Sort   by:  
 Page size 
ProteomicsModelling mitochondrial SAM depletion in fruit flies and mice
S-adenosylmethionine (SAM) is the principle biological methyl group donor for a diverse range of substrates. It is synthesised in the cytosolic methionine cycle and shuttled throughout the cell. The mitochondrial SAM (mitoSAM) pool depends on import through the inner-membrane SAMC and supports the m...
ORGANISM(S): Mus musculus (Mouse) Drosophila melanogaster (Fruit fly) 
2021-02-22 | PXD019550 | Pride
Metabolism Methylation Mitochondria Sam 
ProteomicsA patient-based Drosophila model for mitochondrial S-Adenosylhomocysteine transport deficiency
The SLC25A26 gene encodes a mitochondrial inner membrane carrier that transports S-adenosylmethionine (SAM) into the mitochondrial matrix in exchange for S-adenosylhomocysteine (SAH). SAM is the predominant methyl-group donor for most cellular methylation processes, of which SAH is produced as a by-...
ORGANISM(S): Drosophila melanogaster (Fruit fly) 
2022-01-19 | PXD026900 | Pride
Sam Samc Methylation Sah Mitochondria Drosophila Slc25a26 
ProteomicsLoss of the Mitochondrial SAM Transporter Reveals a Lipoylation-Dependent Metabolic Vulnerability in the Postnatal Heart
SLC25A26 encodes the sole mitochondrial S-adenosylmethionine carrier (SAMC). Inside mitochondria, SAM functions as a methyl group donor for various methyltransferases and as a substrate for radical SAM enzymes. Variants in SAMC are associated with mitochondrial disease, and we previously demonstrate...
ORGANISM(S): Mus musculus (Mouse) 
2026-07-03 | PXD050486 | Pride
ProteomicsThe mitochondrial methylome is evolutionary conserved and regulated by cytosolic SAM
S-adenosylmethionine (SAM) is the principle biological methyl group donor for a diverse range of substrates. It is synthesised in the cytosolic methionine cycle and shuttled throughout the cell. The mitochondrial SAM (mitoSAM) pool depends on import through the inner-membrane SAMC and supports the m...
ORGANISM(S): Mus musculus (Mouse) Homo sapiens (Human) Drosophila melanogaster (Fruit fly) 
2021-02-22 | PXD019494 | Pride
Mitochondria Prm Human Mouse Methylation Drosophila 
ProteomicsThe mitochondrial methylation potential gates early and late ribosome assembly
S-adenosylmethionine (SAM) is the principal methyl group donor of the cell, required to modify various molecules, including DNA, RNA and proteins. Inside mitochondria, SAM is associated with several steps of mitochondrial gene expression. However, the exact role and significance of these modificatio...
ORGANISM(S): Mus musculus (Mouse) 
2025-05-19 | PXD055907 | Pride
Sam Rna processing Elac2 Methylation Rnasep Mitochondrial ribosome Mitochondrial translation S-adenosylmethionine Samc Rnasez Adomet Slc25a26 
ProteomicsMethyl-SILAF mapping of the Drosophila mitochondrial protein methylome
S-adenosylmethionine (SAM) is the principal biological methyl group donor for a diverse range of substrates. It is synthesised in the cytosolic methionine cycle and shuttled throughout the cell. The mitochondrial SAM (mitoSAM) pool depends on import through the inner-membrane S-adenosylmethionine ca...
ORGANISM(S): Drosophila melanogaster (Fruit fly) 
2021-02-21 | PXD019654 | Pride
Ptm Mitochondria Methylation Drosophila 
ProteomicsThe mitochondrial methylation potential gates early and late ribosome assembly
S-adenosylmethionine (SAM) is the principal methyl group donor of the cell, required to modify various molecules, including DNA, RNA and proteins. Inside mitochondria, SAM is associated with several steps of mitochondrial gene expression. However, the exact role and significance of these modificatio...
ORGANISM(S): Mus musculus (Mouse) 
2025-05-19 | PXD062614 | Pride
Methylation Elac2 Oxford nanopore sequencing S-adenosylmethionine Rnase p Samc Adomet Slc25a26 Direct long-range rna sequencing Sam Rna processing Mitochondrial ribosome Rnase z Mitochondrial translation 
Unknown8-Cl-Ado and 8-NH<sub>2</sub>-Ado synergize with venetoclax to target the methionine-MAT2A-SAM axis in acute myeloid leukemia.
Not available
S-EPMC11147765 | biostudies-literature
UnknownS-Adenosyl-L-methionine hydrolase (adenosine-forming), a conserved bacterial and archaeal protein related to SAM-dependent halogenases.
Not available
S-EPMC2692205 | biostudies-literature
UnknownDiscovery and characterization of a marine bacterial SAM-dependent chlorinase.
Not available
S-EPMC2762381 | biostudies-literature
Sort   by:  
 Page size