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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

TOM20 Tom20p

Tom20, MOM19
Top mentioned proteins: Tom22, Tom40, CAN, V1a, ACID
Papers using Tom20 antibodies
Structural basis for recruitment of mitochondrial fission complexes by Fis1
Mihara Katsuyoshi et al., In The Journal of Cell Biology, 2006
... ), Drp1, Opa1 (BD), Tom20 (Santa Cruz Biotechnology, Inc.), FLAG (M2; Sigma-Aldrich), ...
A novel insertion pathway of mitochondrial outer membrane proteins with multiple transmembrane segments
Mihara Katsuyoshi et al., In The Journal of Cell Biology, 2002
... Antibodies against HA (Covance), FLAG (M2; Sigma-Aldrich), Hsp60 (Assay Designs), mHsp70 (Assay Designs), Tom20 (Santa Cruz Biotechnology, Inc.), Tom22 (Sigma-Aldrich), Tim8 ...
tBID, a membrane-targeted death ligand, oligomerizes BAK to release cytochrome c
Virgin Skip, 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 ...
Syntabulin-mediated anterograde transport of mitochondria along neuronal processes
Sheng Zu-Hang et al., In The Journal of Cell Biology, 1998
... (BD Biosciences), and TOM20 (Santa Cruz Biotechnology, Inc.) ...
Papers on Tom20
Bax assembles into large ring-like structures remodeling the mitochondrial outer membrane in apoptosis.
Jakobs et al., Göttingen, Germany. In Embo J, Feb 2016
STED nanoscopy indicates that the area enclosed by a Bax ring is devoid of mitochondrial outer membrane proteins such as Tom20, Tom22, and Sam50.
Norcantharidin Inhibits SK-N-SH Neuroblastoma Cell Growth by Induction of Autophagy and Apoptosis.
Jiang et al., 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.
Rational design of crystal contact-free space in protein crystals for analyzing spatial distribution of motions within protein molecules.
Kohda et al., Fukuoka, Japan. In Protein Sci, Jan 2016
We applied the CCFS method to a highly mobile presequence peptide bound to the mitochondrial import receptor, Tom20, and a catalytically relevant flexible segment in the oligosaccharyltransferase, AglB.
Altered Mitochondrial Dynamics Contributes to Propofol-induced Cell Death in Human Stem Cell-derived Neurons.
Bai et al., Milwaukee, United States. In Anesthesiology, Nov 2015
Mitochondrial fission was assessed using TOM20 staining and electron microscopy.
Counteracting PINK/Parkin deficiency in the activation of mitophagy: a potential therapeutic intervention for Parkinson's Disease.
Ziviani et al., Padova, Italy. In Curr Neuropharmacol, Nov 2015
Mitochondrial outer membrane proteins Mitofusin (MFN), VDAC, Fis1 and TOM20 were found to be targets for Parkin mediated ubiquitination9-11.
Transgenic Zebrafish Expressing mCherry in the Mitochondria of Dopaminergic Neurons.
Ekker et al., Ottawa, Canada. In Zebrafish, Oct 2015
To visualize mitochondria in dopaminergic neurons of live zebrafish, we used the regulatory elements of the dopamine transporter (dat) gene to target a reporter, mCherry, after fusion with the mitochondrial localizing signal (MLS) of Tom20.
PINK1 and Parkin control localized translation of respiratory chain component mRNAs on mitochondria outer membrane.
Lu et al., Stanford, United States. In Cell Metab, Feb 2015
Translationally repressed nRCC mRNAs are localized in a PINK1/Tom20-dependent manner to mitochondrial outer membrane, where they are derepressed and activated by PINK1/Parkin through displacement of translation repressors, including Pumilio and Glorund/hnRNP-F, a Parkin substrate, and enhanced binding of activators such as eIF4G.
Glucose-induced regulation of protein import receptor Tom22 by cytosolic and mitochondria-bound kinases.
Meisinger et al., Freiburg, Germany. In Cell Metab, 2013
CK1 phosphorylates Tom22 at Thr57 and stimulates the assembly of Tom22 and Tom20.
Unique components of the plant mitochondrial protein import apparatus.
Whelan et al., 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).
Interaction between the human mitochondrial import receptors Tom20 and Tom70 in vitro suggests a chaperone displacement mechanism.
Young et al., Montréal, Canada. In J Biol Chem, 2011
a novel model in which Tom20 binds Tom70 to facilitate preprotein release from the chaperones by competition
Dual role of the receptor Tom20 in specificity and efficiency of protein import into mitochondria.
Endo et al., Nagoya, Japan. In Proc Natl Acad Sci U S A, 2011
Tom20 has a dual role in protein import into mitochondria: recognition of the targeting signal in the presequence and tethering the presequence to the TOM40 complex to increase import efficiency.
De novo synthesis of peroxisomes upon mitochondrial targeting of Pex3p.
Erdmann et al., Bochum, Germany. In Eur J Cell Biol, 2010
Pex3p was targeted to mitochondria by fusion with the mitochondrial targeting signal of Tom20p.
Tom20 mediates localization of mRNAs to mitochondria in a translation-dependent manner.
Arava et al., Haifa, Israel. In Mol Cell Biol, 2010
Our data reveal a large-scale mRNA association mode that involves interaction of Tom20p with the translated mitochondrial targeting sequence and may be assisted by Puf3p.
Structure, topology and function of the translocase of the outer membrane of mitochondria.
Gooley et al., Melbourne, Australia. In Plant Physiol Biochem, 2008
Recently, bioinformatic and structural analysis of Tom20, an important receptor subunit of the TOM complex, suggests that this protein complex arose from different ancestors for plants compared to animals and fungi, but has subsequently converged to provide similar functions and analogous structures.
The transmembrane segment of Tom20 is recognized by Mim1 for docking to the mitochondrial TOM complex.
Lithgow et al., Melbourne, Australia. In J Mol Biol, 2008
Study shows that the transmembrane segment of Tom20 contains critical residues essential for docking the Tom20 receptor into its correct environment within the TOM complex; the docking reaction is catalyzed by the unique assembly factor Mim1/Tom13.
Functions of outer membrane receptors in mitochondrial protein import.
Kohda et al., 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.
Structural basis of presequence recognition by the mitochondrial protein import receptor Tom20.
Kohda et al., Suita, Japan. In Cell, 2000
We report here the NMR structure of a general import receptor, rat Tom20, in a complex with a presequence peptide derived from rat aldehyde dehydrogenase.
The transport machinery for the import of preproteins across the outer mitochondrial membrane.
Pfanner et al., Freiburg, Germany. In Int J Biochem Cell Biol, 2000
The receptor proteins Tom70 and Tom20 associate with this complex in a weaker manner where they are involved in the initial recognition of preproteins.
Tom22 is a multifunctional organizer of the mitochondrial preprotein translocase.
Pfanner et al., Amsterdam, Netherlands. In Nature, 1999
The single membrane anchor of Tom22 is required for a stable interaction between the core complexes, whereas its cytosolic domain serves as docking point for the peripheral receptors Tom20 and Tom70.
Tom5 functionally links mitochondrial preprotein receptors to the general import pore.
Pfanner et al., Freiburg, Germany. In Nature, 1997
Tom20-Tom22 and Tom70-Tom37 function as import receptors with a preference for preproteins that have amino-terminal presequences or internal targeting information, respectively.
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