GENTAUR Belgium BVBA BE0473327336 Voortstraat 49, 1910 Kampenhout BELGIUM Tel 0032 16 58 90 45
GENTAUR U.S.A Genprice Inc,Logistics 547 Yurok Circle, SanJose, CA 95123
Tel (408) 780-0908, Fax (408) 780-0908, [email protected]

Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, Gentaur another in time delivery

Enolase 1 (EC 4 2 1 11) (2-phospho-D-glycerate hydro-lyase 1) (2-phosphoglycerate dehydratase 1)

 ENO1_YEAST              Reviewed;         437 AA.
P00924; D6VV34; P99013;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
05-OCT-2010, sequence version 3.
26-FEB-2020, entry version 220.
RecName: Full=Enolase 1;
EC=4.2.1.11;
AltName: Full=2-phospho-D-glycerate hydro-lyase 1;
AltName: Full=2-phosphoglycerate dehydratase 1;
Name=ENO1; Synonyms=ENOA, HSP48; OrderedLocusNames=YGR254W; ORFNames=G9160;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6256394;
Holland M.J., Holland J.P., Thill G.P., Jackson K.A.;
"The primary structures of two yeast enolase genes. Homology between the 5'
noncoding flanking regions of yeast enolase and glyceraldehyde-3-phosphate
dehydrogenase genes.";
J. Biol. Chem. 256:1385-1395(1981).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9133741;
DOI=10.1002/(sici)1097-0061(19970330)13:4<369::aid-yea81>3.0.co;2-v;
Mazzoni C., Ruzzi M., Rinaldi T., Solinas F., Montebove F., Frontali L.;
"Sequence analysis of a 10.5 kb DNA fragment from the yeast chromosome VII
reveals the presence of three new open reading frames and of a tRNAThr
gene.";
Yeast 13:369-372(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169869;
Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
Nature 387:81-84(1997).
[4]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
G3 (Bethesda) 4:389-398(2014).
[5]
PROTEIN SEQUENCE OF 2-437.
PubMed=7005235;
Chin C.C.Q., Brewer J.M., Wold F.;
"The amino acid sequence of yeast enolase.";
J. Biol. Chem. 256:1377-1384(1981).
[6]
PROTEIN SEQUENCE OF 2-12.
STRAIN=ATCC 26786 / X2180-1A;
Sanchez J.-C., Golaz O., Schaller D., Morch F., Frutiger S., Hughes G.J.,
Appel R.D., Deshusses J., Hochstrasser D.F.;
Submitted (AUG-1995) to UniProtKB.
[7]
PROTEIN SEQUENCE OF 30-47.
STRAIN=ATCC 204508 / S288c;
PubMed=7895733; DOI=10.1002/elps.11501501210;
Garrels J.I., Futcher B., Kobayashi R., Latter G.I., Schwender B.,
Volpe T., Warner J.R., McLaughlin C.S.;
"Protein identifications for a Saccharomyces cerevisiae protein database.";
Electrophoresis 15:1466-1486(1994).
[8]
PROTEIN SEQUENCE OF 69-79.
STRAIN=ATCC 38531 / Y41;
PubMed=7737086; DOI=10.1002/elps.1150160124;
Norbeck J., Blomberg A.;
"Gene linkage of two-dimensional polyacrylamide gel electrophoresis
resolved proteins from isogene families in Saccharomyces cerevisiae by
microsequencing of in-gel trypsin generated peptides.";
Electrophoresis 16:149-156(1995).
[9]
MUTAGENESIS OF LYS-346, AND ACTIVE SITE.
PubMed=8634301; DOI=10.1021/bi952186y;
Poyner R.R., Laughlin L.T., Sowa G.A., Reed G.H.;
"Toward identification of acid/base catalysts in the active site of
enolase: comparison of the properties of K345A, E168Q, and E211Q
variants.";
Biochemistry 35:1692-1699(1996).
[10]
MUTAGENESIS OF HIS-160.
PubMed=11027610; DOI=10.1006/bbrc.2000.3618;
Brewer J.M., Holland M.J., Lebioda L.;
"The H159A mutant of yeast enolase 1 has significant activity.";
Biochem. Biophys. Res. Commun. 276:1199-1202(2000).
[11]
SUBCELLULAR LOCATION.
PubMed=11502169; DOI=10.1021/bi010277r;
Grandier-Vazeille X., Bathany K., Chaignepain S., Camougrand N., Manon S.,
Schmitter J.-M.;
"Yeast mitochondrial dehydrogenases are associated in a supramolecular
complex.";
Biochemistry 40:9758-9769(2001).
[12]
MUTAGENESIS OF HIS-160 AND ASN-208.
PubMed=13678299; DOI=10.1023/a:1025390123761;
Brewer J.M., Glover C.V., Holland M.J., Lebioda L.;
"Enzymatic function of loop movement in enolase: preparation and some
properties of H159N, H159A, H159F, and N207A enolases.";
J. Protein Chem. 22:353-361(2003).
[13]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=17287358; DOI=10.1073/pnas.0607084104;
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
"Analysis of phosphorylation sites on proteins from Saccharomyces
cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
[15]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-358, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22106047; DOI=10.1002/pmic.201100166;
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
"Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
Proteomics 12:236-240(2012).
[16]
X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
PubMed=3374614; DOI=10.1038/333683a0;
Lebioda L., Stec B.;
"Crystal structure of enolase indicates that enolase and pyruvate kinase
evolved from a common ancestor.";
Nature 333:683-686(1988).
[17]
X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
PubMed=2645275; DOI=10.2210/pdb2enl/pdb;
Lebioda L., Stec B., Brewer J.M.;
"The structure of yeast enolase at 2.25-A resolution. An 8-fold beta +
alpha-barrel with a novel beta beta alpha alpha (beta alpha)6 topology.";
J. Biol. Chem. 264:3685-3693(1989).
[18]
X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
PubMed=2405163; DOI=10.1016/0022-2836(90)90023-f;
Stec B., Lebioda L.;
"Refined structure of yeast apo-enolase at 2.25-A resolution.";
J. Mol. Biol. 211:235-248(1990).
[19]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND
MAGNESIUM IONS, AND COFACTOR.
PubMed=8605183; DOI=10.1021/bi952859c;
Larsen T.M., Wedekind J.E., Rayment I., Reed G.H.;
"A carboxylate oxygen of the substrate bridges the magnesium ions at the
active site of enolase: structure of the yeast enzyme complexed with the
equilibrium mixture of 2-phosphoglycerate and phosphoenolpyruvate at 1.8-A
resolution.";
Biochemistry 35:4349-4358(1996).
[20]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH SUBSTRATE.
PubMed=9376357; DOI=10.1021/bi9712450;
Zhang E., Brewer J.M., Minor W., Carreira L.A., Lebioda L.;
"Mechanism of enolase: the crystal structure of asymmetric dimer enolase-2-
phospho-D-glycerate/enolase-phosphoenolpyruvate at 2.0-A resolution.";
Biochemistry 36:12526-12534(1997).
[21]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF MUTANT ALA-40 IN COMPLEX WITH
MAGNESIUM IONS AND SUBSTRATE ANALOG.
PubMed=12054465; DOI=10.1016/s0003-9861(02)00024-3;
Poyner R.R., Larsen T.M., Wong S.-W., Reed G.H.;
"Functional and structural changes due to a serine to alanine mutation in
the active-site flap of enolase.";
Arch. Biochem. Biophys. 401:155-163(2002).
[22]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANT GLN-212 AND MUTANT GLN-169,
MUTAGENESIS OF GLU-212 AND LYS-346, AND ACTIVE SITE.
PubMed=12846578; DOI=10.1021/bi0346345;
Sims P.A., Larsen T.M., Poyner R.R., Cleland W.W., Reed G.H.;
"Reverse protonation is the key to general acid-base catalysis in
enolase.";
Biochemistry 42:8298-8306(2003).
-!- CATALYTIC ACTIVITY:
Reaction=(2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate;
Xref=Rhea:RHEA:10164, ChEBI:CHEBI:15377, ChEBI:CHEBI:58289,
ChEBI:CHEBI:58702; EC=4.2.1.11;
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:8605183};
Note=Mg(2+) is required for catalysis and for stabilizing the dimer.
{ECO:0000269|PubMed:8605183};
-!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
glyceraldehyde 3-phosphate: step 4/5.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12054465,
ECO:0000269|PubMed:8605183, ECO:0000269|PubMed:9376357}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11502169}.
-!- MISCELLANEOUS: Present with 76700 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the enolase family. {ECO:0000305}.
---------------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
---------------------------------------------------------------------------
EMBL; J01322; AAA88712.1; -; Genomic_DNA.
EMBL; X99228; CAA67616.1; -; Genomic_DNA.
EMBL; Z73039; CAA97283.1; -; Genomic_DNA.
EMBL; BK006941; DAA08345.1; -; Genomic_DNA.
PIR; S64586; NOBY.
RefSeq; NP_011770.3; NM_001181383.3.
PDB; 1EBG; X-ray; 2.10 A; A/B=2-437.
PDB; 1EBH; X-ray; 1.90 A; A/B=2-437.
PDB; 1ELS; X-ray; 2.40 A; A=2-437.
PDB; 1L8P; X-ray; 2.10 A; A/B/C/D=2-437.
PDB; 1NEL; X-ray; 2.60 A; A=2-437.
PDB; 1ONE; X-ray; 1.80 A; A/B=2-437.
PDB; 1P43; X-ray; 1.80 A; A/B=2-437.
PDB; 1P48; X-ray; 2.00 A; A/B=2-437.
PDB; 2AL1; X-ray; 1.50 A; A/B=2-437.
PDB; 2AL2; X-ray; 1.85 A; A/B=2-437.
PDB; 2ONE; X-ray; 2.00 A; A/B=2-437.
PDB; 2XGZ; X-ray; 1.80 A; A/B=2-437.
PDB; 2XH0; X-ray; 1.70 A; A/B/C/D=2-437.
PDB; 2XH2; X-ray; 1.80 A; A/B/C/D=2-437.
PDB; 2XH4; X-ray; 1.70 A; A/B/C/D=2-437.
PDB; 2XH7; X-ray; 1.80 A; A/B=2-437.
PDB; 3ENL; X-ray; 2.25 A; A=2-437.
PDB; 4ENL; X-ray; 1.90 A; A=2-437.
PDB; 5ENL; X-ray; 2.20 A; A=2-437.
PDB; 6ENL; X-ray; 2.20 A; A=2-437.
PDB; 7ENL; X-ray; 2.20 A; A=2-437.
PDBsum; 1EBG; -.
PDBsum; 1EBH; -.
PDBsum; 1ELS; -.
PDBsum; 1L8P; -.
PDBsum; 1NEL; -.
PDBsum; 1ONE; -.
PDBsum; 1P43; -.
PDBsum; 1P48; -.
PDBsum; 2AL1; -.
PDBsum; 2AL2; -.
PDBsum; 2ONE; -.
PDBsum; 2XGZ; -.
PDBsum; 2XH0; -.
PDBsum; 2XH2; -.
PDBsum; 2XH4; -.
PDBsum; 2XH7; -.
PDBsum; 3ENL; -.
PDBsum; 4ENL; -.
PDBsum; 5ENL; -.
PDBsum; 6ENL; -.
PDBsum; 7ENL; -.
SMR; P00924; -.
BioGrid; 33505; 142.
DIP; DIP-5561N; -.
IntAct; P00924; 82.
MINT; P00924; -.
STRING; 4932.YGR254W; -.
Allergome; 786; Sac c Enolase.
MoonDB; P00924; Curated.
MoonProt; P00924; -.
CarbonylDB; P00924; -.
iPTMnet; P00924; -.
COMPLUYEAST-2DPAGE; P00924; -.
SWISS-2DPAGE; P00924; -.
UCD-2DPAGE; P00924; -.
MaxQB; P00924; -.
PaxDb; P00924; -.
PRIDE; P00924; -.
TopDownProteomics; P00924; -.
EnsemblFungi; YGR254W_mRNA; YGR254W; YGR254W.
GeneID; 853169; -.
KEGG; sce:YGR254W; -.
EuPathDB; FungiDB:YGR254W; -.
SGD; S000003486; ENO1.
HOGENOM; CLU_031223_0_0_1; -.
InParanoid; P00924; -.
KO; K01689; -.
OMA; EFMIIPV; -.
BioCyc; YEAST:YGR254W-MONOMER; -.
BRENDA; 4.2.1.11; 984.
Reactome; R-SCE-70171; Glycolysis.
Reactome; R-SCE-70263; Gluconeogenesis.
SABIO-RK; P00924; -.
UniPathway; UPA00109; UER00187.
EvolutionaryTrace; P00924; -.
PRO; PR:P00924; -.
Proteomes; UP000002311; Chromosome VII.
RNAct; P00924; protein.
GO; GO:0005737; C:cytoplasm; HDA:SGD.
GO; GO:0005829; C:cytosol; HDA:SGD.
GO; GO:0000324; C:fungal-type vacuole; IDA:SGD.
GO; GO:0005739; C:mitochondrion; IDA:SGD.
GO; GO:0000015; C:phosphopyruvate hydratase complex; IDA:SGD.
GO; GO:0005886; C:plasma membrane; HDA:SGD.
GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
GO; GO:1904408; F:melatonin binding; IDA:SGD.
GO; GO:0004634; F:phosphopyruvate hydratase activity; IMP:SGD.
GO; GO:0006094; P:gluconeogenesis; IEP:SGD.
GO; GO:0006096; P:glycolytic process; IMP:SGD.
GO; GO:0032889; P:regulation of vacuole fusion, non-autophagic; IDA:SGD.
CDD; cd03313; enolase; 1.
Gene3D; 3.20.20.120; -; 1.
Gene3D; 3.30.390.10; -; 1.
HAMAP; MF_00318; Enolase; 1.
InterPro; IPR000941; Enolase.
InterPro; IPR036849; Enolase-like_C_sf.
InterPro; IPR029017; Enolase-like_N.
InterPro; IPR020810; Enolase_C.
InterPro; IPR020809; Enolase_CS.
InterPro; IPR020811; Enolase_N.
PANTHER; PTHR11902; PTHR11902; 1.
Pfam; PF00113; Enolase_C; 1.
Pfam; PF03952; Enolase_N; 1.
PIRSF; PIRSF001400; Enolase; 1.
PRINTS; PR00148; ENOLASE.
SMART; SM01192; Enolase_C; 1.
SMART; SM01193; Enolase_N; 1.
SUPFAM; SSF51604; SSF51604; 1.
SUPFAM; SSF54826; SSF54826; 1.
TIGRFAMs; TIGR01060; eno; 1.
PROSITE; PS00164; ENOLASE; 1.
1: Evidence at protein level;
3D-structure; Cytoplasm; Direct protein sequencing; Glycolysis;
Isopeptide bond; Lyase; Magnesium; Metal-binding; Phosphoprotein;
Reference proteome; Ubl conjugation.
INIT_MET 1
/note="Removed"
/evidence="ECO:0000269|PubMed:7005235, ECO:0000269|Ref.6"
CHAIN 2..437
/note="Enolase 1"
/id="PRO_0000134062"
REGION 373..376
/note="Substrate binding"
/evidence="ECO:0000269|PubMed:12054465,
ECO:0000269|PubMed:8605183, ECO:0000269|PubMed:9376357"
ACT_SITE 212
/note="Proton donor"
/evidence="ECO:0000269|PubMed:12846578"
ACT_SITE 346
/note="Proton acceptor"
/evidence="ECO:0000269|PubMed:12846578,
ECO:0000269|PubMed:8634301"
METAL 247
/note="Magnesium"
/evidence="ECO:0000269|PubMed:8605183"
METAL 296
/note="Magnesium"
/evidence="ECO:0000269|PubMed:8605183"
METAL 321
/note="Magnesium"
/evidence="ECO:0000269|PubMed:8605183"
BINDING 160
/note="Substrate"
/evidence="ECO:0000269|PubMed:8605183,
ECO:0000269|PubMed:9376357"
BINDING 169
/note="Substrate"
/evidence="ECO:0000269|PubMed:8605183,
ECO:0000269|PubMed:9376357"
BINDING 296
/note="Substrate"
/evidence="ECO:0000269|PubMed:8605183,
ECO:0000269|PubMed:9376357"
BINDING 321
/note="Substrate"
/evidence="ECO:0000269|PubMed:8605183,
ECO:0000269|PubMed:9376357"
BINDING 397
/note="Substrate"
/evidence="ECO:0000269|PubMed:8605183,
ECO:0000269|PubMed:9376357"
MOD_RES 119
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:17287358"
MOD_RES 138
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P00925"
MOD_RES 188
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P00925"
MOD_RES 313
/note="Phosphothreonine"
/evidence="ECO:0000250|UniProtKB:P00925"
MOD_RES 324
/note="Phosphothreonine"
/evidence="ECO:0000250|UniProtKB:P00925"
CROSSLNK 60
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin)"
/evidence="ECO:0000250|UniProtKB:P00925"
CROSSLNK 243
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin)"
/evidence="ECO:0000250|UniProtKB:P00925"
CROSSLNK 358
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin)"
/evidence="ECO:0000244|PubMed:22106047"
MUTAGEN 40
/note="S->A: Reduces activity by 99.9%."
MUTAGEN 160
/note="H->A,F,N: Reduces activity by 99%."
/evidence="ECO:0000269|PubMed:11027610,
ECO:0000269|PubMed:13678299"
MUTAGEN 169
/note="E->Q: Reduces Kcat over 100000-fold."
MUTAGEN 208
/note="N->A: Reduces activity by 44%."
/evidence="ECO:0000269|PubMed:13678299"
MUTAGEN 212
/note="E->Q: Reduces Kcat over 100000-fold."
/evidence="ECO:0000269|PubMed:12846578"
MUTAGEN 346
/note="K->A: Reduces Kcat over 100000-fold. Abolishes of
the proton exchange reaction that initiates the enzymatic
reaction."
/evidence="ECO:0000269|PubMed:12846578,
ECO:0000269|PubMed:8634301"
CONFLICT 242
/note="I -> V (in Ref. 1; AAA88712)"
/evidence="ECO:0000305"
STRAND 5..12
/evidence="ECO:0000244|PDB:2AL1"
STRAND 18..26
/evidence="ECO:0000244|PDB:2AL1"
STRAND 29..34
/evidence="ECO:0000244|PDB:2AL1"
STRAND 43..45
/evidence="ECO:0000244|PDB:1EBH"
HELIX 57..59
/evidence="ECO:0000244|PDB:2AL1"
HELIX 63..71
/evidence="ECO:0000244|PDB:2AL1"
HELIX 73..80
/evidence="ECO:0000244|PDB:2AL1"
HELIX 87..98
/evidence="ECO:0000244|PDB:2AL1"
STRAND 100..102
/evidence="ECO:0000244|PDB:1EBH"
TURN 104..106
/evidence="ECO:0000244|PDB:2AL1"
HELIX 108..125
/evidence="ECO:0000244|PDB:2AL1"
HELIX 130..138
/evidence="ECO:0000244|PDB:2AL1"
STRAND 145..147
/evidence="ECO:0000244|PDB:2AL1"
STRAND 152..156
/evidence="ECO:0000244|PDB:2AL1"
HELIX 158..160
/evidence="ECO:0000244|PDB:2AL1"
STRAND 161..164
/evidence="ECO:0000244|PDB:2AL1"
STRAND 169..173
/evidence="ECO:0000244|PDB:2AL1"
HELIX 180..202
/evidence="ECO:0000244|PDB:2AL1"
HELIX 204..207
/evidence="ECO:0000244|PDB:2AL1"
STRAND 213..215
/evidence="ECO:0000244|PDB:1P48"
HELIX 222..236
/evidence="ECO:0000244|PDB:2AL1"
TURN 239..241
/evidence="ECO:0000244|PDB:2AL1"
STRAND 243..247
/evidence="ECO:0000244|PDB:2AL1"
HELIX 250..253
/evidence="ECO:0000244|PDB:2AL1"
TURN 261..264
/evidence="ECO:0000244|PDB:2AL1"
HELIX 270..272
/evidence="ECO:0000244|PDB:2AL1"
HELIX 276..289
/evidence="ECO:0000244|PDB:2AL1"
STRAND 292..296
/evidence="ECO:0000244|PDB:2AL1"
HELIX 304..311
/evidence="ECO:0000244|PDB:2AL1"
TURN 312..314
/evidence="ECO:0000244|PDB:2AL2"
STRAND 316..321
/evidence="ECO:0000244|PDB:2AL1"
TURN 322..326
/evidence="ECO:0000244|PDB:2AL1"
HELIX 328..336
/evidence="ECO:0000244|PDB:2AL1"
STRAND 341..345
/evidence="ECO:0000244|PDB:2AL1"
HELIX 347..350
/evidence="ECO:0000244|PDB:2AL1"
HELIX 353..365
/evidence="ECO:0000244|PDB:2AL1"
STRAND 369..373
/evidence="ECO:0000244|PDB:2AL1"
HELIX 383..390
/evidence="ECO:0000244|PDB:2AL1"
STRAND 394..397
/evidence="ECO:0000244|PDB:2AL1"
HELIX 404..420
/evidence="ECO:0000244|PDB:2AL1"
HELIX 421..423
/evidence="ECO:0000244|PDB:2AL1"
STRAND 424..426
/evidence="ECO:0000244|PDB:2AL1"
HELIX 428..430
/evidence="ECO:0000244|PDB:2AL1"
HELIX 434..436
/evidence="ECO:0000244|PDB:2AL1"
SEQUENCE 437 AA; 46816 MW; 69F45214DBD375BE CRC64;
MAVSKVYARS VYDSRGNPTV EVELTTEKGV FRSIVPSGAS TGVHEALEMR DGDKSKWMGK
GVLHAVKNVN DVIAPAFVKA NIDVKDQKAV DDFLISLDGT ANKSKLGANA ILGVSLAASR
AAAAEKNVPL YKHLADLSKS KTSPYVLPVP FLNVLNGGSH AGGALALQEF MIAPTGAKTF
AEALRIGSEV YHNLKSLTKK RYGASAGNVG DEGGVAPNIQ TAEEALDLIV DAIKAAGHDG
KIKIGLDCAS SEFFKDGKYD LDFKNPNSDK SKWLTGPQLA DLYHSLMKRY PIVSIEDPFA
EDDWEAWSHF FKTAGIQIVA DDLTVTNPKR IATAIEKKAA DALLLKVNQI GTLSESIKAA
QDSFAAGWGV MVSHRSGETE DTFIADLVVG LRTGQIKTGA PARSERLAKL NQLLRIEEEL
GDNAVFAGEN FHHGDKL


Related products :

Catalog number Product name Quantity
E0537r ELISA kit 2-phospho-D-glycerate hydro-lyase,Eno2,Eno-2,Enolase 2,Gamma-enolase,Neural enolase,Neuron-specific enolase,NSE,Rat,Rattus norvegicus 96T
E0537r ELISA 2-phospho-D-glycerate hydro-lyase,Eno2,Eno-2,Enolase 2,Gamma-enolase,Neural enolase,Neuron-specific enolase,NSE,Rat,Rattus norvegicus 96T
E0537m ELISA kit 2-phospho-D-glycerate hydro-lyase,Eno2,Eno-2,Enolase 2,Gamma-enolase,Mouse,Mus musculus,Neural enolase,Neuron-specific enolase,NSE 96T
U0537m CLIA 2-phospho-D-glycerate hydro-lyase,Eno2,Eno-2,Enolase 2,Gamma-enolase,Mouse,Mus musculus,Neural enolase,Neuron-specific enolase,NSE 96T
U0537r CLIA 2-phospho-D-glycerate hydro-lyase,Eno2,Eno-2,Enolase 2,Gamma-enolase,Neural enolase,Neuron-specific enolase,NSE,Rat,Rattus norvegicus 96T
E0537m ELISA 2-phospho-D-glycerate hydro-lyase,Eno2,Eno-2,Enolase 2,Gamma-enolase,Mouse,Mus musculus,Neural enolase,Neuron-specific enolase,NSE 96T
U0537h CLIA 2-phospho-D-glycerate hydro-lyase,ENO2,Enolase 2,Gamma-enolase,Homo sapiens,Human,Neural enolase,Neuron-specific enolase,NSE 96T
E0537h ELISA kit 2-phospho-D-glycerate hydro-lyase,ENO2,Enolase 2,Gamma-enolase,Homo sapiens,Human,Neural enolase,Neuron-specific enolase,NSE 96T
E0537h ELISA 2-phospho-D-glycerate hydro-lyase,ENO2,Enolase 2,Gamma-enolase,Homo sapiens,Human,Neural enolase,Neuron-specific enolase,NSE 96T
U1449r CLIA 2-phospho-D-glycerate hydro-lyase,Alpha-enolase,Eno1,Eno-1,Enolase 1,NNE,Non-neural enolase,Rat,Rattus norvegicus 96T
E1449r ELISA 2-phospho-D-glycerate hydro-lyase,Alpha-enolase,Eno1,Eno-1,Enolase 1,NNE,Non-neural enolase,Rat,Rattus norvegicus 96T
E1449r ELISA kit 2-phospho-D-glycerate hydro-lyase,Alpha-enolase,Eno1,Eno-1,Enolase 1,NNE,Non-neural enolase,Rat,Rattus norvegicus 96T
E1449m ELISA 2-phospho-D-glycerate hydro-lyase,Alpha-enolase,Eno1,Eno-1,Enolase 1,Mouse,Mus musculus,NNE,Non-neural enolase 96T
U1449m CLIA 2-phospho-D-glycerate hydro-lyase,Alpha-enolase,Eno1,Eno-1,Enolase 1,Mouse,Mus musculus,NNE,Non-neural enolase 96T
E1449m ELISA kit 2-phospho-D-glycerate hydro-lyase,Alpha-enolase,Eno1,Eno-1,Enolase 1,Mouse,Mus musculus,NNE,Non-neural enolase 96T
U1449b CLIA 2-phospho-D-glycerate hydro-lyase,Alpha-enolase,Bos taurus,Bovine,ENO1,Enolase 1,HAP47,NNE,Non-neural enolase,Phosphopyruvate hydratase 96T
E1449b ELISA kit 2-phospho-D-glycerate hydro-lyase,Alpha-enolase,Bos taurus,Bovine,ENO1,Enolase 1,HAP47,NNE,Non-neural enolase,Phosphopyruvate hydratase 96T
E1449b ELISA 2-phospho-D-glycerate hydro-lyase,Alpha-enolase,Bos taurus,Bovine,ENO1,Enolase 1,HAP47,NNE,Non-neural enolase,Phosphopyruvate hydratase 96T
EIAAB12971 2-phospho-D-glycerate hydro-lyase,Beta-enolase,Bos taurus,Bovine,ENO3,Enolase 3,MSE,Muscle-specific enolase,Skeletal muscle enolase
EIAAB12968 2-phospho-D-glycerate hydro-lyase,Beta-enolase,Eno3,Eno-3,Enolase 3,Mouse,MSE,Mus musculus,Muscle-specific enolase,Skeletal muscle enolase
EIAAB12967 2-phospho-D-glycerate hydro-lyase,Beta-enolase,Eno3,Eno-3,Enolase 3,MSE,Muscle-specific enolase,Rat,Rattus norvegicus,Skeletal muscle enolase
EIAAB12970 2-phospho-D-glycerate hydro-lyase,Beta-enolase,ENO3,Enolase 3,Homo sapiens,Human,MSE,Muscle-specific enolase,Skeletal muscle enolase
EIAAB12969 2-phospho-D-glycerate hydro-lyase,Beta-enolase,ENO3,Enolase 3,MSE,Muscle-specific enolase,Oryctolagus cuniculus,Rabbit,Skeletal muscle enolase
EIAAB12965 2-phospho-D-glycerate hydro-lyase,Beta-enolase,ENO3,Enolase 3,MSE,Muscle-specific enolase,Pig,Skeletal muscle enolase,Sus scrofa
U1449h CLIA 2-phospho-D-glycerate hydro-lyase,Alpha-enolase,C-myc promoter-binding protein,ENO1,ENO1L1,Enolase 1,Homo sapiens,Human,MBP-1,MBPB1,MPB1,MPB-1,NNE,Non-neural enolase,Phosphopyruvate hydratase,Pla 96T
Pathways :
WP253: Glycolysis
WP1946: Cori Cycle
WP1030: Selenium metabolism Selenoproteins
WP28: Selenium Metabolism and Selenoproteins
WP1293: Selenium metabolism Selenoproteins
WP1567: Glycolysis and Gluconeogenesis
WP1700: Selenoamino acid metabolism
WP1718: Vitamin B6 metabolism
WP668: Octadecanoid Pathway
WP1149: Selenium metabolism Selenoproteins
WP1493: Carbon assimilation C4 pathway
WP1688: Polyketide sugar unit biosynthesis
WP1705: Sulfur metabolism
WP2349: vitamin B3 (niacin), NAD and NADP biosynthesis pathway
WP390: Serine-isocitrate lyase pathway
WP108: Selenium metabolism/Selenoproteins
WP1358: Selenium metabolism Selenoproteins
WP1640: Cysteine and methionine metabolism
WP1703: Streptomycin biosynthesis

Related Genes :
[Eno1 Eno-1] Alpha-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (Enolase 1) (Non-neural enolase) (NNE)
[ENO2 LOS2 At2g36530 F1O11.16] Bifunctional enolase 2/transcriptional activator (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase 2) (2-phosphoglycerate dehydratase 2) (LOW EXPRESSION OF OSMOTICALLY RESPONSIVE GENES 1)
[ENO1 CAALFM_C108500CA CaO19.395 CaO19.8025] Enolase 1 (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (2-phosphoglycerate dehydratase)
[Eno1 Eno-1] Alpha-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (Enolase 1) (Non-neural enolase) (NNE)
[ENO1 ENO1L1 MBPB1 MPB1] Alpha-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (C-myc promoter-binding protein) (Enolase 1) (MBP-1) (MPB-1) (Non-neural enolase) (NNE) (Phosphopyruvate hydratase) (Plasminogen-binding protein)
[ENO3] Beta-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (Enolase 3) (Muscle-specific enolase) (MSE) (Skeletal muscle enolase)
[Eno2 Eno-2] Gamma-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (Enolase 2) (Neural enolase) (Neuron-specific enolase) (NSE)
[ENO2] Gamma-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (Enolase 2) (Neural enolase) (Neuron-specific enolase) (NSE)
[Eno2 Eno-2] Gamma-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (Enolase 2) (Neural enolase) (Neuron-specific enolase) (NSE)
[Eno3 Eno-3] Beta-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (Enolase 3) (Muscle-specific enolase) (MSE) (Skeletal muscle enolase)
[Eno3 Eno-3] Beta-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (Enolase 3) (Muscle-specific enolase) (MSE) (Skeletal muscle enolase)
[ENO1] Alpha-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (Enolase 1) (HAP47) (Non-neural enolase) (NNE) (Phosphopyruvate hydratase)
[hchA A8C65_13880 A9R57_25255 AKG99_20940 AMK83_16550 B7C53_22525 B9M99_11580 B9T59_01945 BJJ90_15205 BMT49_12710 BON65_01250 BON66_15955 BON86_06490 BON95_14610 BUE81_10670 BvCms12BK_01457 BvCms28BK_04168 BvCmsHHP001_02632 BvCmsKKP061_00566 BvCmsKSP045_04450 BvCmsKSP058_03204 BvCmsKSP067_02879 BvCmsNSP006_03750 BvCmsNSP007_03329 BvCmsNSP047_03567 BvCmsSINP011_04162 BW690_17225 BZL69_29425 C2U48_24800 C5715_19445 C5N07_21380 C6669_19295 C7B06_02290 C7B07_03930 C9Z23_21970 C9Z37_00915 C9Z43_06360 C9Z78_05610 CDC27_10055 CDL37_00765 CI694_25210 COD46_23180 CQP61_17160 CRD98_26150 D2188_01360 D9D20_21030 D9D43_06110 D9H68_20750 D9H70_25730 D9I87_15275 DEN89_24995 DEO04_05510 DL800_09215 DQE83_22775 DTL43_21780 DU321_04440 DXT73_20690 E2134_24005 E2135_17195 E2855_02503 E2863_02392 E5P22_21380 E5S46_06650 EC95NR1_00961 ED648_25045 ELT20_21515 ELV08_24970 EPT01_11070 EQ825_23250 ERS085379_01273 ERS085386_05041 ExPECSC038_01920 EXX71_02385 EXX78_21815 EYD11_09165 F7F11_20115 F7F29_22635 FNJ83_13175 FQ915_04255 FQR64_09390 FWK02_18105 HmCmsJML079_02678 HMPREF3040_01583 HW43_13705 NCTC10082_04431 NCTC10418_03071 NCTC10767_03558 NCTC11022_01867 NCTC11126_04427 NCTC11181_05650 NCTC12950_02263 NCTC8985_00529 NCTC9111_05933 NCTC9703_00277 PGD_01271 PU06_24500 SAMEA3472043_00447 SAMEA3472055_03589 SAMEA3472056_01268 SAMEA3472070_00654 SAMEA3472080_04213 SAMEA3472090_03376 SAMEA3472110_00060 SAMEA3472112_00448 SAMEA3752372_00752 UN91_23615 WQ89_10695] Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.124) (Maillard deglycase)
[ENO3] Beta-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (Enolase 3) (Muscle-specific enolase) (MSE) (Skeletal muscle enolase)
[eno MSMEG_5415 MSMEI_5267] Enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (2-phosphoglycerate dehydratase)
[yjeF nnrD nnrE A6V01_16625 AC789_1c45800 ACN002_4392 AW106_17115 BB545_04070 BN17_41441 BOH76_10905 BON72_19710 BON76_04155 BON95_14955 BTQ06_07255 BVL39_04290 C5N07_07145 C6669_06565 C7235_22665 C7B02_22745 C9162_14280 C9306_16010 C9Z28_08925 C9Z37_19300 C9Z69_17100 C9Z89_19770 CA593_04975 COD30_21525 CR538_23135 CRD98_04165 CRM83_17370 D0X26_12915 D2184_07750 D6T60_21965 D9J44_09440 D9K48_15185 DAH18_07435 DAH32_17635 DBQ99_23525 DEN97_13975 DEO19_11825 DIV22_15595 DL800_29085 DP277_02605 DQF57_15735 DS732_02620 E5S35_05440 ED600_08260 EHH55_18965 EJC75_20595 EKI52_12685 EYD11_20595 EYY78_08665 F1E03_05325 F7F23_18595 FQ915_09945] Bifunctional NAD(P)H-hydrate repair enzyme (Nicotinamide nucleotide repair protein) [Includes: ADP-dependent (S)-NAD(P)H-hydrate dehydratase (EC 4.2.1.136) (ADP-dependent NAD(P)HX dehydratase); NAD(P)H-hydrate epimerase (EC 5.1.99.6)]
[hchA A9819_11910 ACN81_03425 AML35_08765 AW059_23935 BANRA_00208 BANRA_00433 BANRA_02614 BHF46_18455 BMT91_24760 BON76_21885 BvCmsC61A_00149 BvCmsKSNP120_04693 BvCmsKSP026_03873 BvCmsKSP076_04891 C7B08_25495 C9Z39_20510 CR538_10415 D3Y67_22910 D9G42_11130 D9I97_22010 D9J11_25195 DJ503_24045 DP258_02540 E3B71_05970 EC3234A_36c00010 EC382_21100 ECTO6_01955 EHH55_07135 FORC82_1921 FV293_07100 NCTC8500_02249 NCTC9117_02637 NCTC9969_02156 SAMEA3472108_01151 SAMEA3484427_04795 SAMEA3484429_02051 SAMEA3752557_05476 SAMEA3752559_04333] Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.124) (Maillard deglycase)
[eno OR1_00408] Enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (2-phosphoglycerate dehydratase)
[nnrD nnrE BHS81_24940 BON75_25135 BUE81_24185 BW690_00535 C5P01_11605 C9114_00800 C9141_20385 C9160_20005 C9182_19515 C9201_17640 C9Z03_11025 C9Z39_09990 CG692_00180 CI641_014360 COD46_22200 CWS33_03515 D2185_07770 D3821_07085 D3O91_01535 D3Y67_00680 D9D20_08295 D9H68_15720 D9H94_06330 D9I18_04405 D9J11_13510 DAH30_09295 DAH34_17710 DAH37_06235 DEN89_23315 DEO04_15015 E0I42_01095 E2119_06500 E3B71_17555 E5P22_06605 EAI42_08035 EAI42_19730 EAI46_08330 EEP23_07485 EL75_3998 EL79_4176 EL80_4091 ELT20_09170 EPT01_09990 EXX24_09350 EXX78_19455 F1E13_09470 F1E19_03510 FQR64_20885 FRV13_14670 FV293_00830 RK56_012375] Bifunctional NAD(P)H-hydrate repair enzyme (Nicotinamide nucleotide repair protein) [Includes: ADP-dependent (S)-NAD(P)H-hydrate dehydratase (EC 4.2.1.136) (ADP-dependent NAD(P)HX dehydratase); NAD(P)H-hydrate epimerase (EC 5.1.99.6)]
[ENO1] Alpha-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (Enolase 1) (Non-neural enolase) (NNE)
[ENO1 QccE-14518] Alpha-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (Enolase 1) (Non-neural enolase) (NNE)
[aro-1 aro-2 aro-4 aro-5 aro-9 B14H13.20 NCU016321] Pentafunctional AROM polypeptide [Includes: 3-dehydroquinate synthase (DHQS) (EC 4.2.3.4); 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) (5-enolpyruvylshikimate-3-phosphate synthase) (EPSP synthase) (EPSPS); Shikimate kinase (SK) (EC 2.7.1.71); 3-dehydroquinate dehydratase (3-dehydroquinase) (EC 4.2.1.10); Shikimate dehydrogenase (EC 1.1.1.25)]
[uxuA b4322 JW4285] Mannonate dehydratase (EC 4.2.1.8) (D-mannonate hydro-lyase)
[emp-7 NCU10042] Enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (2-phosphoglycerate dehydratase) (Embden-meyerhof pathway protein 7)
[gad gnaD SSO3198] D-gluconate/D-galactonate dehydratase (GAD) (GNAD) (EC 4.2.1.140) (EC 4.2.1.39) (EC 4.2.1.6)
[eno CBP06_04475 E4195_23395 EQ845_16830] Enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (2-phosphoglycerate dehydratase)
[eno OR214_00082] Enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (2-phosphoglycerate dehydratase)
[eno OR37_00362] Enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (2-phosphoglycerate dehydratase)
[eno OR16_24200] Enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (2-phosphoglycerate dehydratase)
[] Genome polyprotein [Cleaved into: P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); P2; Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); P3; Protein 3AB; Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (EC 3.4.22.28) (Picornain 3C) (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]

Bibliography :
[32021984] Characteristics of S100B and Neuron Specific Enolase in Differentiating Acute Vertigo Cases with Central Cause; a Diagnostic Accuracy Study.
[31690416] Expression of Neuroectodermal Markers in Atypical Fibromas in Two Dwarf Hamsters (Phodopus spp.).
[31631606] [Application of a Radiomics Model for Preding Lymph Node Metastasis in Non-small Cell Lung Cancer].
[31487372] [Inflammation and Neurodegeneration in Patients with Early-Stageand Chronic Bipolar Disorder].
[31471340] Evaluation of the Value of Anti-Citrullinated α-enolase Peptide 1 Antibody in the Diagnosis of Rheumatoid Arthritis.
[31450096] PtCu nanoprobe-initiated cascade reaction modulated iodide-responsive sensing interface for improved electrochemical immunosensor of neuron-specific enolase.
[31416219] Expression of Alpha-Enolase (ENO1), Myc Promoter-Binding Protein-1 (MBP-1) and Matrix Metalloproteinases (MMP-2 and MMP-9) Reflect the Nature and Aggressiveness of Breast Tumors.
[31414742] Establishment of Reference Intervals for Serum Cytokeratin-19 Fragment and Neuron Specific Enolase by Indirect Method Using Data Obtained from Healthy Chinese Population in Chengdu.
[31396350] ENO1 silencing impaires hypoxia-induced gemcitabine chemoresistance associated with redox modulation in pancreatic cancer cells.
[31394980] Invisible hemolysis in serum samples interferes in NSE measurement.