tBID, a membrane-targeted death ligand, oligomerizes BAK to release cytochrome c
In PLoS Pathogens, 1999
... from Santa Cruz Biotechnologies (Santa Cruz, California, United States); monoclonal antibodies to Bcl-xL, cytochrome c, Tom20, Tim44 and PARP were obtained from Pharmingen (San Diego, California, United States); rabbit polyclonal antibody to GFP was obtained from Clontech; M30 antibody against cleaved ...
Norcantharidin Inhibits SK-N-SH Neuroblastoma Cell Growth by Induction of Autophagy and Apoptosis.
Guangzhou, China. In Technol Cancer Res Treat, Feb 2016
In the present study, norcantharidin suppressed the proliferation and cloning ability of SK-N-SH cells in a dose-dependent manner, apparently by reducing the mitochondrial membrane potential and arresting SK-N-SH cells at the G2/M stage, accompanied by elevated expressions of p21 and decreased expressions of cyclin B1 and cell division control 2. Treatment by norcantharidin induced significant mitophagy and autophagy, as demonstrated by a decrease in Translocase Of Outer Mitochondrial Membrane 20 (TOM20), increased beclin1 and LC3-II protein expression, reduced protein SQSTM1/p62 expression, and accumulation of punctate LC3 in the cytoplasm of SK-N-SH cells.
Unique components of the plant mitochondrial protein import apparatus.
Crawley, United Kingdom. In Biochim Biophys Acta, 2013
This includes the evolution of two unique outer membrane import receptors, plant Translocase of outer membrane 20 kDa subunit (TOM20) and Outer membrane protein of 64 kDa (OM64), the loss of a receptor domain from an ancestral import component, Translocase of outer membrane 22 kDa subunit (TOM22), evolution of unique features in the disulfide relay system of the inter membrane space, and the addition of an extra membrane spanning domain to another ancestral component of the inner membrane, Translocase of inner membrane 17 kDa subunit (TIM17).
Functions of outer membrane receptors in mitochondrial protein import.
Nagoya, Japan. In Biochim Biophys Acta, 2002
The recently determined NMR structure of the general import receptor Tom20 in a complex with a presequence peptide reveals that, although the amphiphilicity and positive charges of the presequence is essential for the import ability of the presequence, Tom20 recognizes only the amphiphilicity, but not the positive charges.