permeability transition in human mitochondria persists in the absence of peripheral stalk subunits of ATP synthase
Permeability transition in human mitochondria persists in the absence of peripheral stalk subunits of ATP synthase
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Permeability transition in human mitochondria persists in the absence of peripheral stalk subunits of ATP synthase

He, Jiuya ; Carroll, Joe ; Ding, Shujing ; Fearnley, Ian M. ; Walker, John E.

Proceedings of the National Academy of Sciences - PNAS, 2017-08, Vol.114 (34), p.9086-9091 [Periódico revisado por pares]

United States: National Academy of Sciences

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2
Persistence of the permeability transition pore in human mitochondria devoid of an assembled ATP synthase
Persistence of the permeability transition pore in human mitochondria devoid of an assembled ATP synthase
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Persistence of the permeability transition pore in human mitochondria devoid of an assembled ATP synthase

Carroll, Joe ; He, Jiuya ; Ding, Shujing ; Fearnley, Ian M. ; Walker, John E.

Proceedings of the National Academy of Sciences - PNAS, 2019-06, Vol.116 (26), p.12816-12821 [Periódico revisado por pares]

United States: National Academy of Sciences

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3
REPLY TO BERNARDI: The mitochondrial permeability transition pore and the ATP synthase
REPLY TO BERNARDI: The mitochondrial permeability transition pore and the ATP synthase
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REPLY TO BERNARDI: The mitochondrial permeability transition pore and the ATP synthase

Walker, John E. ; Carroll, Joe ; He, Jiuya

Proceedings of the National Academy of Sciences - PNAS, 2020-02, Vol.117 (6), p.2745-2746 [Periódico revisado por pares]

United States: National Academy of Sciences

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4
The mitochondrial ATP synthase is a negative regulator of the mitochondrial permeability transition pore
The mitochondrial ATP synthase is a negative regulator of the mitochondrial permeability transition pore
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The mitochondrial ATP synthase is a negative regulator of the mitochondrial permeability transition pore

Pekson, Ryan ; Liang, Felix G ; Axelrod, Joshua L ; Lee, Jaehoon ; Qin, Dongze ; Wittig, Andre J H ; Paulino, Victor M ; Zheng, Min ; Peixoto, Pablo M ; Kitsis, Richard N

Proceedings of the National Academy of Sciences - PNAS, 2023-12, Vol.120 (51), p.e2303713120-e2303713120 [Periódico revisado por pares]

United States: National Academy of Sciences

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5
Ladderane phospholipids form a densely packed membrane with normal hydrazine and anomalously low proton/hydroxide permeability
Ladderane phospholipids form a densely packed membrane with normal hydrazine and anomalously low proton/hydroxide permeability
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Ladderane phospholipids form a densely packed membrane with normal hydrazine and anomalously low proton/hydroxide permeability

Moss, Frank R. ; Shuken, Steven R. ; Mercer, Jaron A. M. ; Cohen, Carolyn M. ; Weiss, Thomas M. ; Boxer, Steven G. ; Burns, Noah Z.

Proceedings of the National Academy of Sciences - PNAS, 2018-09, Vol.115 (37), p.9098-9103 [Periódico revisado por pares]

United States: National Academy of Sciences

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6
Passive membrane transport of lignin-related compounds
Passive membrane transport of lignin-related compounds
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Passive membrane transport of lignin-related compounds

Vermaas, Josh V ; Dixon, Richard A ; Chen, Fang ; Mansfield, Shawn D ; Boerjan, Wout ; Ralph, John ; Crowley, Michael F ; Beckham, Gregg T

Proceedings of the National Academy of Sciences - PNAS, 2019-11, Vol.116 (46), p.23117-23123 [Periódico revisado por pares]

United States: National Academy of Sciences

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7
A small-molecule inhibitor of BamA impervious to efflux and the outer membrane permeability barrier
A small-molecule inhibitor of BamA impervious to efflux and the outer membrane permeability barrier
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A small-molecule inhibitor of BamA impervious to efflux and the outer membrane permeability barrier

Hart, Elizabeth M. ; Mitchell, Angela M. ; Konovalova, Anna ; Grabowicz, Marcin ; Sheng, Jessica ; Han, Xiaoqing ; Rodriguez-Rivera, Frances P. ; Schwaid, Adam G. ; Malinverni, Juliana C. ; Balibar, Carl J. ; Bodea, Smaranda ; Si, Qian ; Wang, Hao ; Homsher, Michelle F. ; Painter, Ronald E. ; Ogawa, Anthony K. ; Sutterlin, Holly ; Roemer, Terry ; Black, Todd A. ; Rothman, Deborah M. ; Walker, Scott S. ; Silhavy, Thomas J.

Proceedings of the National Academy of Sciences - PNAS, 2019-10, Vol.116 (43), p.21748-21757 [Periódico revisado por pares]

United States: National Academy of Sciences

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8
Nanoscale control of internal inhomogeneity enhances water transport in desalination membranes
Nanoscale control of internal inhomogeneity enhances water transport in desalination membranes
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Nanoscale control of internal inhomogeneity enhances water transport in desalination membranes

Culp, Tyler E ; Khara, Biswajit ; Brickey, Kaitlyn P ; Geitner, Michael ; Zimudzi, Tawanda J ; Wilbur, Jeffrey D ; Jons, Steven D ; Roy, Abhishek ; Paul, Mou ; Ganapathysubramanian, Baskar ; Zydney, Andrew L ; Kumar, Manish ; Gomez, Enrique D

Science (American Association for the Advancement of Science), 2021-01, Vol.371 (6524), p.72-75 [Periódico revisado por pares]

United States: The American Association for the Advancement of Science

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9
Coupled transmembrane mechanisms control MCU-mediated mitochondrial Ca2+ uptake
Coupled transmembrane mechanisms control MCU-mediated mitochondrial Ca2+ uptake
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Coupled transmembrane mechanisms control MCU-mediated mitochondrial Ca2+ uptake

Vais, Horia ; Payne, Riley ; Paudel, Usha ; Li, Carmen ; Foskett, J. Kevin

Proceedings of the National Academy of Sciences - PNAS, 2020-09, Vol.117 (35), p.21731-21739 [Periódico revisado por pares]

Washington: National Academy of Sciences

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10
Phospholipid retention in the absence of asymmetry strengthens the outer membrane permeability barrier to last-resort antibiotics
Phospholipid retention in the absence of asymmetry strengthens the outer membrane permeability barrier to last-resort antibiotics
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Phospholipid retention in the absence of asymmetry strengthens the outer membrane permeability barrier to last-resort antibiotics

Powers, Matthew J. ; Trent, M. Stephen

Proceedings of the National Academy of Sciences - PNAS, 2018-09, Vol.115 (36), p.E8518-E8527 [Periódico revisado por pares]

United States: National Academy of Sciences

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