Characterization of a glucose-repressed pyruvate kinase (Pyk2p) in Saccharomyces cerevisiae that is catalytically insensitive to fructose-1,6-bisphosphate
about
Warburg effect and translocation-induced genomic instability: two yeast models for cancer cellsHuman pyruvate kinase M2: a multifunctional proteinDifferential behavior of missense mutations in the intersubunit contact domain of the human pyruvate kinase M2 isozymeThe metabolism beyond programmed cell death in yeastYeast Nap1-binding protein Nbp2p is required for mitotic growth at high temperatures and for cell wall integrityThe Saccharomyces cerevisiae ICL2 gene encodes a mitochondrial 2-methylisocitrate lyase involved in propionyl-coenzyme A metabolism.Identification and characterization of MAE1, the Saccharomyces cerevisiae structural gene encoding mitochondrial malic enzymeRedox-dependent Regulation of Gluconeogenesis by a Novel Mechanism Mediated by a Peroxidatic Cysteine of Peroxiredoxin.In vivo and in vitro phosphorylation of two isoforms of yeast pyruvate kinase by protein kinase A.Transcriptional analysis of Kluyveromyces marxianus for ethanol production from inulin using consolidated bioprocessing technologyIncreased glycolytic flux as an outcome of whole-genome duplication in yeastFunctional partitioning of yeast co-expression networks after genome duplicationRegulation of SESAME-mediated H3T11 phosphorylation by glycolytic enzymes and metabolites.Effect of the cancer specific shorter form of human 6-phosphofructo-1-kinase on the metabolism of the yeast Saccharomyces cerevisiae.Pyruvate kinase triggers a metabolic feedback loop that controls redox metabolism in respiring cellsComparative proteome analysis of Saccharomyces cerevisiae: a global overview of in vivo targets of the yeast activator protein 1.Quercetin protects Saccharomyces cerevisiae against oxidative stress by inducing trehalose biosynthesis and the cell wall integrity pathwayComparative analysis indicates regulatory neofunctionalization of yeast duplicates.A Minimal Set of Glycolytic Genes Reveals Strong Redundancies in Saccharomyces cerevisiae Central Metabolism.Homeostasis and the glycogen shunt explains aerobic ethanol production in yeast.A novel pyruvate kinase and its application in lactic acid production under oxygen deprivation in Corynebacterium glutamicum.Increased rates of protein evolution and asymmetric deceleration after the whole-genome duplication in yeasts.Patterns of Gene Conversion in Duplicated Yeast Histones Suggest Strong Selection on a Coadapted Macromolecular Complex.Functioning of a metabolic flux sensor in Escherichia coli.Yeast and cancer cells - common principles in lipid metabolism.Redirection of pyruvate flux toward desired metabolic pathways through substrate channeling between pyruvate kinase and pyruvate-converting enzymes in Saccharomyces cerevisiae.Mistranslation-induced protein misfolding as a dominant constraint on coding-sequence evolution.PKM2 regulates chromosome segregation and mitosis progression of tumor cells.Multi-tasking of biosynthetic and energetic functions of glycolysis explained by supply and demand logic.The effect of selenium enrichment on baker's yeast proteomeAbsolute quantification of the glycolytic pathway in yeast: deployment of a complete QconCAT approach.Development of a D-xylose fermenting and inhibitor tolerant industrial Saccharomyces cerevisiae strain with high performance in lignocellulose hydrolysates using metabolic and evolutionary engineering.In silico evidence for functional specialization after genome duplication in yeast.Regulation of yeast pyruvate kinase by ultrasensitive allostery independent of phosphorylation.Phosphoenolpyruvate carboxykinase as the sole anaplerotic enzyme in Saccharomyces cerevisiaeScreening the yeast genome for energetic metabolism pathways involved in a phenotypic response to the anti-cancer agent 3-bromopyruvate.Pyruvate kinase is a dosage-dependent regulator of cellular amino acid homeostasis.Glycolytic Functions Are Conserved in the Genome of the Wine Yeast Hanseniaspora uvarum, and Pyruvate Kinase Limits Its Capacity for Alcoholic Fermentation.Flux Control in Glycolysis Varies Across the Tree of Life.Reversible protein aggregation is a protective mechanism to ensure cell cycle restart after stress.
P2860
Q21129304-94F00E1D-7E49-464B-8599-01196307302FQ24625882-C7B7267B-0B6D-4EAE-BB26-C91D39EBB4E3Q24654900-212DD913-8BC4-4B66-9730-DFECC196BB16Q26853012-BFFED694-7E5E-4D0A-9B82-6B723DA43F66Q27933802-C3721FBE-BB71-4DBF-B797-781ACF5CE683Q27935724-3682A0FB-8BAC-4E5A-AF37-2B5B47C96B75Q27936875-B7202B76-AE8E-47B5-95E9-24E186D11687Q27939275-C16E5B8C-F3B5-4A4B-88CD-285460E9D3DFQ27939476-0EABC13B-6E16-4EB9-B536-EDE0F0F095D6Q28611221-AE826350-4A50-47EC-8AFC-C8DDEE89CEF5Q28757241-D23EACF1-1670-4BF1-8ECB-D44BF9AB003AQ33237358-F92BCDFC-6D7C-4122-9D70-163E28E5CEEDQ33584813-8D80B2D4-5B99-4897-ACD2-04755F7480FCQ33651252-3EC2EE1E-1038-4869-8B22-CEB76B70BD51Q34215123-0B639612-F3DB-4A63-A934-2F261C4D861EQ34297831-610C50E0-6F2A-4552-A70E-D9BBDFA6F23BQ34429215-16A4DA27-AF72-4BCC-8AE1-06FA328A1D0CQ35850302-49865C6E-5EDE-47AC-835F-DA40731143F2Q35902090-07243F7D-62FE-4AEA-9204-2F5840785335Q36055665-B6A45745-F715-412E-9052-8FCCFE10879DQ36194501-80EDE07B-569F-46BA-9771-F7E057051D05Q36271937-079AB992-237F-4C69-B2F1-AE2E937B0F88Q36429411-517A9890-8367-4CBE-8D1D-B1361A995C65Q36545591-AEA60BAD-ED29-4CDC-9D37-AE21569CF64EQ36546961-D6CA2900-CF6E-429C-900D-CB7D7C738AB1Q36774449-E32C7BB9-4781-4E57-AFB9-2F719A32C8D9Q37227320-0ADC9BB9-9C6F-407E-AB3D-2467C5B1706AQ37638990-7CBFA1F8-2CCE-4C20-9F24-B5EC12813D38Q38263318-8F299BD6-AE67-483C-9827-F24282DE5AE3Q38499986-3F79D09D-BFA2-4B17-8AB2-3EA256971149Q39766915-38DCB1EC-2180-435C-A2FC-FE5DC69CD8EEQ41394061-274D36C0-7346-4285-AAC2-0CCCED7CBE9AQ41817676-8FB1EE8E-A7F7-487B-B8C0-E0CCA992E23BQ42272245-C456F639-30DC-42A0-9EEF-A9F177F5CC43Q42552346-EA928D78-F9E5-4E27-8992-6423F70C169DQ42744255-3225E0DD-704B-489C-AEB9-83F159A2D182Q43083254-DB29D407-9BA0-44F7-A9C9-5F63ADD46F76Q46309927-4E02D453-CB8E-4306-B655-95320E1DEF89Q47813215-1EE2E808-5DE8-454A-B4BD-245ECAEE2A17Q47897765-5C5953DC-2B95-4ECA-94E6-4D3ACBB8CEB4
P2860
Characterization of a glucose-repressed pyruvate kinase (Pyk2p) in Saccharomyces cerevisiae that is catalytically insensitive to fructose-1,6-bisphosphate
description
1997 nî lūn-bûn
@nan
1997 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի մայիսին հրատարակված գիտական հոդված
@hy
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
name
Characterization of a glucose- ...... e to fructose-1,6-bisphosphate
@ast
Characterization of a glucose- ...... e to fructose-1,6-bisphosphate
@en
Characterization of a glucose- ...... to fructose-1,6-bisphosphate.
@nl
type
label
Characterization of a glucose- ...... e to fructose-1,6-bisphosphate
@ast
Characterization of a glucose- ...... e to fructose-1,6-bisphosphate
@en
Characterization of a glucose- ...... to fructose-1,6-bisphosphate.
@nl
altLabel
Characterization of a glucose- ...... e to fructose-1,6-bisphosphate
@en
prefLabel
Characterization of a glucose- ...... e to fructose-1,6-bisphosphate
@ast
Characterization of a glucose- ...... e to fructose-1,6-bisphosphate
@en
Characterization of a glucose- ...... to fructose-1,6-bisphosphate.
@nl
P2093
P2860
P921
P3181
P1476
Characterization of a glucose- ...... e to fructose-1,6-bisphosphate
@en
P2093
C P Hollenberg
E Schlüter
F K Zimmermann
J J Heinisch
P2860
P304
P3181
P356
10.1128/JB.179.9.2987-2993.1997
P407
P577
1997-05-01T00:00:00Z