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"Charles Duncan may refer to: * Charles Duncan (stonemason) (1823–1891), Scottish-born Utah stonemason * Charles Duncan (politician) (1865–1933), British Labour Party politician and trade unionist, MP for Barrow-in-Furness and for Clay Cross * Charles Stafford Duncan (1892–1952), American painter * Charles K. Duncan (1911–1994), United States Navy admiral * Charles Duncan (British Army soldier) (1920–1943), British soldier posthumously awarded the George Cross * Charles Duncan Jr. (born 1926), U.S. Secretary of Energy for President Carter * Charlie Duncan (1889–?), Scottish footballer * Charles Duncan (artist) (1887–1970), American avant-garde painter * Charles T. Duncan (1838–1915), Virginia lawyer and state judge * Charles Duncan (captain) ( 1786–1789), British ship captain and maritime fur trader "
"Ti'julk Mr'asz, codename Gates, is a fictional character, a member of the Legion of Super-Heroes in the DC Universe. Like all natives of the planet Vyrga, Gates has a largely insectoid body. He is also noted for his strong political views, tending towards socialism. Fictional character biography Gates was the third non-biped member (after Quislet and Tellus) in the history of the Legion (the first after the 1994 Reboot). He was also unique amongst Legionnaires in being their only unwilling member, having been drafted by his planetary government to represent them in the Legion (which he perceived as being militaristic and inherently fascist). Apparently Gates is one of the very few free-thinkers on his homeworld; the rest are unindividualistic conformists. Gates has played key roles in many missions; his tactics enabled Star Boy to defeat Validus of the Fatal Five and he was able to resist the Emerald Eye's possession. Gates was part of the Legion team that was stranded in the 20th century for a time, where he came up with the strategy to defeat Mantis, and forged a close friendship with teammate Brainiac 5. Gates also joined Ultra Boy in helping out at soup kitchens during their stay. Like many of the Legionnaires that were original to the Post-Zero Hour continuity, Gates did not appear in the "Threeboot" continuity. Gates reappeared with his Legion in Final Crisis: Legion of 3 Worlds #2. In the later issues he shows disdain towards the Legion of New Earth for having few non-humanoid members. In #4, he is tasked with bringing the three versions of Brainiac 5 to the Fortress of Solitude, along with Light Lass. In #5, following the villains' defeat, Gates decided to remain with the pre-Crisis Legion. New 52 In The New 52 timeline, Gates made his first appearance in Legion Lost, where he and several other Legion of Super-Heroes members had become trapped in the 21st Century. He was thought killed in the time bubble/transporter accident that stranded the Legionnaires in the past,Legion Lost Vol.2 #1 but in fact survived, though physically damaged.Legion Lost Vol.2 #4 He and his teammates would reunited with their 31st Century comrades and, in another time travel adventure, encounter the present day Justice League United and together battle the cosmic threat Infinitus.Justice League United #6-10, Annual #1 Powers and abilities Gates has the ability to create glowing green, circular teleportation "gates", which people and objects can travel freely through to emerge from a partner gate at a location he himself defines mentally (it is also possible to make the trip in reverse, travelling from the partner gate to the original gate). Gates' "gates" have been shown to have sharp edges; he accidentally severed Ra's al Ghul's arm once while teleporting. Equipment As a member of the Legion of Super-Heroes he is provided a Legion Flight Ring. It allows him to fly and protects him from the vacuum of space and other dangerous environments. External links *A Hero History Of Gates References Category:DC Comics aliens Category:Extraterrestrial superheroes Category:DC Comics superheroes Category:Characters created by Mark Waid "
"Aldolase A (ALDOA, or ALDA), also known as fructose-bisphosphate aldolase, is an enzyme that in humans is encoded by the ALDOA gene on chromosome 16. The protein encoded by this gene is a glycolytic enzyme that catalyzes the reversible conversion of fructose-1,6-bisphosphate to glyceraldehyde 3-phosphate (G3P) and dihydroxyacetone phosphate (DHAP). Three aldolase isozymes (A, B, and C), encoded by three different genes, are differentially expressed during development. Aldolase A is found in the developing embryo and is produced in even greater amounts in adult muscle. Aldolase A expression is repressed in adult liver, kidney and intestine and similar to aldolase C levels in brain and other nervous tissue. Aldolase A deficiency has been associated with myopathy and hemolytic anemia. Alternative splicing and alternative promoter usage results in multiple transcript variants. Related pseudogenes have been identified on chromosomes 3 and 10. [provided by RefSeq, Aug 2011] Structure ALDOA is a homotetramer and one of the three aldolase isozymes (A, B, and C), encoded by three different genes. The ALDOA gene contains 8 exons and the 5' UTR IB. Key amino acids responsible for its catalytic function have been identified. The residue Tyr363 functions as the acid–base catalyst for protonating C3 of the substrate, while Lys146 is proposed to stabilize the negative charge of the resulting conjugate base of Tyr363 and the strained configuration of the C-terminal. Residue Glu187 participates in multiple functions, including FBP aldolase catalysis, acid–base catalysis during substrate binding, dehydration, and substrate cleavage. Though ALDOA localizes to the nucleus, it lacks any known nuclear localization signals (NLS). Mechanism In mammalian aldolase, the key catalytic amino acid residues involved in the reaction are lysine and tyrosine. The tyrosine acts as an efficient hydrogen acceptor while the lysine covalently binds and stabilizes the intermediates. Many bacteria use two magnesium ions in place of the lysine. {The reaction mechanism of aldolase. The enzyme's reactive site amino acid's side-chains are shown in blue. Abbreviations: DHAP - dihydroxyacetone phosphate; Fru1,6bP - Fructose-1,6-bisphosphate; GAD - glyceraldehyde 3-phosphate; } The numbering of the carbon atoms indicates the fate of the carbons according to their position in fructose 6-phosphate. Function ALDOA is a key enzyme in the fourth step of glycolysis, as well as in the reverse pathway gluconeogenesis. It catalyzes the reversible conversion of fructose-1,6-bisphosphate to glyceraldehydes-3-phosphate and dihydroxyacetone phosphate by aldol cleavage of the C3–C4 bond. As a result, it is a crucial player in ATP biosynthesis. ALDOA also contributes to other "moonlighting" functions such as muscle maintenance, regulation of cell shape and motility, striated muscle contraction, actin cytoskeleton organization, and regulation of cell proliferation. ALDOA likely regulates actin cytoskeleton remodeling through interacting with cytohesin-2 (ARNO) and Arf6. ALDOA is ubiquitously expressed in most tissues, though it is predominantly expressed in developing embryo and adult muscle. In lymphocytes, ALDOA is the predominant aldolase isoform. Within the cell, ALDOA typically localizes to the cytoplasm, but it can localize to the nucleus during DNA synthesis of the cell cycle S phase. This nuclear localization is regulated by the protein kinases AKT and p38. It is suggested that the nucleus serves as a reservoir for ALDOA in low glucose conditions. ALDOA has also been found in mitochondria. ALDOA is regulated by the energy metabolism substrates glucose, lactate, and glutamine. In human mast cells (MCs), ALDOA has been observed to undergo post-translational regulation by protein tyrosine nitration, which may alter its relative affinity for FBP and/or IP3. This change then affects IP3 and PLC signaling cascades in IgE-dependent responses. Clinical significance Aldolase A (ALDOA) is a highly expressed in multiple cancers, including lung squamous cell carcinoma (LSCC), renal cancer, and hepatocellular carcinoma. It is proposed that ALDOA overexpression enhances glycolysis in these tumor cells, promoting their growth. In LSCC, its upregulation correlates with metastasis and poor prognosis, while its downregulation reduces tumor cell motility and tumorigenesis. Thus, ALDOA could be a potential LSCC biomarker and therapeutic drug target. Aldolase A deficiency is a rare, autosomal recessive disorder that is linked to hemolysis and accompanied by weakness, muscle pain, and myopathy. Interactive pathway mapInteractions Aldolase A has been shown to interact with: *PLD2, *actin, *GLUT4, *phospholipase D2, *light chain 8 of dynein, *erythrocyte anion exchanger Band 3 protein, *ryanodine receptor, *Cytohesin-2, and *V-ATPase (vacuolar-type H+-ATPase). See also *ALDOB *ALDOC *Fructose-bisphosphate aldolase ReferencesFurther reading * * External links * http://pdbdev.sdsc.edu:48346/pdb/molecules/pdb50_5.html * * PDBe-KB provides an overview of all the structure information available in the PDB for Human Fructose-bisphosphate aldolase A Category:Enzymes "