Kim J W, Dang C V. Multifaceted roles of glycolytic enzymes [J]. Trends Biochem. Sci, 2005, 30: 142-150
Niinaka Y, Paku S, Haga A, et al. Expression and secretion of neuroleukin/phosphohexose isomerase/maturation factor as autocrine motility factor by tumor cells [J]. Cancer Res. 1998, 58: 2667-2674
Munoz-Bertomeu J, Cascales-Minana B, Irles-Segura A, et al. The plastidial glyceraldehyde-3-phosphate dehydrogenase is critical for viable pollen development in Arabidopsis [J]. Plant Physiol. 2010, 152: 1830-1841
Ji H, Wang JF, Guo JR, et al. Progress in the biological function of alpha-enolase [J]. Anim Nutr, 2016, 2(1):12-17
Lee H, Guo Y, Ohta M, et al. LOS2, a genetic locus required for cold-responsive gene transcription encodes a bi-functional ENOLASE [J]. EMBO J. 2002, 21: 2692-2702
Andriotis VM, Kruger NJ, Pike MJ, Smith AM. Plastidial glycolysis in developing Arabidopsis embryos[J]. New Phytologist, 2010, 185(3):649-62.
Vander Straeten D, Rodrigues-Pousada R A, Goodman H M, et al. Plant enolase: gene structure, expression and evolution [J]. Plant Cell 1991, 3: 719-735
Fukayama H, Masumoto C, Taniguchi Y. et al. Characterization and expression analyses of two plastidic enolase genes in rice[J]. Biosci Biotech Bioch, 2015, 79(3):402-409
Lohman, K. and Meyerhof, O. Uber die enzymatische umwandlung von phosphoglyzerins?ure in brenztraubens?ure und phosphors?ure (Enzymatic transformation of phosphoglyceric acid into pyruvic and phosphoric acid). Biochem. Z, 1934, 273: 60-72
Díaz-Ramos A, Roig-Borrellas A, García-Melero A, et al. α-enolase, a multifunctional protein: its role on pathophysiological situations [J]. J. Biomed. Biotechnol. 2012, 2012: 156795
Reed G H, Poyner R R, Larsen T M, et al. Structural and mechanistic studies of enolase [J]. Curr. Opin. Struct. Biol. 1996, 6: 736-743
Brewer J M, Wampler J E. A differential scanning calorimetric study of the effects of metal ions, substrate/product, substrate analogues and chaotropic anions on the thermal denaturation of yeast enolase 1 [J]. Int. J. Biol. Macromol. 2001, 28: 213-218
Brewer J M. Specificity and mechanism of action of metal ions in yeast enolase [J]. FEBS Lett. 1985, 182: 8-14
Subramanian A. Structural analysis of alpha-enolase. Mapping the functional domains involved in down-regulation of the c-myc protooncogene [J]. J. Biol. Chem. 2000, 275: 5958-5965
McAlister L, Holland M J. Targeted deletion of a yeast enolase structural gene. Identification and isolation of yeast enolase isozymes [J]. J. Biol. Chem. 1982, 257: 7181-7188
Munoz-Bertomeu J, Cascales-Minana B, Mulet J. M, et al. Plastidial glyceraldehyde-3-phosphate dehydrogenase deficiency leads to altered root development and affects the sugar and amino acid balance in Arabidopsis [J]. Plant Physiol. 2009, 151: 541-558
Emes M J, Tobin A K. Control of metabolism and development in higher plant plastids [J]. Int. Rev. Cytol. 1993, 145: 149-216
Weber A P, Schwacke R, Flugge U I. Solute transporters of the plastid envelope membrane [J]. Annu. Rev. Plant Biol. 2005, 56: 133-164
Eremina M, Rozhon W, Yang S, et al. ENO2 activity is required for the development and reproductive success of plants, and is feedback-repressed by AtMBP1 [J]. Plant J. 2015, 81: 895-906
Kaipio K, Kallio J, Pesonen U. Mitochondrial targeting signal in human neuropeptide Y gene [J]. Biochem. Biophy. Res. Commun. 2005, 337: 633-640
Kochetov A V. Alternative translation start sites and hidden coding potential of eukaryotic mRNAs [J]. BioEssays 2008, 30: 683-691
Cheng T H, Cohen S N. Human MDM2 isoforms translated differentially on constitutive versus p53-regulated transcripts have distinct#$NLfunctions in the p53/MDM2 and TSG101/MDM2 feedback control loops [J]. Mol. Cell. Biol. 2007, 27: 111-119
Kodama Y, Sano H. Functional diversification of a basic helix-loop-helix protein due to alternative transcription during generation of amphidiploidy in tobacco plants [J]. Biochem. J. 2007,403: 493-499
Kozak M. Regulation of translation via mRNA structure in prokaryotes and eukaryotes [J]. Gene, 2005, 361: 13-37
薛金锋, 刘雄昊, 李卓. 真核细胞中多重表达框mRNA的选择性翻译起始[J]. 中国生物化学与分子生物学报, 2015, 31: 608-615
Burgui I, Yángüez E, Sonenberg N, et al. Influenza virus mRNA translation revisited: is the eIF4E cap-binding factor required for viral mRNA translation? [J]. J Virol. 2007, 81: 12427-12438
陈慧梅. 拟南芥烯醇化酶定位、磷酸化位点鉴定及其截短体蛋白的初步研究[D]. 北京师范大学硕士毕业论文. 北京: 北京师范大学, 2015
Moshonov S, Elfakess R, Golan-Mashiach M, et al. Links between core promoter and basic gene features influence gene expression [J]. BMC Genomics 2008, 9: 92
Pesole G, Mignone F, Gissi C, et al. Structural and functional features of eukaryotic mRNA untranslated regions [J]. Gene, 2001, 276: 73-81
Kozak M. A short leader sequence impairs the fidelity of initiation by eukaryotic ribosomes [J]. Gene Expr. 1991, 1: 111-115
Kozak M. Effects of long 5' leader sequences on initiation by eukaryotic ribosomes in vitro [J]. Gene Expr. 1991, 1: 117-125
Pisarev A V, Kolupaeva V G, Yusupov M M, et al. Ribosomal position and contacts of mRNA in eukaryotic translation initiation complexes [J]. EMBO J. 2008, 27: 1609-1621
Kozak M. Pushing the limits of the scanning mechanism for initiation of translation [J]. Gene 2002, 299: 1-34
Elfakess R, Sinvani H, Haimov O, et al. Unique translation initiation of mRNAs-containing TISU element [J]. Nucl Acids Res. 2011, 39: 7598-7609
Kozak M. Downstream secondary structure facilitates recognition of initiator codons by eukaryotic ribosomes [J]. Proc. Natl. Acad. Sci. USA 1990, 87(21): 8301-8305
Kozak M. Regulation of translation via mRNA structure in prokaryotes and eukaryotes [J]. Gene, 2005, 361: 13-37
Pisarev A V, Kolupaeva V G, Pisareva V P, et al. Specific functional interactions of nucleotides at key -3 and +4 positions flanking the initiation codon with components of the mammalian 48S translation initiation complex [J]. Genes Dev. 2006, 20: 624-36
Tamarkin-Ben-Harush A, Schechtman E, Dikstein R. Co-occurrence of transcription and translation gene regulatory features underlies coordinated mRNA and protein synthesis [J]. BMC Genomics, 2014, 15: 688
Wethmar K, Barbosa-Silva A, Leutz A, et al. uORFdb--a comprehensive literature database on eukaryotic uORF biology [J]. Nucl. Acids Res. 2014, 42: 60-67
Calvo S E, Pagliarini D J, Mootha V K. Upstream open reading frames cause widespread reduction of protein expression and are polymorphic among humans [J]. Proc Natl Acad Sci USA, 2009, 106: 7507-7512
Ghosh A K, Steele R, Ray R B. Functional domains of c-myc promoter binding protein 1 involved in transcriptional repression and cell growth regulation [J]. Mol. Cell. Biol. 1999, 19: 2880-2886
Feo S, Arcuri D, Piddini E, Passantino R, et al. ENO1 gene product binds to the c-myc promoter and acts as a transcriptional repressor: relationship with Myc promoter-binding protein 1 (MBP-1) [J]. FEBS Lett. 2000, 473: 47-52
叶盼. 拟南芥烯醇化酶2(enolase2)在植物营养生长和花粉发育中的功能研究[D]. 北京师范大学硕士毕业论文. 北京: 北京师范大学, 2012
Ray R, Miller DM. Cloning and characterization of a human c-myc promoter-binding protein [J]. Mol. Cell Biol. 1991, 11: 2154-2161
Lung J, Liu K J, Chang J Y, et al. MBP-1 is efficiently encoded by an alternative transcript of the ENO1 gene but post-translationally regulated by proteasome-dependent protein turnover [J]. FEBS J. 2010, 277: 4308-4321
Zhang YH, Chen C, Shi ZH, et al. Identifcation of salinity-related genes in ENO2 mutant (eno2–) of Arabidopsis thaliana [J]. JIntegr Agr, 2018, 17 (1): 94-110
Miyoung K, Haggag A, Seonghee L, et al. AtMBP-1, an alternative translation product of LOS2, affects abscisic acid responses and is modulated by the E3 ubiquitin ligase AtSAP5 [J]. Plant J. 2013, 76: 481-493
Jaspert N, Weckermann K, Piotrowski M, et al. Enolase, a cross-link between glycolysis and stress response [C]. 20th International Conference on Arabidopsis Research: Edinburgh, Scotland. 2009
Yi T F, Dong G F, Wang Z L, et al. Identification and functional analysis of phosphoproteins regulated by auxin in Arabidopsis roots [J]. J. Plant Biol. 2009, 52: 65-72
Voll L M, Hajirezaei M R, Czogalla-Peter C, et al. Antisense inhibition of enolase strongly limits the metabolism of aromatic amino acids, but has only minor effects on respiration in leaves of transgenic tobacco plants. New Phytol. 2009, 184: 607-18
Seki M, Narusaka M, Abe H, et al. Monitoring the expression pattern of 1300 Arabidopsis genes under drought and cold stresses by using a full-length cDNA microarray [J]. Plant Cell 2001, 13: 61-72
蒋芳玲. 不结球白菜抗寒相关基因的克隆及序列分析[D]. 南京农业大学博士毕业论文. 南京: 南京农业大学, 2006
刘思秀, 王兴龙, 杨金水. 荠菜LOS2基因的克隆与分析[J]. 遗传, 2005, 32: 600-607
Sharma P, Ganeshan S, Fowler D B, et al. Characterisation of two wheat enolase cDNA showing distinct patterns of expression in leaf and crown tissues of plants exposed to low temperature [J]. Ann. Appl. Biol. 2012, 162: 271-283
Forsthoefel N R, Cushman M A F, Cushman J C. Posttranscriptional and posttranslational control of ENOLASE expression in the facultative crassulacean acid metabolism plant Mesembryanthemum crystallinum L. [J]. Plant Physiol. 1995, 108: 1185-1195
Yan S, Tang Z, Su W, et al. Proteomic analysis of salt stress-responsive proteins in rice root [J]. Proteomics, 2005, 5: 235-244
Jiang Y Q, Yang B, Harris N S et al. Comparative proteomic analysis of NaCl stress-responsive proteins in Arabidopsis roots [J]. J. Exp. Bot。 2007, 58: 3591-3607
Ndimba B K, Chivasa S, Simon W J, et al. Identification of Arabidopsis salt and osmotic stress responsive proteins using two-dimensional difference gel electrophoresis and mass spectrometry [J]. Proteomics, 2005, 5: 4185-4196
Barkla B J, Vera-Estrella R, Hernández-Coronado M, et al. Quantitative proteomics of the tonoplast reveals a role for glycolytic enzymes in salt tolerance [J]. Plant Cell, 2009, 21: 4044-4058
李晓峰. 盐芥根响应高盐胁迫的烯醇化酶基因功能和调控研究[D]. 北京师范大学硕士毕业论文. 北京: 北京师范大学, 2010
Ghelis T, Bolbach G, Clodic G, et al. Protein tyrosine kinases and protein tyrosine phosphatases are involved in abscisic acid-dependent processes in Arabidopsis seeds and suspension cells [J]. Plant Physiol. 2008, 148: 1668-1680
Barjaktarovi? Z, Schütz W, Madlung J, et al. Changes in the effective gravitational field strength affect the state of phosphorylation of stress-related proteins in callus cultures of Arabidopsis thaliana [J]. J. Exp. Bot. 2009, 60: 779-789
Zhou Y J, Gao F, Li X F, et al. Alterations in phosphopro- teome under salt stress in Thellungiella roots [J]. ChineseSSciSBull. 2010, 55: 3673-3679
Faul C, Huttelmaier S, Oh J, et al. Promotion of importi-mediated nuelear import by the phosphorylation-dependent binding of cargo protein to 14-3-3 [J]. J Cell Biol, 2005, 169(3): 415-424