Results 61 to 70 of about 3,903 (108)

RNA-mediated inhibition of mitochondrial SHMT2 impairs cancer cell proliferation. [PDF]

Cell Death Discov
Liberati FR, Spizzichino S, Di Russo S, Borsatti GE, Riva A, Magnifico MC, Bouzidi A, Giardina G, Arese M, Scribani Rossi C, Boi D, Boumis G, Di Fonzo F, Guarguaglini G, Contestabile R, Tramonti A, Macone A, Paiardini A, Rinaldo S, Paone A, Cutruzzolà F.   +20 more
europepmc   +1 more source

Mitochondrial one-carbon metabolism is required for TGF-β-induced glycine synthesis and fibrotic responses. [PDF]

Nat Commun
Meliton AY, Shin KWD, Cetin-Atalay R, Atalay MV, Tian Y, Houpy Szafran JC, Cho T, Sun KA, Woods PS, Shamaa OR, Chen B, Dulin NO, Husain AN, Muir A, Shah H, Mutlu GM, Hamanaka RB.   +16 more
europepmc   +1 more source

Upregulated Expression of SHMT2 Predicts Poor Survival of Lung Adenocarcinoma. [PDF]

Genet Res (Camb)
Guo Q, Huang GH, Chen P, Guo C.
europepmc   +1 more source

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Glycine consumption and mitochondrial serine hydroxymethyltransferase in cancer cells: The heme connection

Medical Hypotheses, 2013
It was recently discovered that glycine consumption is strongly related to the rate of proliferation across cancer cells. This is very intriguing and raises the question of what is the actual role of this amino acid in cancer metabolism. Cancer cells are greedy for glycine.
DI SALVO, Martino Luigi, CONTESTABILE, Roberto, PAIARDINI, ALESSANDRO, MARAS, Bruno   +3 more
openaire   +3 more sources

POSTNATAL CHANGES IN THE LEVELS OF GLYCINE AND THE ACTIVITIES OF SERINE HYDROXYMETHYLTRANSFERASE AND GLYCINE: 2‐OXOGLUTARATE AMINOTRANSFERASE IN THE RAT CENTRAL NERVOUS SYSTEM

Journal of Neurochemistry, 1974
Abstract— Of the amino acids found in the CNS of 10‐day‐old rats the concentration of glycine alone was significantly higher in the spinal cord than in all other regions. Spinal levels of glycine, cystathionine, isoleucine and lysine from 1‐ and 10‐day‐old rats did not differ significantly from adult values, whereas the levels of most other amino acids,
L P, Davies, G A, Johnston
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Effect of methionine, glycine and serine on serine hydroxymethyltransferase activity in rat glioma and human neuroblastoma cells

Journal of Neuroscience Research, 1980
AbstractHuman neuroblastoma SK‐N‐SH‐SY5Y (5Y) and rat glioma (C6) cells were cultured with supplemental methionine, glycine, or serine for three to six days. Serine hydroxmethyltransferase (SHMT: L‐serine: tetrahydrofolate 5, 10‐hydroxymethyltransferase, EC 2.12.1) was assayed radiometrically in whole cell homogenates, crude supernatant fractions and ...
R L, Kohl, J R, Perez-Polo, W B, Quay
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DISTRIBUTION OF SERINE HYDROXYMETHYLTRANSFERASE AND GLYCINE TRANSAMINASE IN SEVERAL AREAS OF THE CENTRAL NERVOUS SYSTEM OF THE RAT

Journal of Neurochemistry, 1974
Abstract—The regional distributions of serine hydroxymethyltransferase (SHMT) and glycine transaminase (GT) have been determined in five areas of the CNS of the rat. The SHMT activity per mg protein varied in these areas in the following order: medulia‐pons and spinal cord > cerebellum > midbrain > telencephalon. The GT activity per mg protein
E C, Daly, M H, Aprison
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Mechanism of the glycine cleavage reaction: Retention of C-2 hydrogens of glycine on the intermediate attached to H-protein and evidence for the inability of serine hydroxymethyltransferase to catalyze the glycine decarboxylation

Archives of Biochemistry and Biophysics, 1986
Glycine is converted to carbon dioxide and an intermediate attached to a lipoic acid group on H-protein in the P-protein-catalyzed partial reaction of the glycine cleavage reaction [K. Fujiwara and Y. Motokawa (1983) J. Biol. Chem. 258, 8156-8162]. The results presented in this paper indicate that the decarboxylation is not accompanied by the removal ...
K, Fujiwara, K, Okamura-Ikeda, Y, Ohmura, Y, Motokawa   +3 more
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Effects of glycine and serine on serine hydroxymethyltransferase levels in logarithmic cultures ofNeurospora crassa wild type andSer-1 mutant

Experientia, 1973
Dans un milieu minimal la glycine et la serine, ajoutees en concentrations physiologiques, augmentent le taux de la serine-hydroxymethyltransferase durant la croissance logarithmique duNeurospora crassa. La glycine influence egalement la synthese de cet enzyme chez le mutantSer-1 deNeurospora. Ainsi la glycine exogene exerce une regulation de la serine-
E A, Cossins, G, Combepine, G, Turian
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The organisation and expression of the genes encoding the mitochondrial glycine decarboxylase complex and serine hydroxymethyltransferase in pea (Pisum sativum)

Molecular and General Genetics MGG, 1993
Restriction fragment length polymorphisms have been used to determine the chromosomal location of the genes encoding the glycine decarboxylase complex (GDC) and serine hydroxymethyltransferase (SHMT) of pea leaf mitochondria. The genes encoding the H subunit of GDC and the genes encoding SHMT both show linkage to the classical group I marker i.
Turner, S.R., Hellens, R.P., Ireland, R., Ellis, N., Rawsthorne, S.   +4 more
openaire   +3 more sources