Dewar et al., 2022 - Google Patents
Mistargeting of aggregation prone mitochondrial proteins activates a nucleus-mediated posttranscriptional quality control pathway in trypanosomesDewar et al., 2022
View HTML- Document ID
- 4762532226040726501
- Author
- Dewar C
- Oeljeklaus S
- Mani J
- Mühlhäuser W
- von Känel C
- Zimmermann J
- Ochsenreiter T
- Warscheid B
- Schneider A
- Publication year
- Publication venue
- Nature Communications
External Links
Snippet
Mitochondrial protein import in the parasitic protozoan Trypanosoma brucei is mediated by the atypical outer membrane translocase, ATOM. It consists of seven subunits including ATOM69, the import receptor for hydrophobic proteins. Ablation of ATOM69, but not of any …
- 230000037361 pathway 0 title abstract description 69
Classifications
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by the preceding groups
- G01N33/48—Investigating or analysing materials by specific methods not covered by the preceding groups biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/5005—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving human or animal cells
- G01N33/5008—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving human or animal cells for testing or evaluating the effect of chemical or biological compounds, e.g. drugs, cosmetics
- G01N33/502—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving human or animal cells for testing or evaluating the effect of chemical or biological compounds, e.g. drugs, cosmetics for testing non-proliferative effects
- G01N33/5023—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving human or animal cells for testing or evaluating the effect of chemical or biological compounds, e.g. drugs, cosmetics for testing non-proliferative effects on expression patterns
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by the preceding groups
- G01N33/48—Investigating or analysing materials by specific methods not covered by the preceding groups biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/68—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids
- G01N33/6803—General methods of protein analysis not limited to specific proteins or families of proteins
- G01N33/6842—Proteomic analysis of subsets of protein mixtures with reduced complexity, e.g. membrane proteins, phosphoproteins, organelle proteins
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by the preceding groups
- G01N33/48—Investigating or analysing materials by specific methods not covered by the preceding groups biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/53—Immunoassay; Biospecific binding assay
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N2333/00—Assays involving biological materials from specific organisms or of a specific nature
- G01N2333/90—Enzymes; Proenzymes
- G01N2333/914—Hydrolases (3)
- G01N2333/978—Hydrolases (3) acting on carbon to nitrogen bonds other than peptide bonds (3.5)
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N2500/00—Screening for compounds of potential therapeutic value
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N2800/00—Detection or diagnosis of diseases
Similar Documents
Publication | Publication Date | Title |
---|---|---|
Kim et al. | The mitochondrial-encoded peptide MOTS-c translocates to the nucleus to regulate nuclear gene expression in response to metabolic stress | |
Chu et al. | Regulation of the ER stress response by a mitochondrial microprotein | |
Heidelberger et al. | Proteomic profiling of VCP substrates links VCP to K6‐linked ubiquitylation and c‐Myc function | |
Itakura et al. | Ubiquilins chaperone and triage mitochondrial membrane proteins for degradation | |
McShane et al. | Kinetic analysis of protein stability reveals age-dependent degradation | |
Thorslund et al. | Histone H1 couples initiation and amplification of ubiquitin signalling after DNA damage | |
Abeliovich et al. | Involvement of mitochondrial dynamics in the segregation of mitochondrial matrix proteins during stationary phase mitophagy | |
Hendriks et al. | System-wide identification of wild-type SUMO-2 conjugation sites | |
Mick et al. | MITRAC links mitochondrial protein translocation to respiratory-chain assembly and translational regulation | |
Matic et al. | Site-specific identification of SUMO-2 targets in cells reveals an inverted SUMOylation motif and a hydrophobic cluster SUMOylation motif | |
Beckmann et al. | The RNA-binding proteomes from yeast to man harbour conserved enigmRBPs | |
Lang et al. | Dynamic changes in the mouse skeletal muscle proteome during denervation-induced atrophy | |
Wreden et al. | Varied Mechanisms Underlie the Free Sialic Acid Storage Disorders*♦ | |
Ward et al. | Accumulation of checkpoint protein 53BP1 at DNA breaks involves its binding to phosphorylated histone H2AX | |
McKittrick et al. | Histone H3. 3 is enriched in covalent modifications associated with active chromatin | |
Klein et al. | The mitochondrial amidoxime-reducing component (mARC1) is a novel signal-anchored protein of the outer mitochondrial membrane | |
Weinert et al. | Proteome-wide mapping of the Drosophila acetylome demonstrates a high degree of conservation of lysine acetylation | |
Tan et al. | SCFFBXO22 regulates histone H3 lysine 9 and 36 methylation levels by targeting histone demethylase KDM4A for ubiquitin-mediated proteasomal degradation | |
Madsen et al. | Biotin starvation causes mitochondrial protein hyperacetylation and partial rescue by the SIRT3-like deacetylase Hst4p | |
Linster et al. | Cotranslational N-degron masking by acetylation promotes proteome stability in plants | |
Dewar et al. | Mistargeting of aggregation prone mitochondrial proteins activates a nucleus-mediated posttranscriptional quality control pathway in trypanosomes | |
LaLonde et al. | The UBX protein SAKS1 negatively regulates endoplasmic reticulum-associated degradation and p97-dependent degradation | |
Makiuchi et al. | Novel TPR-containing subunit of TOM complex functions as cytosolic receptor for Entamoeba mitosomal transport | |
Zoltner et al. | Modulation of the surface proteome through multiple ubiquitylation pathways in African trypanosomes | |
Singh et al. | Identification of the proteome complement of humanTLK1 reveals it binds and phosphorylates NEK1 regulating its activity |