Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Ann E. Frazier"'
Autor:
David R. Thorburn, Yilin Kang, Kenji M Fujihara, Catherine S Palmer, Yau C Low, Ann E. Frazier, Nicholas J. Clemons, Daniella H Hock, David A. Stroud, Thomas Daniel Jackson, Diana Stojanovski, Ching-Seng Ang
Publikováno v:
Molecular Biology of the Cell
Acylglycerol kinase (AGK) is a mitochondrial lipid kinase that contributes to protein biogenesis as a subunit of the TIM22 complex at the inner mitochondrial membrane. Mutations in AGK cause Sengers syndrome, an autosomal recessive condition characte
Autor:
Alexander J Anderson, Nicholas J. Clemons, Yilin Kang, David P De Souza, Tegan Stait, Malcolm J. McConville, Diana Stojanovski, David A. Stroud, Kenji M Fujihara, Thomas Daniel Jackson, David R. Thorburn, Michael T. Ryan, Deidreia Tull, Catherine S Palmer, Ann E. Frazier
Publikováno v:
eLife
eLife, Vol 8 (2019)
eLife, Vol 8 (2019)
Human Tim8a and Tim8b are members of an intermembrane space chaperone network, known as the small TIM family. Mutations in TIMM8A cause a neurodegenerative disease, Mohr-Tranebjærg syndrome (MTS), which is characterised by sensorineural hearing loss
Publikováno v:
ResearcherID
Most mitochondrial proteins are synthesized in the cytosol, translocated into the organelle and directed along specific sorting pathways. Over the past 20 years, >30 proteins have been identified as having key roles in mitochondrial protein import. R
Autor:
Rebecca D. Taylor, Ann E. Frazier, Chris Meisinger, Katrin Brandner, Peter Rehling, David U. Mick
Publikováno v:
Molecular Biology of the Cell. 16:5202-5214
The Saccharomyces cerevisiae Taz1 protein is the orthologue of human Tafazzin, a protein that when inactive causes Barth Syndrome (BTHS), a severe inherited X-linked disease. Taz1 is a mitochondrial acyltransferase involved in the remodeling of cardi
Autor:
Albert Sickmann, Virginia Bilanchone, M G Cumsky, Kaye N. Truscott, Helmut E. Meyer, Yanfeng Li, Andreas Geissler, Ann E. Frazier, Wolfgang Voos, Chris Meisinger, Maria I. Lind, Peter Rehling, Jan Dudek, Bernard Guiard, Nikolaus Pfanner
Publikováno v:
Nature Structural & Molecular Biology. 11:226-233
Mitochondrial preproteins destined for the matrix are translocated by two channel-forming transport machineries, the translocase of the outer membrane and the presequence translocase of the inner membrane. The presequence translocase-associated prote
Autor:
Agnieszka Chacinska, Ann E. Frazier, Wolfgang Voos, Peter Rehling, Bernard Guiard, Nikolaus Pfanner, Chris Meisinger, Agnes Schulze-Specking
Publikováno v:
The EMBO Journal. 22:5370-5381
Preproteins with N-terminal presequences are imported into mitochondria at translocation contact sites that include the translocase of the outer membrane (TOM complex) and the presequence translocase of the inner membrane (TIM23 complex). Little is k
Autor:
Yanfeng Li, Chris Meisinger, Bernard Guiard, Maria I. Lind, Nikolaus Pfanner, Peter Rehling, Ann E. Frazier, Helmut E. Meyer, Hanne Müller, Jan Dudek, Andreas Geissler, Wolfgang Voos, Albert Sickmann, Kaye N. Truscott
Publikováno v:
The Journal of Cell Biology
Transport of preproteins into the mitochondrial matrix is mediated by the presequence translocase–associated motor (PAM). Three essential subunits of the motor are known: mitochondrial Hsp70 (mtHsp70); the peripheral membrane protein Tim44; and the
Autor:
Ann E. Frazier, Agnieszka Chacinska, Bernard Guiard, Nikolaus Pfanner, Kaye N. Truscott, Peter Rehling
Publikováno v:
Molecular and cellular biology. 23(21)
The mitochondrial inner membrane contains numerous multispanning integral proteins. The precursors of these hydrophobic proteins are synthesized in the cytosol and therefore have to cross the mitochondrial outer membrane and intermembrane space to re
Autor:
Kaye N. Truscott, Andreas Geissler, Chris Meisinger, Jan Dudek, Maria I. Lind, Bernard Guiard, Nikolaus Pfanner, Ann E. Frazier, Peter Rehling, Helmut E. Meyer, Albert Sickmann, Agnieszka Chacinska
Publikováno v:
Cell. (6):817-829
SummaryThe presequence translocase of the inner mitochondrial membrane (TIM23 complex) operates at a central junction of protein import. It accepts preproteins from the outer membrane TOM complex and directs them to inner membrane insertion or, in co