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TP53

S Wikipedije, slobodne enciklopedije
(Preusmjereno sa P53)
TP53
Dostupne strukture
PDBPretraga ortologa: PDBe RCSB
Spisak PDB ID kodova

4QO1, 1A1U, 1AIE, 1C26, 1DT7, 1GZH, 1H26, 1HS5, 1KZY, 1MA3, 1OLG, 1OLH, 1PES, 1PET, 1SAE, 1SAF, 1SAK, 1SAL, 1TSR, 1TUP, 1UOL, 1XQH, 1YC5, 1YCQ, 1YCR, 1YCS, 2AC0, 2ADY, 2AHI, 2ATA, 2B3G, 2BIM, 2BIN, 2BIO, 2BIP, 2BIQ, 2FEJ, 2FOJ, 2FOO, 2GS0, 2H1L, 2H2D, 2H2F, 2H4F, 2H4H, 2H4J, 2H59, 2J0Z, 2J10, 2J11, 2J1W, 2J1X, 2J1Y, 2J1Z, 2J20, 2J21, 2K8F, 2L14, 2LY4, 2MEJ, 2MWO, 2MWP, 2MZD, 2OCJ, 2PCX, 2RUK, 2VUK, 2WGX, 2X0U, 2X0V, 2X0W, 2XWR, 2YBG, 2YDR, 2Z5S, 2Z5T, 3D05, 3D06, 3D07, 3D08, 3D09, 3D0A, 3DAB, 3DAC, 3IGK, 3IGL, 3KMD, 3KZ8, 3LW1, 3OQ5, 3PDH, 3Q01, 3Q05, 3Q06, 3SAK, 3TG5, 3TS8, 3ZME, 4AGL, 4AGM, 4AGN, 4AGO, 4AGP, 4AGQ, 4BUZ, 4BV2, 4HFZ, 4HJE, 4IBQ, 4IBS, 4IBT, 4IBU, 4IBV, 4IBW, 4IBY, 4IBZ, 4IJT, 4KVP, 4LO9, 4LOE, 4LOF, 4MZI, 4MZR, 4X34, 4ZZJ, 5AOL, 5ABA, 5AOK, 2MWY, 5A7B, 5AOJ, 5AOI, 5ECG, 5AB9, 4FZ3, 4RP6, 4XR8, 5AOM, 4RP7, 5HOU, 5HP0, 5HPD, 5LGY, 5G4M, 5G4O, 5G4N, 5BUA

Identifikatori
AliasiTP53
Vanjski ID-jeviOMIM: 191170 MGI: 98834 HomoloGene: 460 GeneCards: TP53
Lokacija gena (čovjek)
Hromosom 17 (čovjek)
Hrom.Hromosom 17 (čovjek)[1]
Hromosom 17 (čovjek)
Genomska lokacija za TP53
Genomska lokacija za TP53
Bend17p13.1Početak7,661,779 bp[1]
Kraj7,687,538 bp[1]
Lokacija gena (miš)
Hromosom 11 (miš)
Hrom.Hromosom 11 (miš)[2]
Hromosom 11 (miš)
Genomska lokacija za TP53
Genomska lokacija za TP53
Bend11 B3|11 42.83 cMPočetak69,471,185 bp[2]
Kraj69,482,699 bp[2]
Obrazac RNK ekspresije


Više referentnih podataka o ekspresiji
Ontologija gena
Molekularna funkcija protein N-terminus binding
GO:0001131, GO:0001151, GO:0001130, GO:0001204 DNA-binding transcription factor activity
protein self-association
core promoter sequence-specific DNA binding
GO:0001200, GO:0001133, GO:0001201 DNA-binding transcription factor activity, RNA polymerase II-specific
protein phosphatase binding
ATP binding
transcription factor binding
vezivanje iona metala
protein phosphatase 2A binding
vezivanje enzima
vezivanje iona cinka
chromatin binding
protease binding
oštećeno vezivanje sa DNK
GO:0001948, GO:0016582 vezivanje za proteine
histone acetyltransferase binding
copper ion binding
protein kinase binding
chaperone binding
GO:0001077, GO:0001212, GO:0001213, GO:0001211, GO:0001205 DNA-binding transcription activator activity, RNA polymerase II-specific
receptor tyrosine kinase binding
p53 binding
vezivanje identičnih proteina
protein heterodimerization activity
ubiquitin protein ligase binding
RNA polymerase II transcription regulatory region sequence-specific DNA binding
vezivanje sa DNK
GO:0000980 RNA polymerase II cis-regulatory region sequence-specific DNA binding
TFIID-class transcription factor complex binding
mRNA 3'-UTR binding
histone deacetylase binding
disordered domain specific binding
promoter-specific chromatin binding
histone deacetylase regulator activity
protein homodimerization activity
MDM2/MDM4 family protein binding
Ćelijska komponenta citoplazma
mitohondrija
jedro
nuclear body
transcription factor TFIID complex
nuclear matrix
replication fork
Jedarce
Endoplazmatski retikulum
nukleoplazma
mitochondrial matrix
PML body
citosol
intracellular anatomical structure
transcription regulator complex
GO:0009327 makromolekulani kompleks
site of double-strand break
Biološki proces positive regulation of histone deacetylation
DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest
rhythmic process
replicative senescence
negative regulation of telomerase activity
oligodendrocyte apoptotic process
cellular response to DNA damage stimulus
intrinsic apoptotic signaling pathway
positive regulation of neuron apoptotic process
regulation of mitochondrial membrane permeability
positive regulation of reactive oxygen species metabolic process
cellular response to ionizing radiation
positive regulation of thymocyte apoptotic process
negative regulation of helicase activity
ćelijski ciklus
Ras protein signal transduction
Ćelijska proliferacija
cellular response to hypoxia
negative regulation of cell population proliferation
Popravak ekscizijom nukleotida
cellular response to glucose starvation
GO:0009373 regulation of transcription, DNA-templated
GO:1904576 response to antibiotic
transcription, DNA-templated
ER overload response
GO:0060469, GO:0009371 positive regulation of transcription, DNA-templated
negative regulation of cell growth
intrinsic apoptotic signaling pathway by p53 class mediator
positive regulation of peptidyl-tyrosine phosphorylation
GO:0022415 viral process
response to gamma radiation
negative regulation of fibroblast proliferation
positive regulation of intrinsic apoptotic signaling pathway
Ćelijska diferencijacija
determination of adult lifespan
positive regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress
cellular response to UV
DNA damage response, signal transduction by p53 class mediator
negative regulation of apoptotic process
protein tetramerization
oxidative stress-induced premature senescence
positive regulation of release of cytochrome c from mitochondria
circadian behavior
GO:0045996 negative regulation of transcription, DNA-templated
GO:0034613 protein localization
intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator
positive regulation of execution phase of apoptosis
multicellular organism development
positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway
GO:1901313 positive regulation of gene expression
mitotic G1 DNA damage checkpoint signaling
positive regulation of protein oligomerization
positive regulation of apoptotic process
entrainment of circadian clock by photoperiod
response to X-ray
GO:0003257, GO:0010735, GO:1901228, GO:1900622, GO:1904488 positive regulation of transcription by RNA polymerase II
base-excision repair
DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator
regulation of cell cycle G2/M phase transition
proteasome-mediated ubiquitin-dependent protein catabolic process
regulation of signal transduction by p53 class mediator
GO:0097285 apoptoza
transcription by RNA polymerase II
positive regulation of protein export from nucleus
GO:0010703, GO:0010702 programirana ćelijska smrt
regulation of apoptotic process
protein deubiquitination
phosphatidylinositol-mediated signaling
GO:1901227 negative regulation of transcription by RNA polymerase II
Autofagija
mRNA transcription
cytokine-mediated signaling pathway
positive regulation of RNA polymerase II transcription preinitiation complex assembly
RNA polymerase II preinitiation complex assembly
protein homotetramerization
GO:0034622 protein-containing complex assembly
cellular response to gamma radiation
signal transduction by p53 class mediator
cellular response to actinomycin D
positive regulation of pri-miRNA transcription by RNA polymerase II
positive regulation of production of miRNAs involved in gene silencing by miRNA
in utero embryonic development
somitogenesis
release of cytochrome c from mitochondria
hematopoietic progenitor cell differentiation
T cell proliferation involved in immune response
B cell lineage commitment
T cell lineage commitment
response to ischemia
double-strand break repair
GO:0044324, GO:0003256, GO:1901213, GO:0046019, GO:0046020, GO:1900094, GO:0061216, GO:0060994, GO:1902064, GO:0003258, GO:0072212 regulation of transcription by RNA polymerase II
protein import into nucleus
GO:0001306 response to oxidative stress
transforming growth factor beta receptor signaling pathway
Gastrulacija
negative regulation of neuroblast proliferation
central nervous system development
heart development
Jednodnevni biološki ritam
negative regulation of DNA replication
rRNA transcription
response to UV
response to salt stress
embryo development ending in birth or egg hatching
negative regulation of gene expression
positive regulation of cardiac muscle cell apoptotic process
cerebellum development
negative regulation of transforming growth factor beta receptor signaling pathway
T cell differentiation in thymus
regulation of tissue remodeling
multicellular organism growth
positive regulation of mitochondrial membrane permeability
positive regulation of transcription from RNA polymerase II promoter in response to stress
regulation of cell population proliferation
mitochondrial DNA repair
regulation of DNA damage response, signal transduction by p53 class mediator
regulation of neuron apoptotic process
negative regulation of proteolysis
negative regulation of mitotic cell cycle
bone marrow development
embryonic organ development
protein stabilization
GO:0051312, GO:0007083 chromosome organization
neuron apoptotic process
regulation of cell cycle
hematopoietic stem cell differentiation
interferon-gamma-mediated signaling pathway
cardiac septum morphogenesis
positive regulation of transcription from RNA polymerase II promoter in response to hypoxia
positive regulation of programmed necrotic cell death
intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress
regulation of thymocyte apoptotic process
GO:0060554, GO:0060555 necroptosis
cellular response to UV-C
negative regulation of mitophagy
regulation of mitochondrial membrane permeability involved in apoptotic process
regulation of intrinsic apoptotic signaling pathway by p53 class mediator
negative regulation of production of miRNAs involved in gene silencing by miRNA
negative regulation of glucose catabolic process to lactate via pyruvate
intrinsic apoptotic signaling pathway in response to hypoxia
regulation of fibroblast apoptotic process
negative regulation of reactive oxygen species metabolic process
regulation of cellular senescence
Izvori:Amigo / QuickGO
Ortolozi
VrsteČovjekMiš
Entrez
Ensembl
UniProt
RefSeq (mRNK)
NM_001276761
NM_000546
NM_001126112
NM_001126113
NM_001126114

NM_001126115
NM_001126116
NM_001126117
NM_001126118
NM_001276695
NM_001276696
NM_001276697
NM_001276698
NM_001276699
NM_001276760

NM_001127233
NM_011640

RefSeq (bjelančevina)
NP_000537
NP_001119584
NP_001119585
NP_001119586
NP_001119587

NP_001119588
NP_001119589
NP_001119590
NP_001263624
NP_001263625
NP_001263626
NP_001263627
NP_001263628
NP_001263689
NP_001263690

NP_001120705
NP_035770

Lokacija (UCSC)Chr 17: 7.66 – 7.69 MbChr 11: 69.47 – 69.48 Mb
PubMed pretraga[3][4]
Wikipodaci
Pogledaj/uredi – čovjekPogledaj/uredi – miš

Tumorski protein P53, znan i kao p53, ćelijski tumorski-antigen p53 (UniProt ime), domaćinski gen,[5] fosfoprotein p53, tumorski supresor p53, antigen NY-CO-13 ili transformacijski vezani protein 53 (TRP53), je bilo koja proteinska izoforma proteina kodiranog homolognim genom u različitim organizmima, kao što su TP53 (ljudi) i Trp53 (miševi). Ovaj homolog (za koji se prvobitno mislilo da je, i o njemu se često govori, kao jedan protein) presudan je u višim kičmenjacima, gdje sprečava stvaranje karcinoma, te stoga funkcionira kao supresor tumora.[6] Kao takav, p53 je opisan kao "čuvar genoma" zbog svoje uloge u očuvanju stabilnosti, sprečavanjem mutacije genoma.[7] Stoga se TP53 koriste za označavanje imena gena TP53 i razlikovanje od proteina koje kodiraju (klasificiran je kao gen za supresiju tumora).[8][9][10][11][12]

Naziv 'p53' dobio je 1979. godine opisujući prividnu molekulskuu masu. Analiza SDS-PAGE pokazuje da je riječ o proteinu od 53-kilodaltona (kDa). Međutim, stvarna masa proteina p53 pune dužine (p53α) na osnovu zbroja mase aminokiselinskih ostataka iznosi samo 43,7 kDa. Ova razlika je zbog velikog broja prolinskih ostataka u proteinu, koji usporavaju njegovu migraciju na SDS-PAGE, čineći ga tako težim nego što zapravo jeste.[13] Pored proteina pune dužine, ljudski gen TP53 kodira najmanje 15 izoformnih proteina, veličine od 3,5 do 43,7 kDa. Svi ovi proteini p53 nazivaju se izoformama p53.[6] Gen TP53 je najčešće mutirani gen (> 50%) u karcinomu čovjeka, što ukazuje da TP53 ima presudnu ulogu u sprečavanju stvaranja karcinoma. Gen TP53 kodira proteine koji se vežu za DNK i regulišu ekspresiju, kako bi se spriječile mutacije genoma.[14]

U ljudi se gen TP53 nalazi na kratkom kraku hromosoma 17 (17p13.1).[8][9][10][11] Proteže na 20 kb, s nekodirajućim egzonom 1 i vrlo dugim intronom od 10 kb. Kodirajuća sekvenca sadrži pet regija koje imauju visok stupanj konzerviranosti kod kičmenjaka, pretežno u egzonima 2, 5, 6, 7 i 8, ali sekvence pronađene kod beskičmenjaka pokazuju samo sličnost sa sisarskim TP53.[15]Ortolozi TP53[16] su identificirani kod većine sisara za koje su dostupni potpuni podaci o genomu.

Ljudski gen TP53

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U ljudi, uobičajeni polimorfizam uključuje zamjenu arginina za prolin na kodonskom položaju 72. Mnoge studije su istraživale genetičku vezu između ove varijacije i osjetljivost na rak; međutim, rezultati su kontroverzni. Naprimjer, meta-analiza iz 2009. godine nije pokazala vezu za rak vrata maternice.[17] Studija iz 2011. otkrila je da je mutacija prolina TP53 imala dubok utjecaj na rizik od raka gušterače kod muškaraca.[18] Studija na arapskim ženama otkrila je da je homozigotnost prolina na kodonu TP53 povezana sa smanjenim rizikom od raka dojke.[19] Jedno istraživanje sugeriralo je da polimorfizmi kodona TP53 , MDM2 SNP309 i A2164G mogu biti grupno povezani sa osjetljivošću na nerofarinksni karcinom i da je MDM2 SNP309 u kombinaciji s kodonom 72 'TP53' može ubrzati razvoj neorofarinksnog karcinoma kod žena.[20] Metaanalize iz 2011. nisu otkrile značajne veze između polimorfizama kodona 72 TP53 i oba rizika od raka debelog creva[21][22] i rizik od karcinoma endometrija.[23]

Struktura

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Shema poznatih proteinskih domena u p53. (NLS = Signal jedarne lokalizacije).
Kristalna struktura četiri p53 DNK vezujuća domena (kako se nalazi u bioaktivnom homotetrameru)

p53 ima sedam domena:

  1. kiseli transkripcijsko-aktivacijski domen (TAD) N-kraja, poznat i kao aktivacijski domen 1 (AD1), koji aktivira faktore transkripcije. N-kraj sadrži dva komplementarna domena aktivacije transkripcije, od kojih je glavni na ostacima 1-42, a manji na ostacima 55-75, posebno uključen u regulaciju nekoliko proapoptoznih gena.[24]
  2. aktivacijski domen 2 (AD2) važan za apoptoznu aktivnost: ostaci 43–63.
  3. prolinom bogati domen važan za apoptotsku aktivnost p53 jedarnom eksportnom putem MAPK: ostaci 64–92.
  4. centralni dome DNK - veznog jezgra (DBD). Sadrži jedan atom cinka i nekoliko argininskih aminokiselina: ostaci 102–292. Ovo područje odgovorno je za vezivanje p53 ko-represora LMO3.[25]
  5. Signalizacija jedarne lokalizacije (NLS), ostaci 316–325.
  6. domen homooligomerizacije (OF): ostaci 307–355. Tetramerizacija je bitna za aktivnost p53 in vivo.
  7. C-terminal uključen u regulaciju vezanja DNK centralnog domena: ostaci 356–393.[26]

Mutacije koje deaktiviraju p53 u raku obično se javljaju u DBD. Većina ovih mutacija uništava sposobnost proteina da se veže za svoje ciljne sekvence DNK i na taj način sprečava transkripcijsku aktivaciju ovih gena. Kao takve, mutacije u DBD-u su recesivne mutacije sa gubitakom funkcije. Molekule p53 s mutacijama u OD smanjuju se s divlji tip p53 i sprečavaju ih da aktiviraju transkripciju. Stoga mutacije OD imaju dominantan negativan efekat na funkciju p53.

Divlji tip p53 je labilni protein, koji sadrži presavijene i nestrukturirane regije, koje funkcioniraju na sinergijski način.[27]

Funkcija

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Oštećenje i popravak DNK

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p53 ima ulogu u regulaciji ili napredovanju tokom ćelijskog ciklusa, apoptoza i genomske stabilnosti pomoću nekoliko mehanizama:

  • Može aktivirati popravak DNK kada DNK pretrpi oštećenje. Stoga može biti važan faktor u starenju.[28]
  • Može zaustaviti rast držanjem ćelijskog ciklusana G1/S regulacijskoj tački na prepoznavanju oštećenja DNK – ako zadrži ćeliju dovoljno dugo, proteini za obnavljanje DNK će imati vrijeme da popravi štetu i ćeliji će biti omogućeno da nastavi ćelijski ciklus.
  • Može pokrenuti apoptozu (tj. progrmiranu ćelijsku smrt) ako se pokaže da je oštećenje DNK nepopravljivo.
  • Od suštinske je važnosti za odgovor starenja na kratke telomere .
Put p53: U normalnoj ćeliji, p53 je inaktiviran svojim negativnim regulatorom, mdm2. Nakon oštećenja DNK ili drugih stresova, različiti putevi će dovesti do disocijacije kompleksa p53 i mdm2. Jednom aktiviran, p53 izazvat će zaustavljanje ćelijskog ciklusa kako bi omogućio ili popravak i preživljavanje ćelije ili apoptozu da odbaci oštećenu ćeliju. Nije poznat način na koji p53 čini ovaj izbor.

WAF1 / CIP1 kodiranje za p21 i stotine drugih nizvodnih gena p21 (WAF1) veže se za G1 –x S / CDK (CDK4/CDK6, CDK2 i CDK1) kompleksi (važne molekule za G1 / S tranziciju u ćelijskom ciklusu) koji inhibiraju njihovu aktivnost.

Kada je p21 (WAF1) složen sa CDK2, ćelija ne može nastaviti ćelijske diobe do slijedeće faze. Mutant p53 više neće vezati DNK na učinkovit način i kao posljedica toga, protein p21 neće biti dostupan kao "zaustavni signal" za diobu ćelija.[29] Studije ljudskih embrionskih matičnih ćelija (hESC) obično opisuju nefunkcionalnu os p53-p21 G1 / S puta kontrolne tačke s naknadnim značajem za regulaciju ćelijskog ciklusa i odgovor na oštećenje DNK (DDR). Važno je da je p21 iRNK jasno prisutna i povećana regulacija nakon DDR-a u hESC-ima, ali protein p21 nije moguće otkriti. U ovom tipu ćelija, p53 aktivira brojne mikroRNK (poput miR-302a, miR-302b, miR-302c i miR-302d), koje direktno inhibiraju ekspresiju p21 u hESCs.

Protein p21 veže se direktno za ciklin-CDK komplekse, koji pokreću ćelijski ciklus i inhibira njihovu kinaznu aktivnost, uzrokujući tako zaustavljanje ćelijskog ciklusa, kako bi se omogućilo popravak. Pritom p21 također može posredovati zaustavljanje rasta povezano s diferencijacijom i trajnije zaustavljanje rasta povezano sa ćelijskom senescencijom. Gen p21 sadrži nekoliko elemenata odgovora p53 koji posreduju u direktnom vezivanju proteina p53, što rezultira transkripcijskom aktivacijom gena koji kodira protein p21.

Putevi p53 i RB1 povezani su putem p14ARF, što povećava mogućnost da se mogu međusobno regulirati.[30]

Ekspresiju p53 može podstaknuti UV-svjetlost, koja također uzrokuje oštećenje DNK. U ovom slučaju, p53 može inicirati događaje koji vode do sunčanja.[31][32]

Interakcije

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Pokazano je da p53 uspostavlja interakcije sa:

Takođert pogledajte

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Reference

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000141510 - Ensembl, maj 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000059552 - Ensembl, maj 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Toufektchan, E.; Toledo, F. (2018). "The Guardian of the Genome Revisited: P53 Downregulates Genes Required for Telomere Maintenance, DNA Repair, and Centromere Structure". Cancers. 10 (5): 135. doi:10.3390/cancers10050135. PMC 5977108. PMID 29734785.
  6. ^ a b Surget S, Khoury MP, Bourdon JC (decembar 2013). "Uncovering the role of p53 splice variants in human malignancy: a clinical perspective". OncoTargets and Therapy. 7: 57–68. doi:10.2147/OTT.S53876. PMC 3872270. PMID 24379683.
  7. ^ Read AP, Strachan T (1999). "Chapter 18: Cancer Genetics". Human molecular genetics 2. New York: Wiley. ISBN 978-0-471-33061-5.
  8. ^ a b Matlashewski G, Lamb P, Pim D, Peacock J, Crawford L, Benchimol S (decembar 1984). "Isolation and characterization of a human p53 cDNA clone: expression of the human p53 gene". The EMBO Journal. 3 (13): 3257–62. doi:10.1002/j.1460-2075.1984.tb02287.x. PMC 557846. PMID 6396087.
  9. ^ a b Isobe M, Emanuel BS, Givol D, Oren M, Croce CM (1986). "Localization of gene for human p53 tumour antigen to band 17p13". Nature. 320 (6057): 84–5. Bibcode:1986Natur.320...84I. doi:10.1038/320084a0. PMID 3456488. S2CID 4310476.
  10. ^ a b Kern SE, Kinzler KW, Bruskin A, Jarosz D, Friedman P, Prives C, Vogelstein B (juni 1991). "Identification of p53 as a sequence-specific DNA-binding protein". Science. 252 (5013): 1708–11. Bibcode:1991Sci...252.1708K. doi:10.1126/science.2047879. PMID 2047879. S2CID 19647885.
  11. ^ a b McBride OW, Merry D, Givol D (januar 1986). "The gene for human p53 cellular tumor antigen is located on chromosome 17 short arm (17p13)". Proceedings of the National Academy of Sciences of the United States of America. 83 (1): 130–4. Bibcode:1986PNAS...83..130M. doi:10.1073/pnas.83.1.130. PMC 322805. PMID 3001719.
  12. ^ Greška kod citiranja: Nevaljana oznaka <ref>; nije naveden tekst za reference s imenom Bourdon
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