TGFBR1

TGFBR1
Dostupne strukture
PDB	Pretraga ortologa: PDBe RCSB
Spisak PDB ID kodova
	1B6C, 1IAS, 1PY5, 1RW8, 1VJY, 2L5S, 2PJY, 2WOT, 2WOU, 2X7O, 3FAA, 3GXL, 3HMM, 3KCF, 3KFD, 3TZM, 4X0M, 4X2J, 4X2K, 4X2N, 4X2G, 4X2F, 5E8W, 5E8X, 5E8U, 5E8T, 5E8S, 5E90, 5E8Z
Identifikatori
Aliasi	TGFBR1
Vanjski ID-jevi	OMIM: 190181 MGI: 98728 HomoloGene: 3177 GeneCards: TGFBR1
Lokacija gena (čovjek)
Hrom.	Hromosom 9 (čovjek)
Kraj	99,154,192 bp
Lokacija gena (miš)
Hrom.	Hromosom 4 (miš)
Kraj	47,414,931 bp
Ontologija gena
Molekularna funkcija	• type II transforming growth factor beta receptor binding; • I-SMAD binding; • transforming growth factor beta-activated receptor activity; • kinase activity; • signaling receptor binding; • ATP binding; • protein kinase activity; • vezivanje iona metala; • protein serine/threonine kinase activity; • transforming growth factor beta receptor activity, type I; • aktivnost sa transferazom; • growth factor binding; • transmembrane receptor protein serine/threonine kinase activity; • GO:0001948, GO:0016582 vezivanje za proteine; • SMAD binding; • nucleotide binding; • transforming growth factor beta binding; • activin binding;
Ćelijska komponenta	• endozom; • membrana; • bicellular tight junction; • cell surface; • Lipidni splav; • integral component of membrane; • receptor complex; • ćelijska membrana; • međućelijske veze; • intracellular anatomical structure; • intracellular membrane-bounded organelle; • integral component of plasma membrane; • activin receptor complex; • jedro;
Biološki proces	• skeletal system development; • response to cholesterol; • regulation of protein ubiquitination; • post-embryonic development; • protein phosphorylation; • negative regulation of chondrocyte differentiation; • mesenchymal cell differentiation; • Angiogeneza; • transforming growth factor beta receptor signaling pathway; • positive regulation of filopodium assembly; • extracellular structure organization; • pharyngeal system development; • GO:0097285 apoptoza; • cellular response to transforming growth factor beta stimulus; • pathway-restricted SMAD protein phosphorylation; • positive regulation of protein kinase B signaling; • GO:0009373 regulation of transcription, DNA-templated; • Nefrogeneza; • collagen fibril organization; • thymus development; • cell motility; • negative regulation of extrinsic apoptotic signaling pathway; • positive regulation of apoptotic signaling pathway; • in utero embryonic development; • negative regulation of transforming growth factor beta receptor signaling pathway; • GO:0060469, GO:0009371 positive regulation of transcription, DNA-templated; • heart development; • positive regulation of cell growth; • parathyroid gland development; • artery morphogenesis; • blastocyst development; • activin receptor signaling pathway; • roof of mouth development; • Ćelijska diferencijacija; • male gonad development; • Fosforilacija; • skeletal system morphogenesis; • Zarastanje rana; • negative regulation of apoptotic process; • epithelial to mesenchymal transition; • Regulacija ekspresije gena; • embryonic cranial skeleton morphogenesis; • peptidyl-threonine phosphorylation; • GO:0007243 intracellular signal transduction; • positive regulation of endothelial cell proliferation; • positive regulation of cell migration; • regulation of epithelial to mesenchymal transition; • positive regulation of pathway-restricted SMAD protein phosphorylation; • endothelial cell activation; • negative regulation of endothelial cell proliferation; • transmembrane receptor protein serine/threonine kinase signaling pathway; • lens development in camera-type eye; • GO:0035404 peptidyl-serine phosphorylation; • positive regulation of cell population proliferation; • regulation of growth; • neuron fate commitment; • regulation of protein binding; • endothelial cell migration; • germ cell migration; • positive regulation of SMAD protein signal transduction; • cardiac epithelial to mesenchymal transition; • GO:0072468 Transdukcija signala; • anterior/posterior pattern specification; • proepicardium development; • ventricular trabecula myocardium morphogenesis; • ventricular compact myocardium morphogenesis; • positive regulation of epithelial to mesenchymal transition; • protein deubiquitination; • positive regulation of stress fiber assembly; • regulation of cardiac muscle cell proliferation; • ventricular septum morphogenesis; • angiogenesis involved in coronary vascular morphogenesis; • coronary artery morphogenesis; • positive regulation of epithelial to mesenchymal transition involved in endocardial cushion formation; • positive regulation of tight junction disassembly; • epicardium morphogenesis; • positive regulation of apoptotic process; • GO:1901313 positive regulation of gene expression; • pattern specification process;
	Izvori:Amigo / QuickGO
Ortolozi
	7046
	21812
	ENSG00000106799
	ENSMUSG00000007613
	P36897
	Q64729
	NM_001130916; NM_001306210; NM_004612
	NM_009370; NM_001312868; NM_001312869
	NP_001124388; NP_001293139; NP_004603
	NP_001299797; NP_001299798; NP_033396
	Wikipodaci
Pogledaj/uredi – čovjek	Pogledaj/uredi – miš

Beta receptor I transformirajućeg faktora rasta (aktivinski receptor A tipa sličnog kunazi II, 53kDa) je membranski vezani TGF-beta receptorski protein porodice receptora TGF-beta za superporodicu signalnih liganda TGF-beta. TGFBR1 je njegov ljudski gen.

Aminokiselinska sekvenca

Dužina polipeptidnog lanca je 503 aminokiseline, а molekulska težina Da. 55 960^[5]

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
MEAAVAAPRP	RLLLLVLAAA	AAAAAALLPG	ATALQCFCHL	CTKDNFTCVT
DGLCFVSVTE	TTDKVIHNSM	CIAEIDLIPR	DRPFVCAPSS	KTGSVTTTYC
CNQDHCNKIE	LPTTVKSSPG	LGPVELAAVI	AGPVCFVCIS	LMLMVYICHN
RTVIHHRVPN	EEDPSLDRPF	ISEGTTLKDL	IYDMTTSGSG	SGLPLLVQRT
IARTIVLQES	IGKGRFGEVW	RGKWRGEEVA	VKIFSSREER	SWFREAEIYQ
TVMLRHENIL	GFIAADNKDN	GTWTQLWLVS	DYHEHGSLFD	YLNRYTVTVE
GMIKLALSTA	SGLAHLHMEI	VGTQGKPAIA	HRDLKSKNIL	VKKNGTCCIA
DLGLAVRHDS	ATDTIDIAPN	HRVGTKRYMA	PEVLDDSINM	KHFESFKRAD
IYAMGLVFWE	IARRCSIGGI	HEDYQLPYYD	LVPSDPSVEE	MRKVVCEQKL
RPNIPNRWQS	CEALRVMAKI	MRECWYANGA	ARLTALRIKK	TLSQLSQQEG
IKM

Funkcija

Protein kodiran ovim genom formira heteromerni kompleks sa tipom II TGF-β receptora kada je vezan za TGF-β, transducirajući signal TGF-β sa ćelijske površine na citoplazmu. Kodirani protein je serin/treonin protein kinaza. Mutacije u ovom genu povezane su s sindromom Loeys – Dietzove aortne aneurizme (LDS, LDAS).^[6]

Interakcije

Pokazalo se da TGF beta receptor 1 stupa u interakciju skako slijedi:

Inhibitori

Studije na životinjama

Defekti se primjećuju kada je gen TGFBR-1 ili nokautiran ili kada je konstitutivno aktivan mutant TGFBR-1 (koji je aktivan u prisustvu ili odsustvu liganda)

U mišjim nokaut TGFBR-1 modelima, ženke bile su sterilne. Razvili su oviduktne divertikule i neispravan glatki mišić maternice, što znači da su slojevi glatkih mišića maternice bili slabo formirani. Oviduktni divertikule su male, ispupčene vrećice smještene na jajovodu, koji je cijev koja prenosi jajnu ćeliju iz jajnika u maternicu. Ova deformacija jajovoda nastala je obostrano i rezultirala je smanjenim razvojem embriona i njegovim otežanim prolaskom u maternicu. Ovulacija i oplodnja su se još dogoađale u nokautima, ali ostaci embriona pronađeni su u ovim oviduktnim divertikulama.^[25]

Kod mišjih TGFBR-1 nock-in modela u kojima je konstitutivno aktivni gen TGFBR-1 uvjetno induciran, prekomjerna aktivacija receptora TGFBR-1 dovodi do neplodnosti, smanjenja broja žlijezda materice i hipermišićavih maternica (povećanje količina glatkih mišića u maternici).^[26]

Ovi eksperimenti pokazuju da receptor TGFB-1 ima kritičnu ulogu u funkciji ženskog reproduktivnog trakta. Oni također pokazuju da genetičke mutacije u genu TGFBR-1 mogu dovesti do problema s plodnošću kod žena.

Reference

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000106799 - Ensembl, maj 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000007613 - 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.
^ "UniProt, P36897". Pristupljeno 12. 9. 2021.
^ "Entrez Gene: TGFBR1 transforming growth factor, beta receptor I (activin A receptor type II-like kinase, 53kDa)".
^ ^a ^b Razani B, Zhang XL, Bitzer M, von Gersdorff G, Böttinger EP, Lisanti MP (mart 2001). "Caveolin-1 regulates transforming growth factor (TGF)-beta/SMAD signaling through an interaction with the TGF-beta type I receptor". The Journal of Biological Chemistry. 276 (9): 6727–38. doi:10.1074/jbc.M008340200. PMID 11102446.
^ Guerrero-Esteo M, Sanchez-Elsner T, Letamendia A, Bernabeu C (august 2002). "Extracellular and cytoplasmic domains of endoglin interact with the transforming growth factor-beta receptors I and II". The Journal of Biological Chemistry. 277 (32): 29197–209. doi:10.1074/jbc.M111991200. PMID 12015308.
^ Barbara NP, Wrana JL, Letarte M (januar 1999). "Endoglin is an accessory protein that interacts with the signaling receptor complex of multiple members of the transforming growth factor-beta superfamily". The Journal of Biological Chemistry. 274 (2): 584–94. doi:10.1074/jbc.274.2.584. PMID 9872992.
^ Wang T, Donahoe PK, Zervos AS (juli 1994). "Specific interaction of type I receptors of the TGF-beta family with the immunophilin FKBP-12". Science. 265 (5172): 674–6. doi:10.1126/science.7518616. PMID 7518616.
^ Liu F, Ventura F, Doody J, Massagué J (juli 1995). "Human type II receptor for bone morphogenic proteins (BMPs): extension of the two-kinase receptor model to the BMPs". Molecular and Cellular Biology. 15 (7): 3479–86. doi:10.1128/mcb.15.7.3479. PMC 230584. PMID 7791754.
^ Kawabata M, Imamura T, Miyazono K, Engel ME, Moses HL (decembar 1995). "Interaction of the transforming growth factor-beta type I receptor with farnesyl-protein transferase-alpha". The Journal of Biological Chemistry. 270 (50): 29628–31. doi:10.1074/jbc.270.50.29628. PMID 8530343.
^ Wrighton KH, Lin X, Feng XH (juli 2008). "Critical regulation of TGFbeta signaling by Hsp90". Proceedings of the National Academy of Sciences of the United States of America. 105 (27): 9244–9. doi:10.1073/pnas.0800163105. PMC 2453700. PMID 18591668.
^ Mochizuki T, Miyazaki H, Hara T, Furuya T, Imamura T, Watabe T, Miyazono K (juli 2004). "Roles for the MH2 domain of Smad7 in the specific inhibition of transforming growth factor-beta superfamily signaling". The Journal of Biological Chemistry. 279 (30): 31568–74. doi:10.1074/jbc.M313977200. PMID 15148321.
^ Asano Y, Ihn H, Yamane K, Kubo M, Tamaki K (januar 2004). "Impaired Smad7-Smurf-mediated negative regulation of TGF-beta signaling in scleroderma fibroblasts". The Journal of Clinical Investigation. 113 (2): 253–64. doi:10.1172/JCI16269. PMC 310747. PMID 14722617.
^ Koinuma D, Shinozaki M, Komuro A, Goto K, Saitoh M, Hanyu A, Ebina M, Nukiwa T, Miyazawa K, Imamura T, Miyazono K (decembar 2003). "Arkadia amplifies TGF-beta superfamily signalling through degradation of Smad7". The EMBO Journal. 22 (24): 6458–70. doi:10.1093/emboj/cdg632. PMC 291827. PMID 14657019.
^ Kavsak P, Rasmussen RK, Causing CG, Bonni S, Zhu H, Thomsen GH, Wrana JL (decembar 2000). "Smad7 binds to Smurf2 to form an E3 ubiquitin ligase that targets the TGF beta receptor for degradation". Molecular Cell. 6 (6): 1365–75. doi:10.1016/s1097-2765(00)00134-9. PMID 11163210.
^ Hayashi H, Abdollah S, Qiu Y, Cai J, Xu YY, Grinnell BW, Richardson MA, Topper JN, Gimbrone MA, Wrana JL, Falb D (juni 1997). "The MAD-related protein Smad7 associates with the TGFbeta receptor and functions as an antagonist of TGFbeta signaling". Cell. 89 (7): 1165–73. doi:10.1016/s0092-8674(00)80303-7. PMID 9215638. S2CID 16552782.
^ ^a ^b Datta PK, Moses HL (maj 2000). "STRAP and Smad7 synergize in the inhibition of transforming growth factor beta signaling". Molecular and Cellular Biology. 20 (9): 3157–67. doi:10.1128/mcb.20.9.3157-3167.2000. PMC 85610. PMID 10757800.
^ Griswold-Prenner I, Kamibayashi C, Maruoka EM, Mumby MC, Derynck R (novembar 1998). "Physical and functional interactions between type I transforming growth factor beta receptors and Balpha, a WD-40 repeat subunit of phosphatase 2A". Molecular and Cellular Biology. 18 (11): 6595–604. doi:10.1128/mcb.18.11.6595. PMC 109244. PMID 9774674.
^ Datta PK, Chytil A, Gorska AE, Moses HL (decembar 1998). "Identification of STRAP, a novel WD domain protein in transforming growth factor-beta signaling". The Journal of Biological Chemistry. 273 (52): 34671–4. doi:10.1074/jbc.273.52.34671. PMID 9856985.
^ Ebner R, Chen RH, Lawler S, Zioncheck T, Derynck R (novembar 1993). "Determination of type I receptor specificity by the type II receptors for TGF-beta or activin". Science. 262 (5135): 900–2. doi:10.1126/science.8235612. PMID 8235612.
^ Oh SP, Seki T, Goss KA, Imamura T, Yi Y, Donahoe PK, Li L, Miyazono K, ten Dijke P, Kim S, Li E (mart 2000). "Activin receptor-like kinase 1 modulates transforming growth factor-beta 1 signaling in the regulation of angiogenesis". Proceedings of the National Academy of Sciences of the United States of America. 97 (6): 2626–31. doi:10.1073/pnas.97.6.2626. PMC 15979. PMID 10716993.
^ Kawabata M, Chytil A, Moses HL (mart 1995). "Cloning of a novel type II serine/threonine kinase receptor through interaction with the type I transforming growth factor-beta receptor". The Journal of Biological Chemistry. 270 (10): 5625–30. doi:10.1074/jbc.270.10.5625. PMID 7890683.
^ Li Q, Agno JE, Edson MA, Nagaraja AK, Nagashima T, Matzuk MM (oktobar 2011). "Transforming growth factor β receptor type 1 is essential for female reproductive tract integrity and function". PLOS Genetics. 7 (10): e1002320. doi:10.1371/journal.pgen.1002320. PMC 3197682. PMID 22028666.
^ Gao Y, Duran S, Lydon JP, DeMayo FJ, Burghardt RC, Bayless KJ, Bartholin L, Li Q (februar 2015). "Constitutive activation of transforming growth factor Beta receptor 1 in the mouse uterus impairs uterine morphology and function". Biology of Reproduction. 92 (2): 34. doi:10.1095/biolreprod.114.125146. PMC 4435420. PMID 25505200.

Dopunska literatura

Massagué J (juni 1992). "Receptors for the TGF-beta family". Cell. 69 (7): 1067–70. doi:10.1016/0092-8674(92)90627-O. PMID 1319842. S2CID 54268875.
Wrana JL (1998). "TGF-beta receptors and signalling mechanisms". Mineral and Electrolyte Metabolism. 24 (2–3): 120–30. doi:10.1159/000057359. PMID 9525694. S2CID 84458561.
Josso N, di Clemente N, Gouédard L (juni 2001). "Anti-Müllerian hormone and its receptors". Molecular and Cellular Endocrinology. 179 (1–2): 25–32. doi:10.1016/S0303-7207(01)00467-1. PMID 11420127. S2CID 27316217.

Vanjski linkovi

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000106799 - Ensembl, maj 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000007613 - 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.

[UniProt-5] "UniProt, P36897". Pristupljeno 12. 9. 2021.

[6] "Entrez Gene: TGFBR1 transforming growth factor, beta receptor I (activin A receptor type II-like kinase, 53kDa)".

[pmid11102446-7] Razani B, Zhang XL, Bitzer M, von Gersdorff G, Böttinger EP, Lisanti MP (mart 2001). "Caveolin-1 regulates transforming growth factor (TGF)-beta/SMAD signaling through an interaction with the TGF-beta type I receptor". The Journal of Biological Chemistry. 276 (9): 6727–38. doi:10.1074/jbc.M008340200. PMID 11102446.

[pmid12015308-8] Guerrero-Esteo M, Sanchez-Elsner T, Letamendia A, Bernabeu C (august 2002). "Extracellular and cytoplasmic domains of endoglin interact with the transforming growth factor-beta receptors I and II". The Journal of Biological Chemistry. 277 (32): 29197–209. doi:10.1074/jbc.M111991200. PMID 12015308.

[pmid9872992-9] Barbara NP, Wrana JL, Letarte M (januar 1999). "Endoglin is an accessory protein that interacts with the signaling receptor complex of multiple members of the transforming growth factor-beta superfamily". The Journal of Biological Chemistry. 274 (2): 584–94. doi:10.1074/jbc.274.2.584. PMID 9872992.

[pmid7518616-10] Wang T, Donahoe PK, Zervos AS (juli 1994). "Specific interaction of type I receptors of the TGF-beta family with the immunophilin FKBP-12". Science. 265 (5172): 674–6. doi:10.1126/science.7518616. PMID 7518616.

[pmid7791754-11] Liu F, Ventura F, Doody J, Massagué J (juli 1995). "Human type II receptor for bone morphogenic proteins (BMPs): extension of the two-kinase receptor model to the BMPs". Molecular and Cellular Biology. 15 (7): 3479–86. doi:10.1128/mcb.15.7.3479. PMC 230584. PMID 7791754.

[pmid8530343-12] Kawabata M, Imamura T, Miyazono K, Engel ME, Moses HL (decembar 1995). "Interaction of the transforming growth factor-beta type I receptor with farnesyl-protein transferase-alpha". The Journal of Biological Chemistry. 270 (50): 29628–31. doi:10.1074/jbc.270.50.29628. PMID 8530343.

[pmid18591668-13] Wrighton KH, Lin X, Feng XH (juli 2008). "Critical regulation of TGFbeta signaling by Hsp90". Proceedings of the National Academy of Sciences of the United States of America. 105 (27): 9244–9. doi:10.1073/pnas.0800163105. PMC 2453700. PMID 18591668.

[pmid15148321-14] Mochizuki T, Miyazaki H, Hara T, Furuya T, Imamura T, Watabe T, Miyazono K (juli 2004). "Roles for the MH2 domain of Smad7 in the specific inhibition of transforming growth factor-beta superfamily signaling". The Journal of Biological Chemistry. 279 (30): 31568–74. doi:10.1074/jbc.M313977200. PMID 15148321.

[pmid14722617-15] Asano Y, Ihn H, Yamane K, Kubo M, Tamaki K (januar 2004). "Impaired Smad7-Smurf-mediated negative regulation of TGF-beta signaling in scleroderma fibroblasts". The Journal of Clinical Investigation. 113 (2): 253–64. doi:10.1172/JCI16269. PMC 310747. PMID 14722617.

[pmid14657019-16] Koinuma D, Shinozaki M, Komuro A, Goto K, Saitoh M, Hanyu A, Ebina M, Nukiwa T, Miyazawa K, Imamura T, Miyazono K (decembar 2003). "Arkadia amplifies TGF-beta superfamily signalling through degradation of Smad7". The EMBO Journal. 22 (24): 6458–70. doi:10.1093/emboj/cdg632. PMC 291827. PMID 14657019.

[pmid11163210-17] Kavsak P, Rasmussen RK, Causing CG, Bonni S, Zhu H, Thomsen GH, Wrana JL (decembar 2000). "Smad7 binds to Smurf2 to form an E3 ubiquitin ligase that targets the TGF beta receptor for degradation". Molecular Cell. 6 (6): 1365–75. doi:10.1016/s1097-2765(00)00134-9. PMID 11163210.

[pmid9215638-18] Hayashi H, Abdollah S, Qiu Y, Cai J, Xu YY, Grinnell BW, Richardson MA, Topper JN, Gimbrone MA, Wrana JL, Falb D (juni 1997). "The MAD-related protein Smad7 associates with the TGFbeta receptor and functions as an antagonist of TGFbeta signaling". Cell. 89 (7): 1165–73. doi:10.1016/s0092-8674(00)80303-7. PMID 9215638. S2CID 16552782.

[pmid10757800-19] Datta PK, Moses HL (maj 2000). "STRAP and Smad7 synergize in the inhibition of transforming growth factor beta signaling". Molecular and Cellular Biology. 20 (9): 3157–67. doi:10.1128/mcb.20.9.3157-3167.2000. PMC 85610. PMID 10757800.

[pmid9774674-20] Griswold-Prenner I, Kamibayashi C, Maruoka EM, Mumby MC, Derynck R (novembar 1998). "Physical and functional interactions between type I transforming growth factor beta receptors and Balpha, a WD-40 repeat subunit of phosphatase 2A". Molecular and Cellular Biology. 18 (11): 6595–604. doi:10.1128/mcb.18.11.6595. PMC 109244. PMID 9774674.

[pmid9856985-21] Datta PK, Chytil A, Gorska AE, Moses HL (decembar 1998). "Identification of STRAP, a novel WD domain protein in transforming growth factor-beta signaling". The Journal of Biological Chemistry. 273 (52): 34671–4. doi:10.1074/jbc.273.52.34671. PMID 9856985.

[pmid8235612-22] Ebner R, Chen RH, Lawler S, Zioncheck T, Derynck R (novembar 1993). "Determination of type I receptor specificity by the type II receptors for TGF-beta or activin". Science. 262 (5135): 900–2. doi:10.1126/science.8235612. PMID 8235612.

[pmid10716993-23] Oh SP, Seki T, Goss KA, Imamura T, Yi Y, Donahoe PK, Li L, Miyazono K, ten Dijke P, Kim S, Li E (mart 2000). "Activin receptor-like kinase 1 modulates transforming growth factor-beta 1 signaling in the regulation of angiogenesis". Proceedings of the National Academy of Sciences of the United States of America. 97 (6): 2626–31. doi:10.1073/pnas.97.6.2626. PMC 15979. PMID 10716993.

[pmid7890683-24] Kawabata M, Chytil A, Moses HL (mart 1995). "Cloning of a novel type II serine/threonine kinase receptor through interaction with the type I transforming growth factor-beta receptor". The Journal of Biological Chemistry. 270 (10): 5625–30. doi:10.1074/jbc.270.10.5625. PMID 7890683.

[25] Li Q, Agno JE, Edson MA, Nagaraja AK, Nagashima T, Matzuk MM (oktobar 2011). "Transforming growth factor β receptor type 1 is essential for female reproductive tract integrity and function". PLOS Genetics. 7 (10): e1002320. doi:10.1371/journal.pgen.1002320. PMC 3197682. PMID 22028666.

[26] Gao Y, Duran S, Lydon JP, DeMayo FJ, Burghardt RC, Bayless KJ, Bartholin L, Li Q (februar 2015). "Constitutive activation of transforming growth factor Beta receptor 1 in the mouse uterus impairs uterine morphology and function". Biology of Reproduction. 92 (2): 34. doi:10.1095/biolreprod.114.125146. PMC 4435420. PMID 25505200.

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