RYR1

RYR1
Identifikatori
Aliasi	RYR1
Vanjski ID-jevi	OMIM: 180901 MGI: 99659 HomoloGene: 68069 GeneCards: RYR1
Lokacija gena (čovjek)
Hrom.	Hromosom 19 (čovjek)
Kraj	38,595,273 bp
Lokacija gena (miš)
Hrom.	Hromosom 7 (miš)
Kraj	29,125,179 bp
Obrazac RNK ekspresije
	Više referentnih podataka o ekspresiji
Ontologija gena
Molekularna funkcija	• voltage-gated calcium channel activity; • calcium channel activity; • calmodulin binding; • protease binding; • ion channel activity; • GO:0001948, GO:0016582 vezivanje za proteine; • vezivanje enzima; • calcium-release channel activity; • ryanodine-sensitive calcium-release channel activity; • calcium-induced calcium release activity; • calcium ion binding; • nucleotide binding; • ATP binding; • vezivanje iona metala;
Ćelijska komponenta	• citoplazma; • integral component of membrane; • membrana; • I band; • T-tubule; • ćelijska membrana; • integral component of plasma membrane; • Sarkoplazmatski retikulum; • junctional sarcoplasmic reticulum membrane; • terminal cisterna; • smooth endoplasmic reticulum; • cell cortex; • junctional membrane complex; • Egzosom; • integral component of organelle membrane; • ryanodine receptor complex; • sarcoplasmic reticulum membrane; • Z disc; • cytoplasmic vesicle membrane; • GO:0009327 makromolekulani kompleks; • Kalcijski kanal; • Sarkolema;
Biološki proces	• ossification involved in bone maturation; • regulation of cardiac conduction; • response to hypoxia; • Mišićna kontrakcija; • release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; • regulation of cytosolic calcium ion concentration; • outflow tract morphogenesis; • cellular calcium ion homeostasis; • ion transport; • multicellular organism development; • ion transmembrane transport; • skeletal muscle fiber development; • calcium ion transmembrane transport; • response to caffeine; • calcium ion transport; • skin development; • transmembrane transport; • cellular response to caffeine; • protein homotetramerization; • cellular response to calcium ion; • release of sequestered calcium ion into cytosol; • GO:0015915 transport;
	Izvori:Amigo / QuickGO
Ortolozi
	6261
	20190
	ENSG00000196218
	ENSMUSG00000030592
	P21817
	E9PZQ0
	NM_000540; NM_001042723
	NM_009109
	NP_000531; NP_001036188
	NP_033135
	Wikipodaci
Pogledaj/uredi – čovjek	Pogledaj/uredi – miš

Rijanodinski receptor 1 (RYR-1), znan i kao kanal za oslobađanje kalcija iz skeletnih mišića ili receptor rijanodinskog tipa skeletnih mišića je jedan izklase rijanodinskih receptora i proteina koji se prvenstveno nalazi u skeletnim mišićima. Taj protein koji je kod ljudi kodiran genom RYR1 sa hromosoma 19.^[5]^[6]

Aminokiselinska sekvenca uredi

Dužina polipeptidnog lanca je 5.038 aminokiselina, a molekulska težina 565.176 Da.^[6]

C: Cistein

D: Asparaginska kiselina

E: Glutaminska kiselina

F: Fenilalanin

G: Glicin

H: Histidin

I: Izoleucin

K: Lizin

L: Leucin

M: Metionin

N: Asparagin

P: Prolin

Q: Glutamin

R: Arginin

S: Serin

T: Treonin

V: Valin

W: Triptofan

Y: Tirozin

10	20	30	40	50
MGDAEGEDEV	QFLRTDDEVV	LQCSATVLKE	QLKLCLAAEG	FGNRLCFLEP
TSNAQNVPPD	LAICCFVLEQ	SLSVRALQEM	LANTVEAGVE	SSQGGGHRTL
LYGHAILLRH	AHSRMYLSCL	TTSRSMTDKL	AFDVGLQEDA	TGEACWWTMH
PASKQRSEGE	KVRVGDDIIL	VSVSSERYLH	LSTASGELQV	DASFMQTLWN
MNPICSRCEE	GFVTGGHVLR	LFHGHMDECL	TISPADSDDQ	RRLVYYEGGA
VCTHARSLWR	LEPLRISWSG	SHLRWGQPLR	VRHVTTGQYL	ALTEDQGLVV
VDASKAHTKA	TSFCFRISKE	KLDVAPKRDV	EGMGPPEIKY	GESLCFVQHV
ASGLWLTYAA	PDPKALRLGV	LKKKAMLHQE	GHMDDALSLT	RCQQEESQAA
RMIHSTNGLY	NQFIKSLDSF	SGKPRGSGPP	AGTALPIEGV	ILSLQDLIIY
FEPPSEDLQH	EEKQSKLRSL	RNRQSLFQEE	GMLSMVLNCI	DRLNVYTTAA
HFAEFAGEEA	AESWKEIVNL	LYELLASLIR	GNRSNCALFS	TNLDWLVSKL
DRLEASSGIL	EVLYCVLIES	PEVLNIIQEN	HIKSIISLLD	KHGRNHKVLD
VLCSLCVCNG	VAVRSNQDLI	TENLLPGREL	LLQTNLINYV	TSIRPNIFVG
RAEGTTQYSK	WYFEVMVDEV	TPFLTAQATH	LRVGWALTEG	YTPYPGAGEG
WGGNGVGDDL	YSYGFDGLHL	WTGHVARPVT	SPGQHLLAPE	DVISCCLDLS
VPSISFRING	CPVQGVFESF	NLDGLFFPVV	SFSAGVKVRF	LLGGRHGEFK
FLPPPGYAPC	HEAVLPRERL	HLEPIKEYRR	EGPRGPHLVG	PSRCLSHTDF
VPCPVDTVQI	VLPPHLERIR	EKLAENIHEL	WALTRIEQGW	TYGPVRDDNK
RLHPCLVDFH	SLPEPERNYN	LQMSGETLKT	LLALGCHVGM	ADEKAEDNLK
KTKLPKTYMM	SNGYKPAPLD	LSHVRLTPAQ	TTLVDRLAEN	GHNVWARDRV
GQGWSYSAVQ	DIPARRNPRL	VPYRLLDEAT	KRSNRDSLCQ	AVRTLLGYGY
NIEPPDQEPS	QVENQSRCDR	VRIFRAEKSY	TVQSGRWYFE	FEAVTTGEMR
VGWARPELRP	DVELGADELA	YVFNGHRGQR	WHLGSEPFGR	PWQPGDVVGC
MIDLTENTII	FTLNGEVLMS	DSGSETAFRE	IEIGDGFLPV	CSLGPGQVGH
LNLGQDVSSL	RFFAICGLQE	GFEPFAINMQ	RPVTTWFSKG	LPQFEPVPLE
HPHYEVSRVD	GTVDTPPCLR	LTHRTWGSQN	SLVEMLFLRL	SLPVQFHQHF
RCTAGATPLA	PPGLQPPAED	EARAAEPDPD	YENLRRSAGG	WSEAENGKEG
TAKEGAPGGT	PQAGGEAQPA	RAENEKDATT	EKNKKRGFLF	KAKKVAMMTQ
PPATPTLPRL	PHDVVPADNR	DDPEIILNTT	TYYYSVRVFA	GQEPSCVWAG
WVTPDYHQHD	MSFDLSKVRV	VTVTMGDEQG	NVHSSLKCSN	CYMVWGGDFV
SPGQQGRISH	TDLVIGCLVD	LATGLMTFTA	NGKESNTFFQ	VEPNTKLFPA
VFVLPTHQNV	IQFELGKQKN	IMPLSAAMFQ	SERKNPAPQC	PPRLEMQMLM
PVSWSRMPNH	FLQVETRRAG	ERLGWAVQCQ	EPLTMMALHI	PEENRCMDIL
ELSERLDLQR	FHSHTLRLYR	AVCALGNNRV	AHALCSHVDQ	AQLLHALEDA
HLPGPLRAGY	YDLLISIHLE	SACRSRRSML	SEYIVPLTPE	TRAITLFPPG
RSTENGHPRH	GLPGVGVTTS	LRPPHHFSPP	CFVAALPAAG	AAEAPARLSP
AIPLEALRDK	ALRMLGEAVR	DGGQHARDPV	GGSVEFQFVP	VLKLVSTLLV
MGIFGDEDVK	QILKMIEPEV	FTEEEEEEDE	EEEGEEEDEE	EKEEDEEETA
QEKEDEEKEE	EEAAEGEKEE	GLEEGLLQMK	LPESVKLQMC	HLLEYFCDQE
LQHRVESLAA	FAERYVDKLQ	ANQRSRYGLL	IKAFSMTAAE	TARRTREFRS
PPQEQINMLL	QFKDGTDEED	CPLPEEIRQD	LLDFHQDLLA	HCGIQLDGEE
EEPEEETTLG	SRLMSLLEKV	RLVKKKEEKP	EEERSAEESK	PRSLQELVSH
MVVRWAQEDF	VQSPELVRAM	FSLLHRQYDG	LGELLRALPR	AYTISPSSVE
DTMSLLECLG	QIRSLLIVQM	GPQEENLMIQ	SIGNIMNNKV	FYQHPNLMRA
LGMHETVMEV	MVNVLGGGES	KEIRFPKMVT	SCCRFLCYFC	RISRQNQRSM
FDHLSYLLEN	SGIGLGMQGS	TPLDVAAASV	IDNNELALAL	QEQDLEKVVS
YLAGCGLQSC	PMLVAKGYPD	IGWNPCGGER	YLDFLRFAVF	VNGESVEENA
NVVVRLLIRK	PECFGPALRG	EGGSGLLAAI	EEAIRISEDP	ARDGPGIRRD
RRREHFGEEP	PEENRVHLGH	AIMSFYAALI	DLLGRCAPEM	HLIQAGKGEA
LRIRAILRSL	VPLEDLVGII	SLPLQIPTLG	KDGALVQPKM	SASFVPDHKA
SMVLFLDRVY	GIENQDFLLH	VLDVGFLPDM	RAAASLDTAT	FSTTEMALAL
NRYLCLAVLP	LITKCAPLFA	GTEHRAIMVD	SMLHTVYRLS	RGRSLTKAQR
DVIEDCLMSL	CRYIRPSMLQ	HLLRRLVFDV	PILNEFAKMP	LKLLTNHYER
CWKYYCLPTG	WANFGVTSEE	ELHLTRKLFW	GIFDSLAHKK	YDPELYRMAM
PCLCAIAGAL	PPDYVDASYS	SKAEKKATVD	AEGNFDPRPV	ETLNVIIPEK
LDSFINKFAE	YTHEKWAFDK	IQNNWSYGEN	IDEELKTHPM	LRPYKTFSEK
DKEIYRWPIK	ESLKAMIAWE	WTIEKAREGE	EEKTEKKKTR	KISQSAQTYD
PREGYNPQPP	DLSAVTLSRE	LQAMAEQLAE	NYHNTWGRKK	KQELEAKGGG
THPLLVPYDT	LTAKEKARDR	EKAQELLKFL	QMNGYAVTRG	LKDMELDSSS
IEKRFAFGFL	QQLLRWMDIS	QEFIAHLEAV	VSSGRVEKSP	HEQEIKFFAK
ILLPLINQYF	TNHCLYFLST	PAKVLGSGGH	ASNKEKEMIT	SLFCKLAALV
RHRVSLFGTD	APAVVNCLHI	LARSLDARTV	MKSGPEIVKA	GLRSFFESAS
EDIEKMVENL	RLGKVSQART	QVKGVGQNLT	YTTVALLPVL	TTLFQHIAQH
QFGDDVILDD	VQVSCYRTLC	SIYSLGTTKN	TYVEKLRPAL	GECLARLAAA
MPVAFLEPQL	NEYNACSVYT	TKSPRERAIL	GLPNSVEEMC	PDIPVLERLM
ADIGGLAESG	ARYTEMPHVI	EITLPMLCSY	LPRWWERGPE	APPSALPAGA
PPPCTAVTSD	HLNSLLGNIL	RIIVNNLGID	EASWMKRLAV	FAQPIVSRAR
PELLQSHFIP	TIGRLRKRAG	KVVSEEEQLR	LEAKAEAQEG	ELLVRDEFSV
LCRDLYALYP	LLIRYVDNNR	AQWLTEPNPS	AEELFRMVGE	IFIYWSKSHN
FKREEQNFVV	QNEINNMSFL	TADNKSKMAK	AGDIQSGGSD	QERTKKKRRG
DRYSVQTSLI	VATLKKMLPI	GLNMCAPTDQ	DLITLAKTRY	ALKDTDEEVR
EFLHNNLHLQ	GKVEGSPSLR	WQMALYRGVP	GREEDADDPE	KIVRRVQEVS
AVLYYLDQTE	HPYKSKKAVW	HKLLSKQRRR	AVVACFRMTP	LYNLPTHRAC
NMFLESYKAA	WILTEDHSFE	DRMIDDLSKA	GEQEEEEEEV	EEKKPDPLHQ
LVLHFSRTAL	TEKSKLDEDY	LYMAYADIMA	KSCHLEEGGE	NGEAEEEVEV
SFEEKQMEKQ	RLLYQQARLH	TRGAAEMVLQ	MISACKGETG	AMVSSTLKLG
ISILNGGNAE	VQQKMLDYLK	DKKEVGFFQS	IQALMQTCSV	LDLNAFERQN
KAEGLGMVNE	DGTVINRQNG	EKVMADDEFT	QDLFRFLQLL	CEGHNNDFQN
YLRTQTGNTT	TINIIICTVD	YLLRLQESIS	DFYWYYSGKD	VIEEQGKRNF
SKAMSVAKQV	FNSLTEYIQG	PCTGNQQSLA	HSRLWDAVVG	FLHVFAHMMM
KLAQDSSQIE	LLKELLDLQK	DMVVMLLSLL	EGNVVNGMIA	RQMVDMLVES
SSNVEMILKF	FDMFLKLKDI	VGSEAFQDYV	TDPRGLISKK	DFQKAMDSQK
QFSGPEIQFL	LSCSEADENE	MINCEEFANR	FQEPARDIGF	NVAVLLTNLS
EHVPHDPRLH	NFLELAESIL	EYFRPYLGRI	EIMGASRRIE	RIYFEISETN
RAQWEMPQVK	ESKRQFIFDV	VNEGGEAEKM	ELFVSFCEDT	IFEMQIAAQI
SEPEGEPETD	EDEGAGAAEA	GAEGAEEGAA	GLEGTAATAA	AGATARVVAA
AGRALRGLSY	RSLRRRVRRL	RRLTAREAAT	AVAALLWAAV	TRAGAAGAGA
AAGALGLLWG	SLFGGGLVEG	AKKVTVTELL	AGMPDPTSDE	VHGEQPAGPG
GDADGEGASE	GAGDAAEGAG	DEEEAVHEAG	PGGADGAVAV	TDGGPFRPEG
AGGLGDMGDT	TPAEPPTPEG	SPILKRKLGV	DGVEEELPPE	PEPEPEPELE
PEKADAENGE	KEEVPEPTPE	PPKKQAPPSP	PPKKEEAGGE	FWGELEVQRV
KFLNYLSRNF	YTLRFLALFL	AFAINFILLF	YKVSDSPPGE	DDMEGSAAGD
VSGAGSGGSS	GWGLGAGEEA	EGDEDENMVY	YFLEESTGYM	EPALRCLSLL
HTLVAFLCII	GYNCLKVPLV	IFKREKELAR	KLEFDGLYIT	EQPEDDDVKG
QWDRLVLNTP	SFPSNYWDKF	VKRKVLDKHG	DIYGRERIAE	LLGMDLATLE
ITAHNERKPN	PPPGLLTWLM	SIDVKYQIWK	FGVIFTDNSF	LYLGWYMVMS
LLGHYNNFFF	AAHLLDIAMG	VKTLRTILSS	VTHNGKQLVM	TVGLLAVVVY
LYTVVAFNFF	RKFYNKSEDE	DEPDMKCDDM	MTCYLFHMYV	GVRAGGGIGD
EIEDPAGDEY	ELYRVVFDIT	FFFFVIVILL	AIIQGLIIDA	FGELRDQQEQ
VKEDMETKCF	ICGIGSDYFD	TTPHGFETHT	LEEHNLANYM	FFLMYLINKD
ETEHTGQESY	VWKMYQERCW	DFFPAGDCFR	KQYEDQLS

Funkcija uredi

RYR1 funkcioniše kao kalcijev kanal za oslobađanje u sarkoplazmatski retikulum, kao i kao veza između sarkoplazmatskog retikuluma i poprečne tubule.^[7] RYR1 je povezan sa dihidropiridinskim receptorom (kalcijski kanali L-tipa) unutar sarkolema T-tubula, koji se otvara kao odgovor na depolarizaciju, i na taj način efektivno znači da se RYR1 kanal otvara kao odgovor na depolarizaciju ćelije .

RYR1 ima signalnu ulogu tokom embrionske miogeneze skeletnih mišića. Postoji korelacija između Ca2+ posredovane RYR1 signalizacije i ekspresije više molekula uključenih u ključne miogene signalne puteve.^[8] Od toga, više od 10 različito eksprimiranih gena pripada porodici Wnt koji su neophodni za diferencijaciju. Ovo se poklapa sa zapažanjem da se bez prisutnog RYR1 mišićne ćelije pojavljuju u manjim grupama, nedovoljno su razvijene i nemaju organizaciju. Sastav tipa vlakana je također pogođen, s manje mišićnih vlakana tipa 1, kada su smanjene količine RYR1.^[9] Ovi nalazi pokazuju da RYR1 ima nekontraktilnu ulogu tokom razvoja mišića.

RYR1 je mehanički vezan za neuromišićne spojeve za biološki proces izazvan otpuštanjem kalcija-kalcijem. Dok su signali izvedeni iz nerava potrebni za distribuciju klastera acetilholinskih receptora, postoje dokazi koji ukazuju na to da je aktivnost RYR1 važan posrednik u formiranju i oblikovanju ovih receptora tokom embrijskog razvoja..^[10] Čini se da signali iz nerva i aktivnosti RYR1 uravnotežuju jedni druge. Kada se RYR1 eliminiše, klasteri acetilholinskih receptora pojavljuju se u abnormalno uskom obrascu, ali bez signala iz nerva, klasteri su raštrkani i široki. Iako je njihova direktna uloga još uvijek nepoznata, RYR1 je neophodan za pravilnu distribuciju klastera acetilholinskih receptora.

Klinički značaj uredi

Mutacije u genu RYR1 povezane su sa osjetljivošću na malignu hipertermiju , bolest centralnog jezgra, miopatiju minijezgra sa vanjskom oftalmoplegijom i samarićansku miopatiju, benignu kongenitalnu miopatiju.^[11]Xdemonstrirani su alternativno prerađeni primarni transkripti koji kodiraju različite izoforme.^[7] Dantrolen može biti jedini poznati lijek koji je efikasan u slučajevima maligne hipertermije.

Interakcije uredi

Pokazalo se da RYR1 interraguje sa:

Također pogledajte uredi

Rijanodinski receptor

Reference uredi

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000196218 - Ensembl, maj 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000030592 - Ensembl, maj 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Fujii J, Otsu K, Zorzato F, de Leon S, Khanna VK, Weiler JE, O'Brien PJ, MacLennan DH (July 1991). "Identification of a mutation in porcine ryanodine receptor associated with malignant hyperthermia". Science. 253 (5018): 448–51. Bibcode:1991Sci...253..448F. doi:10.1126/science.1862346. PMID 1862346.
^ ^a ^b Wu S, Ibarra MC, Malicdan MC, Murayama K, Ichihara Y, Kikuchi H, Nonaka I, Noguchi S, Hayashi YK, Nishino I (June 2006). "Central core disease is due to RYR1 mutations in more than 90% of patients". Brain. 129 (Pt 6): 1470–80. doi:10.1093/brain/awl077. PMID 16621918.
^ ^a ^b "Entrez Gene: RYR1 ryanodine receptor 1 (skeletal)".
^ Filipova D, Walter AM, Gaspar JA, Brunn A, Linde NF, Ardestani MA, Deckert M, Hescheler J, Pfitzer G, Sachinidis A, Papadopoulos S (April 2016). "Corrigendum: Gene profiling of embryonic skeletal muscle lacking type I ryanodine receptor Ca(2+) release channel". Scientific Reports. 6: 24450. Bibcode:2016NatSR...624450F. doi:10.1038/srep24450. PMC 4840354. PMID 27102063.
^ Willemse H, Theodoratos A, Smith PN, Dulhunty AF (February 2016). "Unexpected dependence of RyR1 splice variant expression in human lower limb muscles on fiber-type composition". Pflügers Archiv. 468 (2): 269–78. doi:10.1007/s00424-015-1738-9. PMID 26438192. S2CID 5894066.
^ Hanson MG, Niswander LA (December 2014). "An explant muscle model to examine the refinement of the synaptic landscape". Journal of Neuroscience Methods. 238: 95–104. doi:10.1016/j.jneumeth.2014.09.013. PMC 4252626. PMID 25251554.
^ Böhm J, Leshinsky-Silver E, Vassilopoulos S, Le Gras S, Lerman-Sagie T, Ginzberg M, Jost B, Lev D, Laporte J (October 2012). "Samaritan myopathy, an ultimately benign congenital myopathy, is caused by a RYR1 mutation". Acta Neuropathologica. 124 (4): 575–81. doi:10.1007/s00401-012-1007-3. PMID 22752422. S2CID 9014320.
^ Fruen BR, Balog EM, Schafer J, Nitu FR, Thomas DD, Cornea RL (January 2005). "Direct detection of calmodulin tuning by ryanodine receptor channel targets using a Ca2+-sensitive acrylodan-labeled calmodulin". Biochemistry. 44 (1): 278–84. CiteSeerX 10.1.1.578.9139. doi:10.1021/bi048246u. PMID 15628869.
^ Cornea RL, Nitu F, Gruber S, Kohler K, Satzer M, Thomas DD, Fruen BR (April 2009). "FRET-based mapping of calmodulin bound to the RyR1 Ca2+ release channel". Proceedings of the National Academy of Sciences of the United States of America. 106 (15): 6128–33. Bibcode:2009PNAS..106.6128C. doi:10.1073/pnas.0813010106. PMC 2662960. PMID 19332786.
^ Avila G, Lee EH, Perez CF, Allen PD, Dirksen RT (June 2003). "FKBP12 binding to RyR1 modulates excitation-contraction coupling in mouse skeletal myotubes". The Journal of Biological Chemistry. 278 (25): 22600–8. doi:10.1074/jbc.M205866200. PMID 12704193.
^ Bultynck G, De Smet P, Rossi D, Callewaert G, Missiaen L, Sorrentino V, De Smedt H, Parys JB (March 2001). "Characterization and mapping of the 12 kDa FK506-binding protein (FKBP12)-binding site on different isoforms of the ryanodine receptor and of the inositol 1,4,5-trisphosphate receptor". The Biochemical Journal. 354 (Pt 2): 413–22. doi:10.1042/bj3540413. PMC 1221670. PMID 11171121.
^ Gaburjakova M, Gaburjakova J, Reiken S, Huang F, Marx SO, Rosemblit N, Marks AR (May 2001). "FKBP12 binding modulates ryanodine receptor channel gating". The Journal of Biological Chemistry. 276 (20): 16931–5. doi:10.1074/jbc.M100856200. PMID 11279144.
^ Hwang SY, Wei J, Westhoff JH, Duncan RS, Ozawa F, Volpe P, Inokuchi K, Koulen P (August 2003). "Differential functional interaction of two Vesl/Homer protein isoforms with ryanodine receptor type 1: a novel mechanism for control of intracellular calcium signaling". Cell Calcium. 34 (2): 177–84. doi:10.1016/S0143-4160(03)00082-4. PMID 12810060.
^ ^a ^b ^c Feng W, Tu J, Yang T, Vernon PS, Allen PD, Worley PF, Pessah IN (November 2002). "Homer regulates gain of ryanodine receptor type 1 channel complex". The Journal of Biological Chemistry. 277 (47): 44722–30. doi:10.1074/jbc.M207675200. PMID 12223488.
^ Lee JM, Rho SH, Shin DW, Cho C, Park WJ, Eom SH, Ma J, Kim DH (February 2004). "Negatively charged amino acids within the intraluminal loop of ryanodine receptor are involved in the interaction with triadin". The Journal of Biological Chemistry. 279 (8): 6994–7000. doi:10.1074/jbc.M312446200. PMID 14638677.
^ Caswell AH, Motoike HK, Fan H, Brandt NR (January 1999). "Location of ryanodine receptor binding site on skeletal muscle triadin". Biochemistry. 38 (1): 90–7. doi:10.1021/bi981306+. PMID 9890886.
^ Guo W, Campbell KP (April 1995). "Association of triadin with the ryanodine receptor and calsequestrin in the lumen of the sarcoplasmic reticulum". The Journal of Biological Chemistry. 270 (16): 9027–30. doi:10.1074/jbc.270.16.9027. PMID 7721813.
^ Groh S, Marty I, Ottolia M, Prestipino G, Chapel A, Villaz M, Ronjat M (April 1999). "Functional interaction of the cytoplasmic domain of triadin with the skeletal ryanodine receptor". The Journal of Biological Chemistry. 274 (18): 12278–83. doi:10.1074/jbc.274.18.12278. PMID 10212196.

Dopunska literatura uredi

Treves S, Anderson AA, Ducreux S, Divet A, Bleunven C, Grasso C, Paesante S, Zorzato F (October 2005). "Ryanodine receptor 1 mutations, dysregulation of calcium homeostasis and neuromuscular disorders". Neuromuscular Disorders. 15 (9–10): 577–87. doi:10.1016/j.nmd.2005.06.008. PMID 16084090. S2CID 31372661.

Vanjski linkovi uredi

RYR1 protein, human na US National Library of Medicine Medical Subject Headings (MeSH)
GeneReviews/NIH/UW entry on Multiminicore Disease
GeneReviews/NCBI/NIH/UW entry on Malignant Hyperthermia Susceptibility
RYR1 Variation Database Arhivirano 1. 3. 2012. na Wayback Machine

Ovaj članak uključuje tekst iz Nacionalne medicinske biblioteke Sjedinjenih Država, koji je u javnom vlasništvu.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000196218 - Ensembl, maj 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000030592 - 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.

[pmid1862346-5] Fujii J, Otsu K, Zorzato F, de Leon S, Khanna VK, Weiler JE, O'Brien PJ, MacLennan DH (July 1991). "Identification of a mutation in porcine ryanodine receptor associated with malignant hyperthermia". Science. 253 (5018): 448–51. Bibcode:1991Sci...253..448F. doi:10.1126/science.1862346. PMID 1862346.

[pmid16621918-6] Wu S, Ibarra MC, Malicdan MC, Murayama K, Ichihara Y, Kikuchi H, Nonaka I, Noguchi S, Hayashi YK, Nishino I (June 2006). "Central core disease is due to RYR1 mutations in more than 90% of patients". Brain. 129 (Pt 6): 1470–80. doi:10.1093/brain/awl077. PMID 16621918.

[entrez-7] "Entrez Gene: RYR1 ryanodine receptor 1 (skeletal)".

[8] Filipova D, Walter AM, Gaspar JA, Brunn A, Linde NF, Ardestani MA, Deckert M, Hescheler J, Pfitzer G, Sachinidis A, Papadopoulos S (April 2016). "Corrigendum: Gene profiling of embryonic skeletal muscle lacking type I ryanodine receptor Ca(2+) release channel". Scientific Reports. 6: 24450. Bibcode:2016NatSR...624450F. doi:10.1038/srep24450. PMC 4840354. PMID 27102063.

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