1302:
1626:. Specific deficiencies of myeloperoxidase were known since the 1970s. Myeloperoxidase deficiency resulted in an absence of peroxidase staining in neutrophils but not eosinophils. Early studies on myeloperoxidase deficiency revealed that the most common disease variants were missense mutations, including that of the heme-linked methionine residue. This deficiency was often not inherited as a simple autosomal recessive trait but rather as a compound heterozygous mutation. It is thought that patients with myeloperoxidase deficiency have an increased incidence of malignant tumours. However, they do not have a significantly increased rate of infection, owing to redundancy in peroxidase-mediated immune mechanisms.
242:
219:
1268:. In this respect it is primarily a metabolic enzyme or terminal effector; it has little role in cellular signalling pathways. The overall structure of the four mammalian heme peroxidases (MPO, LPO, EPO and TPO) is almost identical. However, MPO is unique in existing as a catalytic dimer bridged by a disulphide bond. One of the first aspects known of eosinophil peroxidase was that it was highly cationic, as indicated by its high isoelectric point (see Protein). Eosinophil peroxidase has not been characterized by
116:
1387:
141:
1579:, depends on the action of enzymes which catalyze the peroxidase reaction. Eosinophil peroxidase can be found in the primary (azurophilic) granules of human and mammalian leukocytes. Peroxidase localization in leukocytes has been studied throughout the 20th century using staining agents such as benzidine hydrochloride. Before the introduction of specific immunoreactive staining, such chemical indicators of enzymatic activity were commonplace. Following the advent of the
1281:
necessary for function are subjected to strong conservation pressure, while regions distant from the active site undergo genetic drift. This can lead to the specialization or differentiation of function arising from modification of an enzymatic core moiety. For example, the closely related thyroid peroxidase catalyzes a specific oxidation reaction in the biosynthesis of a hormone, while other heme peroxidases fulfill roles in immune defense and redox signalling.
248:
147:
3452:
1252:. It is bound within a loop of eight residues of the heavy chain. Ligands are provided by serine and threonine hydroxyl; backbone carbonyl; and carboxylic acid groups, one of which comes from the light polypeptide chain. The calcium site serves not only as a scaffold for protein folding, but also for proper association of the two chains. In fact, when the calcium ion is removed, the protein
1613:
Having diverged from myeloperoxidase and lactoperoxidase, these three enzymes now perform distinct but not non-overlapping roles; lactoperoxidase helps maintain the sterility of mammalian milk; myeloperoxidase and eosinophil peroxidase inhabit granules and play roles in host defense—an example of how
1335:
bonds. Asp232 and Glu380 of EPO are covalently linked through their terminal oxygen atoms to the modified side chains of the protoporphyrin. For comparison, in myeloperoxidase, there is a third attachment point, Met243 forming a sulphonium ion bridge with the pendant vinyl group on heme. This feature
1244:
heme-containing enzyme. The core of the catalytic domain surrounding the active site consists of six α-helices, five from the heavy polypeptide chain and one from the light. The fold of the enzyme is known as the heme peroxidase fold, conserved among all members of this gene family. However, not all
1276:
of EPO, TPO and LPO as well as high sequence similarity allows us to compare the properties of the three. Myeloperoxidase's characteristics are somewhat different, owing to its multimerization state as well as its alternative heme linkage. Further, a homology model has been created for EPO based on
1523:
can oxidize chloride with any considerable rate. The rate of iodide catalysis is five orders of magnitude greater than the rate of chloride catalysis, for comparison. The mutant of MPO wherein heme-linked Met243 was mutated nonconservatively showed a lack of chlorination ability, implicating this
1210:
into a heavy and a light chain during maturation. However, the two chains are still intimately connected not least of all by the covalently linked heme cofactor. The protein is produced on ribosomes embedded on the surface of the endoplasmic reticulum, since it must be ultimately localized to the
1280:
The fold is highly conserved and seems to be optimized for catalytic function. However, differences exist which unsurprisingly account for differences in substrate specificity among peroxidases. This furcation is commonplace in the study of protein evolution. Structural features which are highly
1390:
Active site of eosinophil peroxidase in the resting (reduced) state. Pictured: Proximal histidine-asparagine interaction (bottom); distal histidine and bound water (top). In the oxidized form, the oxyferryl radical takes the place of the bound solvent molecule, and the halide substrate binds
2492:
Breton-Gorius J, Coquin Y, Guichard J (January 1978). "Cytochemical distinction between azurophils and catalase-containing granules in leukocytes. I. Studies in developing neutrophils and monocytes from patients with myeloperoxidase deficiency: comparison with peroxidase-deficient chicken
2124:
Ulrich M, Petre A, Youhnovski N, Prömm F, Schirle M, Schumm M, Pero RS, Doyle A, Checkel J, Kita H, Thiyagarajan N, Acharya KR, Schmid-Grendelmeier P, Simon HU, Schwarz H, Tsutsui M, Shimokawa H, Bellon G, Lee JJ, Przybylski M, Döring G (October 2008).
1610:. Eosinophil peroxidase is secreted by eosinophil cells into the tissue at the site of infection. Activation of cells in the face of an infection leads to the release of granule contents and externalization of protein and chemical agents from the cell.
2048:
Gioia, De; Ghibaudi, Elena M.; Laurenti, Enzo; Salmona, Mario; Ferrari, R. P. (14 October 1996). "A theoretical three-dimensional model for lactoperoxidase and eosinophil peroxidase, built on the scaffold of the myeloperoxidase X-ray structure".
1407:
takes the oxidation state +4. The activated oxygen may then be transferred to a substrate in order to convert it into a reactive oxygen species. There are three distinct cycles which EPO can undergo. The first is the halogenation cycle:
1106:
are potent oxidizing agents. However, the role of eosinophilic peroxidase seems to be to generate hyphalous acids largely from bromide and iodide rather than chloride, since the former are favored greatly over the latter. The enzyme
1359:
side of the heme group. These include a short water network comprising five molecules; stabilized by hydrogen bonding with histidine, glutamine, and arginine residues. The distal face is used for substrate binding and catalysis.
1474:
The physiological implications of this second mechanism are important. Eosinophil peroxidase has been demonstrated to oxidize tyrosine residues on proteins, which has also been implicated in reactive oxygen signalling cascades.
1546:
of 4.0-4.3. This appears to be the distal histidine residue. The structure of the ternary complex of MPO, cyanide and bromide is thought to be a good model for the compound I-halide complex due to its similar geometry (cf.
1127:(bp). This comprises a 381-bp prosequence, a 333-bp sequence encoding the light chain and a 1,392-bp sequence encoding the heavy chain. In addition to these there is a 452-bp untranslated region at the
2008:
Zederbauer M, FurtmĂĽller PG, Brogioni S, Jakopitsch C, Smulevich G, Obinger C (June 2007). "Heme to protein linkages in mammalian peroxidases: impact on spectroscopic, redox and catalytic properties".
1622:
Specific deficiency of eosinophil peroxidase without concomitant deficiency of myeloperoxidase is rare. In a clinical setting, deficiencies of leukocyte enzymes are conveniently studied by optical
1459:
two one-electron reduction steps to oxidize arbitrary substrates to their radical forms. This process operates on the majority of non-halide substrates. The first step is identical followed by:
1440:
species. It's thought that the pi-cation porphyrin radical undergoes reactivity at the methine bridges connecting the four rings. Compound I reduction in the presence of halides
2089:
FurtmĂĽller PG, Zederbauer M, Jantschko W, Helm J, Bogner M, Jakopitsch C, Obinger C (January 2006). "Active site structure and catalytic mechanisms of human peroxidases".
1575:
Large multicellular organisms engage multiple systems as defensive efforts against infecting bacteria or invading parasites. One strategy, which falls under the domain of
255:
154:
1587:
of many cell types was vigorously investigated. Subsequently, eosinophil peroxidase was found to be localized to primary and secondary granules of the eosinophil.
1111:
is responsible for formation of most of the hypochlorous acid in the body, and eosinophil peroxidase is responsible for reactions involving bromide and iodide.
2768:
1478:
The third and less relevant mechanism is the catalase activity of peroxidases. This mechanism appears to operate only in the absence of one-electron donors.
2711:
727:
77:
708:
1452:
Thus, compound I is reduced back to the enzyme's resting state, and halide ions bound in the distal cavity are oxidized to potent oxidizing agents.
1142:
for human eosinophil peroxidase is an unusually strong promoter. All the major regulatory elements are located within 100 bp upstream of the gene.
2309:"Hereditary eosinophil peroxidase deficiency: immunochemical and spectroscopic studies and evidence for a compound heterozygosity of the defect"
1301:
3472:
2944:
2675:
1764:
1746:
1157:
is only expressed in the bone marrow. At this level, it is more than 30 times the average level of expression over all tissues in the body.
241:
1403:
The basic mechanism of heme peroxidases consists in using hydrogen peroxide to produce an activated form of the heme cofactor, in which
927:
934:
218:
3171:
1733:
1712:
1047:
2704:
140:
115:
3327:
1729:
2864:
1515:(SCN). However, the enzyme prefers bromide over chloride, iodide over bromide and thiocyanate over iodide, with regard to
3442:
1708:
1363:
The crystal structures of MPO have been solved both in native states and with inhibitors bound and are deposited in the
57:
2854:
2409:"Ultrastructural localization of myeloperoxidase in human neutrophil and rabbit heterophil and eosinophil leukocytes"
1309:. Right: modified form of heme cofactor released from peroxidase by protease digestion under nonreducing conditions.
2268:"Thiocyanate is the major substrate for eosinophil peroxidase in physiologic fluids. Implications for cytotoxicity"
1926:
Straub C, Pazdrak K, Young TW, Stafford SJ, Wu Z, Wiktorowicz JE, Haag AM, English RD, Soman KV, Kurosky A (2009).
1789:"Molecular cloning of the human eosinophil peroxidase. Evidence for the existence of a peroxidase multigene family"
254:
153:
3312:
3428:
3415:
3402:
3389:
3376:
3363:
3350:
3100:
2970:
2937:
2697:
1253:
3322:
1535:
binds very tightly to mammalian heme peroxidases. Tight binding directly to heme iron converts the protein to a
247:
146:
3276:
3219:
3083:
2961:
2661:
772:
65:
2565:"Pattern of inheritance in hereditary myeloperoxidase deficiency associated with the R569W missense mutation"
3224:
3088:
2998:
1660:
1325:
1273:
1269:
1036:
753:
3058:
3008:
2906:
2836:
2793:
2721:
1665:
1576:
1386:
1028:
3245:
3164:
2988:
1249:
129:
3317:
2127:"Post-translational tyrosine nitration of eosinophil granule toxins mediated by eosinophil peroxidase"
1391:
alongside that. Not pictured: other bound solvent water molecules. Refer to PDB crystal structures or
1228:
Unlike MPO, heme in EPO is not linked via methionine. This affects the catalytic characteristics (see
1058:
2930:
2874:
2801:
2320:
1211:
granules. The precursor protein goes through the following processing steps before becoming active:
44:
3281:
2849:
2733:
1640:
1580:
1429:
1352:
1166:
Molecular weight: 57 kDa (heavy chain), 11 kDa (light chain) (predicted); 52 kDa, 15 kDa (observed)
1139:
2672:
3482:
3214:
3073:
2657:
2637:
2594:
2545:
2066:
1908:
1120:
1024:
89:
910:
889:
863:
842:
1838:"Functional characterization of the promoter for the gene encoding human eosinophil peroxidase"
1511:
reaction. EPO can take chloride, bromide and iodide as substrates, as well as the pseudohalide
1437:
3477:
2629:
2586:
2537:
2502:
2474:
2430:
2389:
2348:
2289:
2248:
2207:
2158:
2106:
2025:
1957:
1900:
1859:
1818:
1645:
1548:
1380:
1376:
1372:
1368:
1364:
1321:
1306:
1169:
1062:
37:
3260:
3255:
3229:
3157:
2983:
2783:
2621:
2576:
2529:
2464:
2420:
2379:
2338:
2328:
2279:
2238:
2197:
2189:
2148:
2138:
2098:
2058:
2017:
1947:
1939:
1890:
1849:
1808:
1800:
1607:
1087:
334:
265:
209:
164:
2689:
3307:
3291:
3204:
3118:
3113:
3068:
3063:
2978:
2753:
2742:
2679:
1520:
1132:
1108:
1032:
1020:
1016:
309:
2922:
85:
2324:
1351:
residue. These two critical residues ensure that iron has an appropriate Fe(III)/Fe(II)
3456:
3345:
3286:
2953:
2202:
2177:
2153:
2126:
1952:
1927:
1813:
1788:
1623:
1584:
1508:
1265:
1001:
2284:
2267:
2243:
2226:
1854:
1837:
642:
637:
632:
627:
622:
617:
612:
607:
602:
597:
592:
576:
571:
566:
561:
556:
540:
535:
530:
525:
3466:
3250:
3209:
3104:
2910:
2816:
2343:
2308:
1836:
Yamaguchi Y, Zhang DE, Sun Z, Albee EA, Nagata S, Tenen DG, Ackerman SJ (July 1994).
1650:
1614:
the concept of a single chemical function can be harnessed in myriad ways in nature.
1516:
1103:
512:
2070:
1912:
3199:
2826:
2757:
2641:
2549:
1567:
was a G→A transition resulting in a nonconservative mutation at the protein level.
1314:
1192:
997:
327:
106:
69:
2612:
Lanza F (September 1998). "Clinical manifestation of myeloperoxidase deficiency".
2598:
1150:
93:
3423:
3358:
3194:
3021:
2821:
2806:
2773:
2725:
2667:
2425:
2408:
2384:
2368:"Brief Report: Simplified Myeloperoxidase Stain Using Benzidine Dihydrochloride"
2367:
1895:
1878:
1769:
National Center for
Biotechnology Information, U.S. National Library of Medicine
1751:
National Center for
Biotechnology Information, U.S. National Library of Medicine
1599:
1595:
1512:
1241:
1207:
1012:
3451:
2313:
Proceedings of the
National Academy of Sciences of the United States of America
410:
3078:
2957:
2102:
1635:
1348:
1196:
1180:
1124:
1043:
1011:, expressed within these myeloid cells. EPO shares many similarities with its
994:
226:
123:
73:
2520:
Petrides PE (September 1998). "Molecular genetics of peroxidase deficiency".
2333:
3397:
3371:
2887:
2844:
1591:
1344:
1337:
1317:
1054:
1040:
672:
470:
348:
293:
280:
192:
179:
81:
2393:
2211:
2162:
2143:
2110:
2029:
1961:
1943:
1804:
1539:
species. Binding of cyanide requires the deprotonated form of a group with
2633:
2625:
2590:
2541:
2533:
2478:
2434:
2352:
2293:
2252:
2062:
1904:
1863:
1822:
974:
969:
2993:
2811:
2763:
2747:
2581:
2564:
2506:
2453:"Deficiency of eosinophil peroxidase detected by automated cytochemistry"
1655:
1536:
1035:, its activities including the oxidation of halide ions to bacteriocidal
958:
817:
798:
2227:"Eosinophils preferentially use bromide to generate halogenating agents"
1313:
The active site of eosinophil peroxidase contains a single iron atom in
2882:
1552:
1532:
1355:
for catalysis. The sixth ligands of iron are said to be located on the
1290:
1187:
1083:
1004:
784:
739:
2495:
Laboratory
Investigation; A Journal of Technical Methods and Pathology
2469:
2452:
2193:
3410:
3180:
2673:
2021:
1684:
The sodium salt of hypochlorous acid is commonly used as pool bleach.
1066:
990:
942:
694:
1524:
residue or its peculiar functional group in substrate specificity.
1123:
of human eosinophil peroxidase was found to have a length of 2,106
3384:
3138:
3133:
3128:
3123:
2307:
Romano M, Patriarca P, Melo C, Baralle FE, Dri P (December 1994).
1603:
1385:
1332:
1300:
1128:
1091:
657:
653:
3051:
3046:
3041:
3036:
3031:
3026:
3016:
1879:"Human eosinophil peroxidase: purification and characterization"
1455:
However, there is a second cycle wherein compound I can proceed
1404:
61:
3153:
2926:
2693:
2685:
Source: The J. C. Segen
Dictionary of Modern Medicine database.
1928:"Toward the Proteome of the Human Peripheral Blood Eosinophil"
1149:
expression has been characterized and is available online via
1787:
Ten RM, Pease LR, McKean DJ, Bell MP, Gleich GJ (May 1989).
2563:
Nauseef WM, Cogley M, Bock S, Petrides PE (February 1998).
2043:
2041:
2039:
3149:
2225:
Mayeno AN, Curran AJ, Roberts RL, Foote CS (April 1989).
317:
1153:. This dataset indicates that both in humans and mice,
3440:
1428:
where Por denotes the heme cofactor, and • denotes a
482:
3336:
3300:
3269:
3238:
3187:
3099:
2969:
2873:
2835:
2792:
2782:
2732:
903:
882:
856:
835:
2178:"Substrates and products of eosinophil peroxidase"
1725:
1723:
1721:
1704:
1702:
1700:
1336:is absent in EPO and the corresponding residue is
1053:The major function of eosinophil peroxidase is to
1000:, innate immune cells of humans and mammals. This
264:
163:
2003:
2001:
1999:
1997:
1995:
1993:
1991:
1436:. In this state oxygen could be described as an
1027:(TPO). The protein is concentrated in secretory
603:negative regulation of interleukin-10 production
48:, EPO, EPP, EPX-PEN, EPXD, eosinophil peroxidase
2407:Dunn WB, Hardin JH, Spicer SS (December 1968).
2084:
2082:
2080:
1989:
1987:
1985:
1983:
1981:
1979:
1977:
1975:
1973:
1971:
1877:Carlson MG, Peterson CG, Venge P (March 1985).
1563:One of the first well-characterized mutants of
1555:ion also binds tightly, forming low-spin heme.
1272:. However, a direct correspondence between the
1031:within eosinophils. Eosinophil peroxidase is a
623:positive regulation of interleukin-4 production
613:negative regulation of interleukin-5 production
16:Protein-coding gene in the species Homo sapiens
2446:
2444:
1730:GRCm38: Ensembl release 89: ENSMUSG00000052234
1179:Electronic absorption maximum at 413 nm (
3165:
2938:
2705:
1782:
1780:
1778:
8:
2769:Bactericidal permeability-increasing protein
1709:GRCh38: Ensembl release 89: ENSG00000121053
3172:
3158:
3150:
2945:
2931:
2923:
2789:
2712:
2698:
2690:
668:
508:
305:
204:
101:
2660:at the U.S. National Library of Medicine
2580:
2468:
2424:
2383:
2342:
2332:
2283:
2242:
2201:
2152:
2142:
2051:Journal of Biological Inorganic Chemistry
1951:
1894:
1853:
1812:
1432:. This activated state of heme is called
1289:Human EPO is known to exist as a soluble
1248:The calcium ion binding site has typical
1240:Eosinophil peroxidase is a predominately
433:fetal liver hematopoietic progenitor cell
1347:residue, hydrogen bonded directly to an
1343:The fifth ligand of iron is a conserved
1328:is linked covalently to the polypeptide
1102:Hypohalous acids formed from halides or
3447:
2176:van Dalen CJ, Kettle AJ (August 2001).
2091:Archives of Biochemistry and Biophysics
1696:
1677:
2266:Slungaard A, Mahoney JR (March 1991).
18:
1324:cofactor. It is notable in that this
1245:members possess peroxidase activity.
269:
230:
225:
168:
127:
122:
7:
1793:The Journal of Experimental Medicine
1598:-derived cell types (along with the
1507:Eosinophil peroxidase catalyzes the
1176:= 10.31 (predicted); 7.62 (observed)
437:vestibular membrane of cochlear duct
2272:The Journal of Biological Chemistry
2231:The Journal of Biological Chemistry
2131:The Journal of Biological Chemistry
1842:The Journal of Biological Chemistry
1602:) which circulate in the blood and
1264:The protein contains only a single
1206:The polypeptide chain is processed
633:hydrogen peroxide catabolic process
1224:covalent linkage of heme cofactor.
900:
879:
853:
832:
808:
789:
763:
744:
718:
699:
487:
405:
343:
322:
14:
2668:Eosinophil peroxidase on InterPro
1932:Proteomics. Clinical Applications
1277:the X-ray diffraction structure.
3450:
1229:
1199:residues: 315, 351, 443, and 695
1050:of protein amino acid residues.
253:
246:
240:
217:
152:
145:
139:
114:
1250:pentagonal bipyramidal geometry
1069:ions in solution. For example:
1048:post-translational modification
593:cellular oxidant detoxification
1594:, one of two major classes of
471:More reference expression data
379:right hemisphere of cerebellum
1:
2865:Eosinophil-derived neurotoxin
2614:Journal of Molecular Medicine
2522:Journal of Molecular Medicine
2451:Valdés MD, Calero MA (1987).
2285:10.1016/S0021-9258(19)67734-3
2244:10.1016/S0021-9258(18)83599-2
1855:10.1016/S0021-9258(17)32184-1
1590:Eosinophils form part of the
1221:modification of heme cofactor
1039:, the cationic disruption of
643:defense response to bacterium
238:
137:
3473:Genes on human chromosome 17
2569:Journal of Leukocyte Biology
1367:under the accession numbers
1202:One active site per monomer.
628:defense response to nematode
618:response to oxidative stress
2855:Eosinophil cationic protein
2426:10.1182/blood.v32.6.935.935
2385:10.1182/blood.v26.2.215.215
1896:10.4049/jimmunol.134.3.1875
1606:and play critical roles in
1215:ER signal sequence cleavage
3499:
1131:end containing the AATAAA
3328:Michaelis–Menten kinetics
2900:
2366:Kaplow LS (August 1965).
2103:10.1016/j.abb.2005.09.017
1765:"Mouse PubMed Reference:"
1747:"Human PubMed Reference:"
973:
968:
964:
957:
941:
922:
907:
886:
875:
860:
839:
828:
815:
811:
796:
792:
783:
770:
766:
751:
747:
738:
725:
721:
706:
702:
693:
678:
671:
667:
651:
511:
507:
495:
490:
481:
468:
417:
408:
355:
346:
316:
308:
304:
287:
274:
237:
216:
207:
203:
186:
173:
136:
113:
104:
100:
55:
52:
42:
35:
30:
26:
21:
3220:Diffusion-limited enzyme
3084:Iodothyronine deiodinase
2662:Medical Subject Headings
2334:10.1073/pnas.91.26.12496
935:Chr 11: 87.75 – 87.77 Mb
928:Chr 17: 58.19 – 58.21 Mb
638:neutrophil degranulation
3089:Iodotyrosine deiodinase
2999:Cytochrome c peroxidase
2182:The Biochemical Journal
2010:Natural Product Reports
1661:Reactive oxygen species
1037:reactive oxygen species
1007:is encoded by the gene
572:secretory granule lumen
526:oxidoreductase activity
3059:Horseradish peroxidase
3009:Glutathione peroxidase
2907:platelet alpha-granule
2144:10.1074/jbc.m801196200
1944:10.1002/prca.200900043
1805:10.1084/jem.169.5.1757
1666:Antimicrobial peptides
1618:Deficiency and disease
1395:
1310:
1186:Binds 1 equivalent of
3313:Eadie–Hofstee diagram
3246:Allosteric regulation
3004:Eosinophil peroxidase
2989:Fatty-acid peroxidase
2860:Eosinophil peroxidase
2658:Eosinophil+peroxidase
2626:10.1007/s001090050267
2534:10.1007/s001090050269
2063:10.1007/s007750050081
1883:Journal of Immunology
1444:proceeds as follows:
1389:
1304:
1270:X-ray crystallography
987:Eosinophil peroxidase
557:extracellular exosome
375:cerebellar hemisphere
271:11 C|11 52.25 cM
232:Chromosome 11 (mouse)
130:Chromosome 17 (human)
3323:Lineweaver–Burk plot
2802:Alkaline phosphatase
2734:Azurophilic granules
2582:10.1002/jlb.63.2.264
1285:Quaternary structure
598:eosinophil migration
562:extracellular region
2850:Major basic protein
2325:1994PNAS...9112496R
1641:Major basic protein
1581:electron microscope
1517:reaction velocities
1353:reduction potential
1236:Secondary structure
1218:propeptide cleavage
567:extracellular space
541:peroxidase activity
3282:Enzyme superfamily
3215:Enzyme promiscuity
3074:Thyroid peroxidase
2678:2016-03-03 at the
2457:Acta Haematologica
1592:myelocytic lineage
1396:
1311:
1274:absorption spectra
1260:Tertiary structure
1121:open reading frame
1025:thyroid peroxidase
773:ENSMUSG00000052234
586:Biological process
550:Cellular component
519:Molecular function
421:tibiofemoral joint
383:right uterine tube
3438:
3437:
3147:
3146:
2920:
2919:
2896:
2895:
2784:Specific granules
2470:10.1159/000205890
2319:(26): 12496–500.
2194:10.1042/bj3580233
1938:(10): 1151–1173.
1646:Secretory pathway
1577:cellular immunity
1365:Protein Data Bank
1322:protoporphyrin IX
1307:protoporphyrin IX
1256:out of solution.
1170:Isoelectric point
1140:promoter sequence
1063:hydrogen peroxide
1057:the formation of
993:found within the
984:
983:
980:
979:
953:
952:
918:
917:
897:
896:
871:
870:
850:
849:
824:
823:
805:
804:
779:
778:
760:
759:
734:
733:
715:
714:
663:
662:
536:metal ion binding
503:
502:
499:
498:
477:
476:
464:
463:
402:
401:
387:prefrontal cortex
371:bone marrow cells
300:
299:
199:
198:
3490:
3455:
3454:
3446:
3318:Hanes–Woolf plot
3261:Enzyme activator
3256:Enzyme inhibitor
3230:Enzyme catalysis
3174:
3167:
3160:
3151:
2984:NADPH peroxidase
2947:
2940:
2933:
2924:
2790:
2754:serine proteases
2720:Contents of the
2714:
2707:
2700:
2691:
2646:
2645:
2609:
2603:
2602:
2584:
2560:
2554:
2553:
2517:
2511:
2510:
2489:
2483:
2482:
2472:
2448:
2439:
2438:
2428:
2404:
2398:
2397:
2387:
2363:
2357:
2356:
2346:
2336:
2304:
2298:
2297:
2287:
2263:
2257:
2256:
2246:
2222:
2216:
2215:
2205:
2173:
2167:
2166:
2156:
2146:
2137:(42): 28629–40.
2121:
2115:
2114:
2086:
2075:
2074:
2045:
2034:
2033:
2022:10.1039/b604178g
2005:
1966:
1965:
1955:
1923:
1917:
1916:
1898:
1874:
1868:
1867:
1857:
1833:
1827:
1826:
1816:
1784:
1773:
1772:
1761:
1755:
1754:
1743:
1737:
1727:
1716:
1706:
1685:
1682:
1608:immune responses
1519:. In fact, only
1430:chemical radical
1326:prosthetic group
1059:hypohalous acids
966:
965:
937:
930:
913:
901:
892:
880:
876:RefSeq (protein)
866:
854:
845:
833:
809:
790:
764:
745:
719:
700:
669:
608:defense response
509:
488:
473:
413:
411:Top expressed in
406:
351:
349:Top expressed in
344:
323:
306:
296:
283:
272:
257:
250:
244:
233:
221:
205:
195:
182:
171:
156:
149:
143:
132:
118:
102:
96:
47:
40:
19:
3498:
3497:
3493:
3492:
3491:
3489:
3488:
3487:
3463:
3462:
3461:
3449:
3441:
3439:
3434:
3346:Oxidoreductases
3332:
3308:Enzyme kinetics
3296:
3292:List of enzymes
3265:
3234:
3205:Catalytic triad
3183:
3178:
3148:
3143:
3095:
3069:Myeloperoxidase
3064:Lactoperoxidase
2979:NADH peroxidase
2965:
2954:Oxidoreductases
2951:
2921:
2916:
2892:
2869:
2831:
2778:
2743:Myeloperoxidase
2728:
2718:
2680:Wayback Machine
2654:
2649:
2611:
2610:
2606:
2562:
2561:
2557:
2519:
2518:
2514:
2491:
2490:
2486:
2450:
2449:
2442:
2406:
2405:
2401:
2365:
2364:
2360:
2306:
2305:
2301:
2265:
2264:
2260:
2224:
2223:
2219:
2188:(Pt 1): 233–9.
2175:
2174:
2170:
2123:
2122:
2118:
2088:
2087:
2078:
2047:
2046:
2037:
2007:
2006:
1969:
1925:
1924:
1920:
1876:
1875:
1871:
1848:(30): 19410–9.
1835:
1834:
1830:
1786:
1785:
1776:
1763:
1762:
1758:
1745:
1744:
1740:
1728:
1719:
1707:
1698:
1694:
1689:
1688:
1683:
1679:
1674:
1632:
1620:
1573:
1561:
1544:
1530:
1521:myeloperoxidase
1505:
1497:
1493:
1489:
1485:
1469:
1466:+ RH → + R + H
1463:+ RH → + R + H
1423:
1419:
1415:
1401:
1299:
1287:
1262:
1238:
1208:proteolytically
1163:
1145:The profile of
1133:polyadenylation
1117:
1109:myeloperoxidase
1098:
1095:
1081:
1077:
1033:heme peroxidase
1021:lactoperoxidase
1017:myeloperoxidase
975:View/Edit Mouse
970:View/Edit Human
933:
926:
923:Location (UCSC)
909:
888:
862:
841:
754:ENSG00000121053
647:
581:
545:
469:
460:
455:
451:
447:
443:
441:pituitary gland
439:
435:
431:
427:
423:
409:
398:
395:Brodmann area 9
393:
389:
385:
381:
377:
373:
369:
365:
363:trabecular bone
361:
347:
291:
278:
270:
260:
259:
258:
251:
231:
208:Gene location (
190:
177:
169:
159:
158:
157:
150:
128:
105:Gene location (
94:EPX - orthologs
56:
43:
36:
17:
12:
11:
5:
3496:
3494:
3486:
3485:
3480:
3475:
3465:
3464:
3460:
3459:
3436:
3435:
3433:
3432:
3419:
3406:
3393:
3380:
3367:
3354:
3340:
3338:
3334:
3333:
3331:
3330:
3325:
3320:
3315:
3310:
3304:
3302:
3298:
3297:
3295:
3294:
3289:
3284:
3279:
3273:
3271:
3270:Classification
3267:
3266:
3264:
3263:
3258:
3253:
3248:
3242:
3240:
3236:
3235:
3233:
3232:
3227:
3222:
3217:
3212:
3207:
3202:
3197:
3191:
3189:
3185:
3184:
3179:
3177:
3176:
3169:
3162:
3154:
3145:
3144:
3142:
3141:
3136:
3131:
3126:
3121:
3116:
3110:
3108:
3097:
3096:
3094:
3093:
3092:
3091:
3086:
3076:
3071:
3066:
3061:
3056:
3055:
3054:
3049:
3044:
3039:
3034:
3029:
3024:
3019:
3006:
3001:
2996:
2991:
2986:
2981:
2975:
2973:
2967:
2966:
2952:
2950:
2949:
2942:
2935:
2927:
2918:
2917:
2915:
2914:
2901:
2898:
2897:
2894:
2893:
2891:
2890:
2885:
2879:
2877:
2871:
2870:
2868:
2867:
2862:
2857:
2852:
2847:
2841:
2839:
2833:
2832:
2830:
2829:
2824:
2819:
2814:
2809:
2804:
2798:
2796:
2787:
2780:
2779:
2777:
2776:
2771:
2766:
2761:
2750:
2745:
2739:
2737:
2730:
2729:
2719:
2717:
2716:
2709:
2702:
2694:
2688:
2687:
2682:
2670:
2665:
2653:
2652:External links
2650:
2648:
2647:
2620:(10): 676–81.
2604:
2555:
2528:(10): 688–98.
2512:
2493:heterophils".
2484:
2440:
2399:
2358:
2299:
2278:(8): 4903–10.
2258:
2237:(10): 5660–8.
2217:
2168:
2116:
2097:(2): 199–213.
2076:
2057:(5): 476–485.
2035:
1967:
1918:
1869:
1828:
1799:(5): 1757–69.
1774:
1756:
1738:
1717:
1695:
1693:
1690:
1687:
1686:
1676:
1675:
1673:
1670:
1669:
1668:
1663:
1658:
1653:
1648:
1643:
1638:
1631:
1628:
1624:flow cytometry
1619:
1616:
1585:ultrastructure
1572:
1569:
1560:
1557:
1542:
1529:
1526:
1509:haloperoxidase
1504:
1501:
1500:
1499:
1495:
1491:
1487:
1483:
1472:
1471:
1467:
1464:
1450:
1449:
1426:
1425:
1421:
1417:
1413:
1400:
1397:
1298:
1295:
1286:
1283:
1266:modular domain
1261:
1258:
1237:
1234:
1226:
1225:
1222:
1219:
1216:
1204:
1203:
1200:
1190:
1184:
1177:
1167:
1162:
1159:
1116:
1113:
1100:
1099:
1093:
1079:
1075:
1073:
1002:oxidoreductase
982:
981:
978:
977:
972:
962:
961:
955:
954:
951:
950:
948:
946:
939:
938:
931:
924:
920:
919:
916:
915:
905:
904:
898:
895:
894:
884:
883:
877:
873:
872:
869:
868:
858:
857:
851:
848:
847:
837:
836:
830:
826:
825:
822:
821:
813:
812:
806:
803:
802:
794:
793:
787:
781:
780:
777:
776:
768:
767:
761:
758:
757:
749:
748:
742:
736:
735:
732:
731:
723:
722:
716:
713:
712:
704:
703:
697:
691:
690:
685:
680:
676:
675:
665:
664:
661:
660:
649:
648:
646:
645:
640:
635:
630:
625:
620:
615:
610:
605:
600:
595:
589:
587:
583:
582:
580:
579:
574:
569:
564:
559:
553:
551:
547:
546:
544:
543:
538:
533:
528:
522:
520:
516:
515:
505:
504:
501:
500:
497:
496:
493:
492:
485:
479:
478:
475:
474:
466:
465:
462:
461:
459:
458:
454:
450:
446:
445:chondrocranium
442:
438:
434:
430:
426:
422:
418:
415:
414:
403:
400:
399:
397:
396:
392:
388:
384:
380:
376:
372:
368:
364:
360:
356:
353:
352:
340:
339:
331:
320:
314:
313:
310:RNA expression
302:
301:
298:
297:
289:
285:
284:
276:
273:
268:
262:
261:
252:
245:
239:
235:
234:
229:
223:
222:
214:
213:
201:
200:
197:
196:
188:
184:
183:
175:
172:
167:
161:
160:
151:
144:
138:
134:
133:
126:
120:
119:
111:
110:
98:
97:
54:
50:
49:
41:
33:
32:
28:
27:
24:
23:
15:
13:
10:
9:
6:
4:
3:
2:
3495:
3484:
3481:
3479:
3476:
3474:
3471:
3470:
3468:
3458:
3453:
3448:
3444:
3430:
3426:
3425:
3420:
3417:
3413:
3412:
3407:
3404:
3400:
3399:
3394:
3391:
3387:
3386:
3381:
3378:
3374:
3373:
3368:
3365:
3361:
3360:
3355:
3352:
3348:
3347:
3342:
3341:
3339:
3335:
3329:
3326:
3324:
3321:
3319:
3316:
3314:
3311:
3309:
3306:
3305:
3303:
3299:
3293:
3290:
3288:
3287:Enzyme family
3285:
3283:
3280:
3278:
3275:
3274:
3272:
3268:
3262:
3259:
3257:
3254:
3252:
3251:Cooperativity
3249:
3247:
3244:
3243:
3241:
3237:
3231:
3228:
3226:
3223:
3221:
3218:
3216:
3213:
3211:
3210:Oxyanion hole
3208:
3206:
3203:
3201:
3198:
3196:
3193:
3192:
3190:
3186:
3182:
3175:
3170:
3168:
3163:
3161:
3156:
3155:
3152:
3140:
3137:
3135:
3132:
3130:
3127:
3125:
3122:
3120:
3117:
3115:
3112:
3111:
3109:
3106:
3105:peroxiredoxin
3102:
3098:
3090:
3087:
3085:
3082:
3081:
3080:
3077:
3075:
3072:
3070:
3067:
3065:
3062:
3060:
3057:
3053:
3050:
3048:
3045:
3043:
3040:
3038:
3035:
3033:
3030:
3028:
3025:
3023:
3020:
3018:
3015:
3012:
3011:
3010:
3007:
3005:
3002:
3000:
2997:
2995:
2992:
2990:
2987:
2985:
2982:
2980:
2977:
2976:
2974:
2972:
2968:
2963:
2959:
2955:
2948:
2943:
2941:
2936:
2934:
2929:
2928:
2925:
2913:
2912:
2911:dense granule
2908:
2903:
2902:
2899:
2889:
2886:
2884:
2881:
2880:
2878:
2876:
2872:
2866:
2863:
2861:
2858:
2856:
2853:
2851:
2848:
2846:
2843:
2842:
2840:
2838:
2834:
2828:
2825:
2823:
2820:
2818:
2817:NADPH oxidase
2815:
2813:
2810:
2808:
2805:
2803:
2800:
2799:
2797:
2795:
2791:
2788:
2785:
2781:
2775:
2772:
2770:
2767:
2765:
2762:
2759:
2755:
2751:
2749:
2746:
2744:
2741:
2740:
2738:
2735:
2731:
2727:
2723:
2715:
2710:
2708:
2703:
2701:
2696:
2695:
2692:
2686:
2683:
2681:
2677:
2674:
2671:
2669:
2666:
2663:
2659:
2656:
2655:
2651:
2643:
2639:
2635:
2631:
2627:
2623:
2619:
2615:
2608:
2605:
2600:
2596:
2592:
2588:
2583:
2578:
2574:
2570:
2566:
2559:
2556:
2551:
2547:
2543:
2539:
2535:
2531:
2527:
2523:
2516:
2513:
2508:
2504:
2500:
2496:
2488:
2485:
2480:
2476:
2471:
2466:
2462:
2458:
2454:
2447:
2445:
2441:
2436:
2432:
2427:
2422:
2419:(6): 935–44.
2418:
2414:
2410:
2403:
2400:
2395:
2391:
2386:
2381:
2377:
2373:
2369:
2362:
2359:
2354:
2350:
2345:
2340:
2335:
2330:
2326:
2322:
2318:
2314:
2310:
2303:
2300:
2295:
2291:
2286:
2281:
2277:
2273:
2269:
2262:
2259:
2254:
2250:
2245:
2240:
2236:
2232:
2228:
2221:
2218:
2213:
2209:
2204:
2199:
2195:
2191:
2187:
2183:
2179:
2172:
2169:
2164:
2160:
2155:
2150:
2145:
2140:
2136:
2132:
2128:
2120:
2117:
2112:
2108:
2104:
2100:
2096:
2092:
2085:
2083:
2081:
2077:
2072:
2068:
2064:
2060:
2056:
2052:
2044:
2042:
2040:
2036:
2031:
2027:
2023:
2019:
2016:(3): 571–84.
2015:
2011:
2004:
2002:
2000:
1998:
1996:
1994:
1992:
1990:
1988:
1986:
1984:
1982:
1980:
1978:
1976:
1974:
1972:
1968:
1963:
1959:
1954:
1949:
1945:
1941:
1937:
1933:
1929:
1922:
1919:
1914:
1910:
1906:
1902:
1897:
1892:
1889:(3): 1875–9.
1888:
1884:
1880:
1873:
1870:
1865:
1861:
1856:
1851:
1847:
1843:
1839:
1832:
1829:
1824:
1820:
1815:
1810:
1806:
1802:
1798:
1794:
1790:
1783:
1781:
1779:
1775:
1770:
1766:
1760:
1757:
1752:
1748:
1742:
1739:
1735:
1731:
1726:
1724:
1722:
1718:
1714:
1710:
1705:
1703:
1701:
1697:
1691:
1681:
1678:
1671:
1667:
1664:
1662:
1659:
1657:
1654:
1652:
1651:Peroxiredoxin
1649:
1647:
1644:
1642:
1639:
1637:
1634:
1633:
1629:
1627:
1625:
1617:
1615:
1611:
1609:
1605:
1601:
1597:
1593:
1588:
1586:
1582:
1578:
1570:
1568:
1566:
1558:
1556:
1554:
1550:
1545:
1538:
1534:
1527:
1525:
1522:
1518:
1514:
1510:
1502:
1481:
1480:
1479:
1476:
1465:
1462:
1461:
1460:
1458:
1453:
1447:
1446:
1445:
1443:
1439:
1435:
1431:
1411:
1410:
1409:
1406:
1398:
1394:
1388:
1384:
1382:
1378:
1374:
1370:
1366:
1361:
1358:
1354:
1350:
1346:
1341:
1339:
1334:
1331:
1327:
1323:
1319:
1316:
1308:
1303:
1296:
1294:
1292:
1284:
1282:
1278:
1275:
1271:
1267:
1259:
1257:
1255:
1251:
1246:
1243:
1235:
1233:
1231:
1223:
1220:
1217:
1214:
1213:
1212:
1209:
1201:
1198:
1194:
1191:
1189:
1185:
1182:
1178:
1175:
1171:
1168:
1165:
1164:
1160:
1158:
1156:
1152:
1148:
1143:
1141:
1136:
1134:
1130:
1126:
1122:
1114:
1112:
1110:
1105:
1104:pseudohalides
1097:
1089:
1085:
1072:
1071:
1070:
1068:
1064:
1060:
1056:
1051:
1049:
1045:
1042:
1038:
1034:
1030:
1026:
1022:
1018:
1015:peroxidases,
1014:
1010:
1006:
1003:
999:
996:
992:
988:
976:
971:
967:
963:
960:
956:
949:
947:
944:
940:
936:
932:
929:
925:
921:
914:
912:
906:
902:
899:
893:
891:
885:
881:
878:
874:
867:
865:
859:
855:
852:
846:
844:
838:
834:
831:
829:RefSeq (mRNA)
827:
820:
819:
814:
810:
807:
801:
800:
795:
791:
788:
786:
782:
775:
774:
769:
765:
762:
756:
755:
750:
746:
743:
741:
737:
730:
729:
724:
720:
717:
711:
710:
705:
701:
698:
696:
692:
689:
686:
684:
681:
677:
674:
670:
666:
659:
655:
650:
644:
641:
639:
636:
634:
631:
629:
626:
624:
621:
619:
616:
614:
611:
609:
606:
604:
601:
599:
596:
594:
591:
590:
588:
585:
584:
578:
575:
573:
570:
568:
565:
563:
560:
558:
555:
554:
552:
549:
548:
542:
539:
537:
534:
532:
529:
527:
524:
523:
521:
518:
517:
514:
513:Gene ontology
510:
506:
494:
489:
486:
484:
480:
472:
467:
456:
452:
448:
444:
440:
436:
432:
428:
424:
420:
419:
416:
412:
407:
404:
394:
390:
386:
382:
378:
374:
370:
366:
362:
358:
357:
354:
350:
345:
342:
341:
338:
336:
332:
330:
329:
325:
324:
321:
319:
315:
311:
307:
303:
295:
290:
286:
282:
277:
267:
263:
256:
249:
243:
236:
228:
224:
220:
215:
211:
206:
202:
194:
189:
185:
181:
176:
166:
162:
155:
148:
142:
135:
131:
125:
121:
117:
112:
108:
103:
99:
95:
91:
87:
83:
79:
75:
71:
67:
63:
59:
51:
46:
39:
34:
29:
25:
20:
3424:Translocases
3421:
3408:
3395:
3382:
3369:
3359:Transferases
3356:
3343:
3200:Binding site
3013:
3003:
2904:
2859:
2827:Cathelicidin
2758:Proteinase 3
2726:granulocytes
2684:
2617:
2613:
2607:
2575:(2): 264–9.
2572:
2568:
2558:
2525:
2521:
2515:
2501:(1): 21–31.
2498:
2494:
2487:
2460:
2456:
2416:
2412:
2402:
2378:(2): 215–9.
2375:
2371:
2361:
2316:
2312:
2302:
2275:
2271:
2261:
2234:
2230:
2220:
2185:
2181:
2171:
2134:
2130:
2119:
2094:
2090:
2054:
2050:
2013:
2009:
1935:
1931:
1921:
1886:
1882:
1872:
1845:
1841:
1831:
1796:
1792:
1768:
1759:
1750:
1741:
1680:
1621:
1612:
1589:
1574:
1564:
1562:
1540:
1531:
1506:
1477:
1473:
1456:
1454:
1451:
1448:+ X → + HOX
1441:
1433:
1427:
1402:
1392:
1362:
1356:
1342:
1329:
1318:complexation
1315:tetradentate
1312:
1288:
1279:
1263:
1254:precipitates
1247:
1239:
1227:
1205:
1193:Glycosylated
1173:
1154:
1146:
1144:
1137:
1118:
1101:
1052:
1008:
998:granulocytes
986:
985:
908:
887:
861:
840:
816:
797:
771:
752:
726:
707:
687:
682:
531:heme binding
333:
326:
53:External IDs
3195:Active site
2971:1.11.1.1-14
2958:peroxidases
2822:Collagenase
2807:Lactoferrin
2774:Collagenase
1600:lymphocytes
1596:bone-marrow
1513:thiocyanate
1297:Active site
1230:Active site
1023:(LPO), and
1013:orthologous
429:granulocyte
425:bone marrow
367:bone marrow
292:87,766,362
279:87,754,826
191:58,205,174
178:58,192,726
31:Identifiers
3467:Categories
3398:Isomerases
3372:Hydrolases
3239:Regulation
3079:Deiodinase
2837:Eosinophil
2794:Neutrophil
2463:(4): 265.
1736:, May 2017
1715:, May 2017
1692:References
1636:Eosinophil
1528:Inhibitors
1503:Substrates
1434:compound I
1393:refs. and.
1349:asparagine
1197:asparagine
1181:Soret band
1125:base pairs
1046:, and the
1044:cell walls
995:eosinophil
337:(ortholog)
74:HomoloGene
3483:EC 1.11.1
3277:EC number
3101:1.11.1.15
2905:see also
2888:Histamine
2845:Cathepsin
2748:Defensins
1438:oxyferryl
1399:Mechanism
1345:histidine
1338:threonine
1242:α-helical
1041:bacterial
911:NP_031972
890:NP_000493
864:NM_007946
843:NM_000502
673:Orthologs
577:cytoplasm
82:GeneCards
3478:Proteins
3301:Kinetics
3225:Cofactor
3188:Activity
2994:Catalase
2875:Basophil
2812:Lysozyme
2764:Lysozyme
2752:neutral
2722:granules
2676:Archived
2394:14332483
2212:11485572
2163:18694936
2111:16288970
2071:24903600
2030:17534531
1962:21048890
1913:34660087
1732:–
1711:–
1656:Catalase
1630:See also
1571:Cytology
1537:low-spin
1195:at four
1135:signal.
1055:catalyze
1029:granules
959:Wikidata
652:Sources:
359:testicle
3457:Biology
3411:Ligases
3181:Enzymes
2883:Heparin
2642:8847256
2634:9766845
2591:9468285
2550:7789099
2542:9766847
2479:3122494
2435:5749754
2353:7809065
2321:Bibcode
2294:2002037
2253:2538427
2203:1222052
2154:2661412
1953:2967046
1905:3918110
1864:8034708
1823:2541222
1814:2189302
1734:Ensembl
1713:Ensembl
1559:Mutants
1553:nitrite
1551:). The
1533:Cyanide
1320:with a
1291:monomer
1188:calcium
1161:Protein
1019:(MPO),
1005:protein
785:UniProt
740:Ensembl
679:Species
658:QuickGO
449:cochlea
312:pattern
38:Aliases
3443:Portal
3385:Lyases
2664:(MeSH)
2640:
2632:
2599:598367
2597:
2589:
2548:
2540:
2507:202802
2505:
2477:
2433:
2392:
2351:
2341:
2292:
2251:
2210:
2200:
2161:
2151:
2109:
2069:
2028:
1960:
1950:
1911:
1903:
1862:
1821:
1811:
1583:, the
1490:→ + O
1420:→ + H
1379:, and
1357:distal
1305:Left:
1151:BioGPS
1067:halide
991:enzyme
989:is an
945:search
943:PubMed
818:P49290
799:P11678
695:Entrez
483:BioGPS
453:spleen
391:spleen
70:107569
62:131399
3337:Types
2964:1.11)
2638:S2CID
2595:S2CID
2546:S2CID
2413:Blood
2372:Blood
2344:45465
2067:S2CID
1909:S2CID
1672:Notes
1604:lymph
1333:ester
1061:from
728:13861
688:Mouse
683:Human
654:Amigo
457:blood
335:Mouse
328:Human
275:Start
210:Mouse
174:Start
170:17q22
107:Human
78:20144
3429:list
3422:EC7
3416:list
3409:EC6
3403:list
3396:EC5
3390:list
3383:EC4
3377:list
3370:EC3
3364:list
3357:EC2
3351:list
3344:EC1
2786:(2°)
2736:(1°)
2630:PMID
2587:PMID
2538:PMID
2503:PMID
2475:PMID
2431:PMID
2390:PMID
2349:PMID
2290:PMID
2249:PMID
2208:PMID
2159:PMID
2107:PMID
2026:PMID
1958:PMID
1901:PMID
1860:PMID
1819:PMID
1549:1D7W
1405:iron
1381:1D7W
1377:1D2V
1373:1D5L
1369:1CXP
1138:The
1119:The
1115:Gene
1088:HOBr
1065:and
709:8288
318:Bgee
266:Band
227:Chr.
165:Band
124:Chr.
58:OMIM
3014:GPX
2724:of
2622:doi
2577:doi
2530:doi
2465:doi
2421:doi
2380:doi
2339:PMC
2329:doi
2280:doi
2276:266
2239:doi
2235:264
2198:PMC
2190:doi
2186:358
2149:PMC
2139:doi
2135:283
2099:doi
2095:445
2059:doi
2018:doi
1948:PMC
1940:doi
1891:doi
1887:134
1850:doi
1846:269
1809:PMC
1801:doi
1797:169
1565:EPX
1494:+ H
1482:+ H
1457:via
1412:+ H
1330:via
1232:).
1155:EPX
1147:EPX
1009:EPX
491:n/a
288:End
187:End
90:OMA
86:EPX
66:MGI
45:EPX
22:EPX
3469::
2962:EC
2956::
2909:,
2636:.
2628:.
2618:76
2616:.
2593:.
2585:.
2573:63
2571:.
2567:.
2544:.
2536:.
2526:76
2524:.
2499:38
2497:.
2473:.
2461:78
2459:.
2455:.
2443:^
2429:.
2417:32
2415:.
2411:.
2388:.
2376:26
2374:.
2370:.
2347:.
2337:.
2327:.
2317:91
2315:.
2311:.
2288:.
2274:.
2270:.
2247:.
2233:.
2229:.
2206:.
2196:.
2184:.
2180:.
2157:.
2147:.
2133:.
2129:.
2105:.
2093:.
2079:^
2065:.
2053:.
2038:^
2024:.
2014:24
2012:.
1970:^
1956:.
1946:.
1934:.
1930:.
1907:.
1899:.
1885:.
1881:.
1858:.
1844:.
1840:.
1817:.
1807:.
1795:.
1791:.
1777:^
1767:.
1749:.
1720:^
1699:^
1541:pK
1383:.
1375:,
1371:,
1340:.
1293:.
1129:3'
1090:+
1086:→
1084:Br
1082:+
656:/
294:bp
281:bp
193:bp
180:bp
88:;
84::
80:;
76::
72:;
68::
64:;
60::
3445::
3431:)
3427:(
3418:)
3414:(
3405:)
3401:(
3392:)
3388:(
3379:)
3375:(
3366:)
3362:(
3353:)
3349:(
3173:e
3166:t
3159:v
3139:6
3134:5
3129:4
3124:3
3119:2
3114:1
3107:)
3103:(
3052:8
3047:7
3042:6
3037:5
3032:4
3027:3
3022:2
3017:1
2960:(
2946:e
2939:t
2932:v
2760:)
2756:(
2713:e
2706:t
2699:v
2644:.
2624::
2601:.
2579::
2552:.
2532::
2509:.
2481:.
2467::
2437:.
2423::
2396:.
2382::
2355:.
2331::
2323::
2296:.
2282::
2255:.
2241::
2214:.
2192::
2165:.
2141::
2113:.
2101::
2073:.
2061::
2055:1
2032:.
2020::
1964:.
1942::
1936:3
1915:.
1893::
1866:.
1852::
1825:.
1803::
1771:.
1753:.
1543:a
1498:O
1496:2
1492:2
1488:2
1486:O
1484:2
1470:O
1468:2
1442:X
1424:O
1422:2
1418:2
1416:O
1414:2
1183:)
1174:I
1172:p
1096:O
1094:2
1092:H
1080:2
1078:O
1076:2
1074:H
212:)
109:)
92::
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