Functional organization of mammalian hexokinases: both N- and C-terminal halves of the rat type II isozyme possess catalytic sites
about
Structure of the human hexokinase type I gene and nucleotide sequence of the 5' flanking regionHexokinase II: cancer's double-edged sword acting as both facilitator and gatekeeper of malignancy when bound to mitochondriaHexokinase-2 bound to mitochondria: cancer's stygian link to the "Warburg Effect" and a pivotal target for effective therapyMichaelis and Menten and the long road to the discovery of cooperativityThe structure of mammalian hexokinase-1Sequence analysis and molecular characterization of Clonorchis sinensis hexokinase, an unusual trimeric 50-kDa glucose-6-phosphate-sensitive allosteric enzymeKinetic studies of rat liver hexokinase D ('glucokinase') in non-co-operative conditions show an ordered mechanism with MgADP as the last product to be releasedReprogramming glucose metabolism in cancer: can it be exploited for cancer therapy?Molecular evolution of dinoflagellate luciferases, enzymes with three catalytic domains in a single polypeptide.Hexokinase II integrates energy metabolism and cellular protection: Akting on mitochondria and TORCing to autophagy.Mitochondrial hexokinase II (HKII) and phosphoprotein enriched in astrocytes (PEA15) form a molecular switch governing cellular fate depending on the metabolic state.Anticancer agents that counteract tumor glycolysis.Evolution of glucose utilization: glucokinase and glucokinase regulator protein.The pivotal roles of mitochondria in cancer: Warburg and beyond and encouraging prospects for effective therapies.The anticancer agent 3-bromopyruvate: a simple but powerful molecule taken from the lab to the bedside.Identification of a mitochondrial-binding site on the N-terminal end of hexokinase IIThe cytotoxicity of 3-bromopyruvate in breast cancer cells depends on extracellular pH.miR-143 regulates hexokinase 2 expression in cancer cells.The roles of glycine residues in the ATP binding site of human brain hexokinase.Amino acid sequence homology between N- and C-terminal halves of a carbonic anhydrase in Porphyridium purpureum, as deduced from the cloned cDNA.The overexpressed hexahistidine-tagged human hexokinase type III is inhibited by D-glucose.HOTAIR regulates HK2 expression by binding endogenous miR-125 and miR-143 in oesophageal squamous cell carcinoma progression.Intracellular Energy-Transfer Networks and High-Resolution Respirometry: A Convenient Approach for Studying Their Function
P2860
Q24530756-3F026517-EF58-448A-BAD9-33F2D46F1B6BQ24595940-9E5DFA0E-32A7-4027-8D14-97DFAC4A793CQ24646296-E16DF2D5-C00C-4275-B17A-A8459C1E3DE4Q27027225-E1436C3A-E88D-4CF3-82CB-D0EB18794ED6Q27764574-A5C16AAA-A9C2-4D2F-ADCB-D47C047B2B3EQ28543067-708F6FE4-8A83-4E34-817B-29BB610C1969Q28577278-1B3D3F64-5358-4DFB-89DA-34FD4029BC91Q33917658-68724E4E-EB33-43BD-B41B-60CCB645E4C4Q34368068-4055EACC-15B0-4824-A2E8-6A4B5F5F2D1EQ34924245-B0E17533-6ECE-41A1-B58F-2AFC865A4899Q35749617-1B9F1D58-D19A-4A65-AF58-A4C6A4A096F0Q36452381-B6527DD4-B363-4594-8166-967BDF678577Q37499429-A3D17C14-2C2A-49E8-92A4-EF17507CA423Q37728362-FEACF4FD-3E52-4FC6-9A1B-C4894A28CF48Q38837920-C132149C-3DA2-44F2-88D5-849B5B50C04EQ38852217-832DFFAE-BC7A-41D3-A250-BDE7A2BA02DAQ38914134-3B5E034F-A4E0-4F0C-962C-88829BEEA747Q39370392-4E0043E5-BB1A-4A35-80C0-2E5840B0F958Q39450991-BC425F00-4C56-4034-9E28-23FB964B2978Q42643523-7A0DF2C9-8C46-4964-B9B6-9B529E82145AQ44232161-E1DED49B-8A52-42DC-ACD8-F7468CC695AEQ45760903-195A8E80-D8EC-43E1-A4B2-17DB55417337Q59138361-774943D9-FFA8-4D7E-B034-125C12788E71
P2860
Functional organization of mammalian hexokinases: both N- and C-terminal halves of the rat type II isozyme possess catalytic sites
description
1996 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի մայիսին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 1996
@ast
im Mai 1996 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 1996/05/01)
@sk
vědecký článek publikovaný v roce 1996
@cs
wetenschappelijk artikel (gepubliceerd op 1996/05/01)
@nl
наукова стаття, опублікована в травні 1996
@uk
مقالة علمية (نشرت في مايو 1996)
@ar
name
Functional organization of mam ...... sozyme possess catalytic sites
@ast
Functional organization of mam ...... sozyme possess catalytic sites
@en
Functional organization of mam ...... sozyme possess catalytic sites
@nl
type
label
Functional organization of mam ...... sozyme possess catalytic sites
@ast
Functional organization of mam ...... sozyme possess catalytic sites
@en
Functional organization of mam ...... sozyme possess catalytic sites
@nl
prefLabel
Functional organization of mam ...... sozyme possess catalytic sites
@ast
Functional organization of mam ...... sozyme possess catalytic sites
@en
Functional organization of mam ...... sozyme possess catalytic sites
@nl
P356
P1476
Functional organization of mam ...... sozyme possess catalytic sites
@en
P2093
H. J. Tsai
J. E. Wilson
P356
10.1006/ABBI.1996.0186
P407
P577
1996-05-01T00:00:00Z