ArticleInternational journal of molecular sciences2009
The mitochondrial protein translocation motor: structural conservation between the human and yeast Tim14/Pam18-Tim16/Pam16 co-chaperones.
Article in International journal of molecular sciences, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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Who cites it
11 citing papers in PubMed, 20 citations in OpenAlex.
- Exploring the Shared Genetic Basis of Age at Menopause and Osteoarthritis.ACR open rheumatology · 2026Article
- Common and divergent pathways in early stages of glutamate and tau-mediated toxicities in neurodegeneration.Experimental neurology · 2024Article
- Interactions of amyloidogenic proteins with mitochondrial protein import machinery in aging-related neurodegenerative diseases.Frontiers in physiology · 2023Review
- Multiple variants of the human presequence translocase motor subunit Magmas govern the mitochondrial import.The Journal of biological chemistry · 2021Article
- Multi-layered molecular mechanisms of polypeptide holding, unfolding and disaggregation by HSP70/HSP110 chaperones.Frontiers in molecular biosciences · 2015Review
- The impairment of MAGMAS function in human is responsible for a severe skeletal dysplasia.PLoS genetics · 2014Article
- Comparative analysis of putative orthologues of mitochondrial import motor subunit: Pam18 and Pam16 in plants.PloS one · 2013Article
- Mortalin, apoptosis, and neurodegeneration.Biomolecules · 2012Article
- The yeast magmas ortholog pam16 has an essential function in fermentative growth that involves sphingolipid metabolism.PloS one · 2012Article
- The minimal proteome in the reduced mitochondrion of the parasitic protist Giardia intestinalis.PloS one · 2011Article
- Role of Magmas in protein transport and human mitochondria biogenesis.Human molecular genetics · 2010Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Most of our knowledge regarding the process of protein import into mitochondria has come from research employing Saccharomyces cerevisiae as a model system. Recently, several mammalian homologues of the mitochondrial motor proteins were identified. Of particular interest for us is the human Tim14/Pam18-Tim16/Pam16 complex. We chose a structural approach in order to examine the evolutionary conservation between yeast Tim14/Pam18-Tim16/Pam16 proteins and their human homologues. For this purpose, we examined the structural properties of the purified human proteins and their interaction with their yeast homologues, in vitro. Our results show that the soluble domains of the human Tim14/Pam18 and Tim16/Pam16 proteins interact with their yeast counterparts, forming heterodimeric complexes and that these complexes interact with yeast mtHsp70.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.