Results 11 to 20 of about 29,839 (226)

ATP-citrate lyase B (ACLB) negatively affects cell death and resistance to Verticillium wilt [PDF]

open access: yesBMC Plant Biology, 2022
Background ATP-citrate lyase (ACL) plays a pivotal role in histone acetylation and aerobic glycolysis. In plant, ACL is a heteromeric enzyme composed of ACLA (45 kD) and ACLB (65 kD).
Fujie Liu   +5 more
doaj   +2 more sources

Catalytic mechanism study of ATP-citrate lyase during citryl-CoA synthesis process [PDF]

open access: yesiScience
Summary: ATP-citrate lyase (ACLY) is a critical metabolic enzyme and promising target for drug development. The structure determinations of ACLY have revealed its homotetramer states with various subunit symmetries, but catalytic mechanism of ACLY ...
Danfeng Shi   +4 more
doaj   +2 more sources

Emerging roles of ATP citrate lyase in kidney diseases: from pathogenic driver to therapeutic target [PDF]

open access: yesRenal Failure
ATP-citrate lyase (ACLY) is a crucial cytosolic and nuclear enzyme that catalyzes the synthesis of acetyl-CoA from citrate, serving as a central metabolic node linking carbohydrate metabolism to de novo lipogenesis and histone acetylation.
Mengjiao Wei   +7 more
doaj   +2 more sources

Myeloid ATP Citrate Lyase Regulates Macrophage Inflammatory Responses In Vitro Without Altering Inflammatory Disease Outcomes [PDF]

open access: yesFrontiers in Immunology, 2021
Macrophages are highly plastic, key regulators of inflammation. Deregulation of macrophage activation can lead to excessive inflammation as seen in inflammatory disorders like atherosclerosis, obesity, multiple sclerosis and sepsis.
Sanne G. S. Verberk   +14 more
doaj   +2 more sources

The role of ATP citrate lyase, phosphoketolase, and malic enzyme in oleaginous Rhodotorula toruloides [PDF]

open access: yesApplied Microbiology and Biotechnology
Rhodotorula toruloides is an oleaginous yeast recognized for its robustness and the production of high content of neutral lipids. Early biochemical studies have linked ATP citrate lyase (ACL), phosphoketolase (PK), and cytosolic malic enzyme (cMAE) with ...
Alīna Reķēna   +3 more
doaj   +2 more sources

ATP citrate lyase inhibition can suppress tumor cell growth [PDF]

open access: yesCancer Cell, 2005
Many tumors display a high rate of glucose utilization, as evidenced by 18-F-2-deoxyglucose PET imaging. One potential advantage of catabolizing glucose through glycolysis at a rate that exceeds bioenergetic need is that the growing cell can redirect the excess glycolytic end product pyruvate toward lipid synthesis.
Hatzivassiliou, Georgia   +8 more
openaire   +4 more sources

Targeting ATP citrate lyase to reduce LDL cholesterol [PDF]

open access: yesNature Reviews Cardiology, 2019
Both pharmacological and genetic inhibition of ATP citrate lyase can reduce plasma LDL-cholesterol ...
openaire   +4 more sources

ATP-Citrate Lyase Supports Cardiac Function and NAD+/NADH Balance and Is Depressed in Human Failing Myocardium [PDF]

open access: yesJACC: Basic to Translational Science
Summary: ATP-citrate lyase (ACLY) regulates lipogenesis and cell proliferation, and forms a cytosolic TCA-bypass circuit impacting NADH. We show that acute and chronic ACLY inhibition in cardiomyocytes depresses the NAD+/NADH ratio by increasing ...
Mariam Meddeb, MD   +15 more
doaj   +2 more sources

ATP Citrate Lyase Improves Mitochondrial Function in Skeletal Muscle [PDF]

open access: yesCell Metabolism, 2015
Mitochondrial dysfunction is associated with skeletal muscle pathology, including cachexia, sarcopenia, and the muscular dystrophies. ATP citrate lyase (ACL) is a cytosolic enzyme that catalyzes mitochondria-derived citrate into oxaloacetate and acetyl-CoA.
Das, Suman   +8 more
openaire   +4 more sources

Molecular basis for acetyl-CoA production by ATP-citrate lyase. [PDF]

open access: yesNat Struct Mol Biol, 2020
ATP‐citrate lyase (ACLY) synthesizes cytosolic acetyl‐CoA, a fundamental cellular building block. Accordingly, aberrant ACLY activity is observed in many diseases. Here we report cryo‐EM structures of human ACLY alone or bound to substrates or products.
Wei X   +4 more
europepmc   +4 more sources

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