Results 121 to 130 of about 3,813 (143)

<i>MTAP</i> Deletion as a Therapeutic Vulnerability in Cancer: From Molecular Mechanism to Clinical Targeting. [PDF]

Int J Mol Sci
Krawczyk P, Wojas-Krawczyk K.
europepmc   +1 more source

MTAP-Null Tumors: A Comprehensive Review on Synthetic Vulnerabilities and Therapeutic Strategies. [PDF]

Cells
Subramaniam B, Chong WC, Babaei A, Bornhorst M, Zhang C, Packer R, Nazarian J.   +6 more
europepmc   +1 more source

The Double-Edged Nature of Methyl Donors in Cancer Development from Prevention to Progression. [PDF]

Int J Mol Sci
Pan D, Wang S, Sun G.
europepmc   +1 more source

Redox metabolism in cell senescence: focusing on contributions from the metabolomic field. [PDF]

Front Mol Biosci
Chacón E, Grünwaldt G, Marmisolle I, Martínez J, Quijano C.   +4 more
europepmc   +1 more source

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Radiosensitivity of ATP:l-methionine S-adenosyltransferase

Experientia, 1972
In vitro-Nachweis, dass S-Adenosyltransferase der Mauseleber gegen Rontgenstrahlen bis zu 10 kR Starke widerstandsfahig ist und weniger empfindlich als Citidylat-Kinase.
R L, Hancock, R E, Giblak
  +7 more sources

Abnormal methionine adenosyltransferase in hypermethioninemia

Biochemical and Biophysical Research Communications, 1975
Abstract Methionine adenosyltransferase activity was reduced in liver from a child with hypermethioninemia. Kinetic studies demonstrated a pattern suggesting negative cooperativity for enzyme derived from rat and human liver. The patient's enzyme was characterized by a decrease in the apparent maximum Km(met).
J D, Finkelstein, W E, Kyle, J J, Martin
openaire   +2 more sources

Methionine adenosyltransferase: Structure and function

Pharmacology & Therapeutics, 1993
Methionine adenosyltransferase (MAT), a key enzyme in metabolism, catalyzes the synthesis of one of the most important and pivotal biological molecules, S-adenosyl-methionine. In every organism studied thus far, MAT exists in multiple forms; most are encoded by related, but distinct genes.
M, Kotb, A M, Geller
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Inhibition of Methionine Adenosyltransferase by the Polyamines

Archives of Biochemistry and Biophysics, 1997
The effect of the polyamines, putrescine, spermine, and spermidine, on the activity of extrahepatic methionine adenosyltransferase (MAT II) was studied. The polyamines inhibited MAT II activity at concentrations equal to or greater than 5 mm. Combinations of polyamines were more effective than individual polyamines in inhibiting MAT activity; maximum ...
A M, Geller, H L, Legros, K, Wherry, M Y, Kotb   +3 more
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Chemotherapeutic potential of methionine analogue inhibitors of tumor-derived methionine adenosyltransferases

Biochemical Pharmacology, 1983
Two isozymes of ATP:L-methionine S-adenosyltransferase (MAT) were fractionated from rat Novikoff solid hepatoma. Their Km values for L-methionine and/or their inhibition constants for various L-methionine analogues were significantly different from the kinetic constants obtained for three isozymes fractionated from normal rat liver.
J B, Lombardini, J R, Sufrin
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Molecular genetics of hepatic methionine adenosyltransferase deficiency

Pharmacology & Therapeutics, 2000
Hepatic methionine adenosyltransferase (MAT) deficiency is caused by mutations in the human MAT1A gene that abolish or reduce hepatic MAT activity that catalyzes the synthesis of S-adenosylmethionine from methionine and ATP. This genetic disorder is characterized by isolated persistent hypermethioninemia in the absence of cystathionine beta-synthase ...
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