Pengguna:Hidayatsrf/Bak pasir: Perbedaan antara revisi
Konten dihapus Konten ditambahkan
Hidayatsrf (bicara | kontrib) Tidak ada ringkasan suntingan |
Hidayatsrf (bicara | kontrib) Tidak ada ringkasan suntingan |
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{{Infobox_gene}}
'''Titin''' {{IPAc-en|ˈ|t|aɪ|t|ɪ|n}}, juga dikenal sebagai '''connectin''', adalah suatu [[protein]] yang pada [[manusia]], dikodekan oleh [[gen]] ''TTN''.<ref name= "Entrez_ 7273">{{cite web | title = Entrez Gene: TTN titin| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7273| accessdate = }}</ref><ref name="pmid2129545">{{cite journal | vauthors = Labeit S, Barlow DP, Gautel M, Gibson T, Holt J, Hsieh CL, Francke U, Leonard K, Wardale J, Whiting A | title = A regular pattern of two types of 100-residue motif in the sequence of titin | journal = Nature | volume = 345 | issue = 6272 | pages = 273–6 | date = May 1990 | pmid = 2129545 | doi = 10.1038/345273a0 }}</ref> Titin adalah sebuah protein raksasa, panjangnya lebih dari 1 [[Mikrometer|µm]],<ref>{{cite web | url=http://www.ks.uiuc.edu/Research/z1z2/ | title=The Chain-like Elasticity of Titin | publisher=Theoretical and Computational Biophysics Group, University of Illinois | accessdate=25 September 2014 | author=Eric H. Lee}}</ref> fungsinya yaitu sebagai mata air molekuler yang bertanggung jawab atas elastisitas pasif [[otot]]. Protein ini terdiri dari 244 domain [[protein]] terlipat secara individual yang dihubungkan dengan urutan [[peptida]] yang tidak terstruktur.<ref name="pmid7569978">{{cite journal | vauthors = Labeit S, Kolmerer B | title = Titins: giant proteins in charge of muscle ultrastructure and elasticity | journal = Science | volume = 270 | issue = 5234 | pages = 293–6 | date = October 1995 | pmid = 7569978 | doi = 10.1126/science.270.5234.293 }}</ref> Domain ini [[denaturasi (biokimia)|terbuka]] saat protein diregangkan dan [[lipatan protein|terlipat kembali]] saat ketegangan dihilangkan.<ref name="pmid11222304">{{cite journal | vauthors = Minajeva A, Kulke M, Fernandez JM, Linke WA | author-link2 = Matthew Kulke | title = Unfolding of titin domains explains the viscoelastic behavior of skeletal myofibrils | journal = Biophysical Journal | volume = 80 | issue = 3 | pages = 1442–51 | date = March 2001 | pmid = 11222304 | pmc = 1301335 | doi = 10.1016/S0006-3495(01)76116-4 }}</ref>
Titin berperan penting dalam kontraksi [[jaringan otot lurik]]. Protein ini menghubungkan [[Myofibril#Penampakan|garis Z]] ke [[Myofibril#Penampakan|garis M]] di dalam [[sarkomer]]. Protein ini berperan memaksa transmisi pada garis Z dan ketegangan istirahat di area [[Myofibril#Penampakan|Pita I]].<ref name="pmid11846417">{{cite journal | vauthors = Itoh-Satoh M, Hayashi T, Nishi H, Koga Y, Arimura T, Koyanagi T, Takahashi M, Hohda S, Ueda K, Nouchi T, Hiroe M, Marumo F, Imaizumi T, Yasunami M, Kimura A | title = Titin mutations as the molecular basis for dilated cardiomyopathy | journal = Biochemical and Biophysical Research Communications | volume = 291 | issue = 2 | pages = 385–93 | date = February 2002 | pmid = 11846417 | doi = 10.1006/bbrc.2002.6448 }}</ref> Protein ini membatasi jangkauan gerak sarkomer ketika dalam kondisi tegang, sehingga berkontribusi terhadap kekakuan pasif otot. Variasi dalam urutan titin antara berbagai jenis otot (mis., Jantung atau kerangka) telah berkorelasi dengan perbedaan sifat mekanik otot-otot ini.<ref name= "Entrez_ 7273"/><ref>{{OMIM|188840}}</ref>
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{| class="wikitable"
|-
! Isoform !! alias/
|-
| Q8WZ42-1 || The "canonical" sequence || 34,350 || 3,816,030
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| Q8WZ42-13 || || 34,484 || 3,831,069
|}
== Struktur ==
Titin adalah protein terbesar yang diketahui; varian manusianya terdiri dari 34.350 [[asam amino]], dengan berat molekul isoform "kanonik" dewasa dari protein sekitar 3.816.188,13 [[unit massa atom|Da]].<ref name="urlExPASy_human"/> Homolog protein ini pada tikus bahkan lebih besar lagi, terdiri dari 35.213 asam amino dengan MW 3.906.487,6 [[unit massa atom|Da]].<ref name="urlExPASy_mouse">{{cite web|url= http://www.expasy.org/cgi-bin/protparam1?A2ASS6@noft@ |title= ProtParam for mouse titin |work= ExPASy Proteomics Server |publisher= Swiss Institute of Bioinformatics |accessdate=2010-05-06}}</ref> Protein ini memiliki [[titik isoelektrik]] teoritis 6,01.<ref name="urlExPASy_human"/> [[Rumus kimia]] empiris proteinnya adalah C<sub>169,719</sub>H<sub>270,464</sub>N<sub>45,688</sub>O<sub>52,237</sub>S<sub>911</sub>.<ref name="urlExPASy_human">{{cite web|url= http://web.expasy.org/cgi-bin/protparam/protparam1?Q8WZ42@1-34350@ |title= ProtParam for human titin |work= ExPASy Proteomics Server |publisher= Swiss Institute of Bioinformatics |accessdate=2011-07-25}}</ref> Ini memiliki teori [[indeks ketidakstabilan]] (II) 42,41, dan karena itu diklasifikasikan sebagai protein tidak stabil.<ref name="urlExPASy_human"/> [[Paruh waktu]] protein [[in vivo]], waktu yang dibutuhkan setengah dari jumlah protein dalam sel untuk dipecah setelah sintesisnya di dalam sel, diperkirakan sekitar 30 jam (pada [[reticulocyte]] [[mamalia]]).<ref name="url_UniProt_Q8WZ42)">{{cite web|url= http://www.uniprot.org/uniprot/Q8WZ42 |title= Titin - Homo sapiens (Human) | work = Universal Protein Resource | publisher = UniProt Consortium | date=2010-10-05 |accessdate=2010-10-15}}</ref>
Protein titin terletak di antara filamen tebal [[myosin]] dan cakram Z.<ref name="Wang_1991">{{cite journal | vauthors = Wang K, McCarter R, Wright J, Beverly J, Ramirez-Mitchell R | title = Regulation of skeletal muscle stiffness and elasticity by titin isoforms: a test of the segmental extension model of resting tension | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 88 | issue = 16 | pages = 7101–5 | date = August 1991 | pmid = 1714586 | pmc = 52241 | doi = 10.1073/pnas.88.16.7101 }}</ref> Titin terdiri dari rangkaian linear dua jenis modul (juga disebut sebagai [[domain protein]]; 244 total salinan): tipe I ([[domain fibronektin tipe III]]; 132 salinan) dan tipe II ([[domain imunoglobulin]]; 112 salinan).<ref name="pmid7569978"/> This linear array is further organized into two regions:
* [[N-terminus|N-terminal]] I-band: acts as the elastic part of the molecule and is composed mainly of type II modules. More specifically the I-band contains two regions of tandem type II immunoglobulin domains on either side of a PEVK region that is rich in proline, glutamate, valine and lysine.<ref name="Wang_1991"/> PVK elasticity has both entropic and enthalpic origins characterizable by a polymer persistence length and a stretch modulus.<ref>{{cite journal | vauthors = Linke WA, Ivemeyer M, Mundel P, Stockmeier MR, Kolmerer B | title = Nature of PEVK-titin elasticity in skeletal muscle | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 95 | issue = 14 | pages = 8052–7 | date = July 1998 | pmid = 9653138 | doi=10.1073/pnas.95.14.8052 | pmc=20927}}</ref> At low to moderate extensions PEVK elasticity can be modeled with a standard wormlike chain (WLC) model of entropic elasticity. At high extensions PEVK stretching can be modeled with a modified WLC model that incorporates enthalpic elasticity. The difference between low-and high- stretch elasticity is due to electrostatic stiffening and hydrophobic effects.
* [[C-terminus|C-terminal]] A-band: is thought to act as a protein-ruler and possesses [[kinase]] activity. The A-band is composed of alternating type I and II modules with super-repeat segments. These have been shown to align to the 43 nm axial repeats of myosin thick filaments with immunoglobulin domains correlating to myosin crowns.<ref name="pmid8683592">{{cite journal | vauthors = Bennett PM, Gautel M | title = Titin domain patterns correlate with the axial disposition of myosin at the end of the thick filament | journal = Journal of Molecular Biology | volume = 259 | issue = 5 | pages = 896–903 | date = June 1996 | pmid = 8683592 | doi = 10.1006/jmbi.1996.0367 }}</ref>
== Function ==
[[File:Sarcomere.svg|thumb|370px|Sliding filament model of muscle contraction. (Titin labeled at upper right.)]]
Titin is a large abundant protein of striated muscle. Titin's primary functions are to stabilize the thick filament, center it between the thin filaments, prevent overstretching of the sarcomere, and to recoil the sarcomere like a spring after it is stretched.<ref>{{cite book | last1 = Saladin | first1 = Kenneth | name-list-format = vanc | title = Anatomy & Physiology | date = 2015 | publisher = McGraw Hill | page = 401 | edition = 7 | accessdate=14 November 2016 }}</ref> An N-terminal Z-disc region and a C-terminal M-line region bind to the Z-line and M-line of the [[sarcomere]], respectively, so that a single titin molecule spans half the length of a sarcomere. Titin also contains binding sites for muscle-associated proteins so it serves as an adhesion template for the assembly of contractile machinery in muscle cells. It has also been identified as a structural protein for [[chromosome]]s.<ref name="Machado_1998"/><ref name = "Machado_2000">{{cite journal | vauthors = Machado C, Andrew DJ | title = Titin as a chromosomal protein | journal = Advances in Experimental Medicine and Biology | volume = 481 | issue = | pages = 221–32; discussion 232–6 | year = 2000 | pmid = 10987075 | doi = 10.1007/978-1-4615-4267-4_13 }}</ref> Considerable variability exists in the I-band, the M-line and the Z-disc regions of titin. Variability in the I-band region contributes to the differences in elasticity of different titin isoforms and, therefore, to the differences in elasticity of different muscle types. Of the many titin variants identified, five are described with complete transcript information available.<ref name= "Entrez_ 7273"/><ref name="pmid2129545" />
Titin interacts with many [[sarcomere|sarcomeric]] proteins including:<ref name="pmid11717165"/>
* Z line region: [[TCAP (gene)|telethonin]] and [[ACTN1|alpha-actinin]]
* I band region: [[CAPN3|calpain-3]] and [[OBSCN|obscurin]]
* M line region: [[MYBPC3|myosin-binding protein C]], [[calmodulin 1]], [[CAPN3]], and [[TRIM63|MURF1]]
== Clinical relevance ==
[[Mutation]]s anywhere within the unusually long sequence of this gene can cause [[premature stop codon]]s or other defects. Titin mutations are associated with hereditary myopathy with early respiratory failure, early-onset myopathy with fatal cardiomyopathy, core myopathy with heart disease, centronuclear myopathy, Limb-girdle muscular dystrophy type 2J, [[family|familial]] [[dilated cardiomyopathy]] 9,<ref name="pmid11846417"/><ref name="pmid10051295">{{cite journal | vauthors = Siu BL, Niimura H, Osborne JA, Fatkin D, MacRae C, Solomon S, Benson DW, Seidman JG, Seidman CE | title = Familial dilated cardiomyopathy locus maps to chromosome 2q31 | journal = Circulation | volume = 99 | issue = 8 | pages = 1022–6 | date = March 1999 | pmid = 10051295 | doi = 10.1161/01.cir.99.8.1022 | url = http://circ.ahajournals.org/cgi/content/abstract/99/8/1022 }}</ref> hypertrophic cardiomyopathy and [[distal muscular dystrophy|tibial muscular dystrophy]].<ref name="pmid12145747">{{cite journal | vauthors = Hackman P, Vihola A, Haravuori H, Marchand S, Sarparanta J, De Seze J, Labeit S, Witt C, Peltonen L, Richard I, Udd B | title = Tibial muscular dystrophy is a titinopathy caused by mutations in TTN, the gene encoding the giant skeletal-muscle protein titin | journal = American Journal of Human Genetics | volume = 71 | issue = 3 | pages = 492–500 | date = September 2002 | pmid = 12145747 | pmc = 379188 | doi = 10.1086/342380 }}</ref> Further research also suggests that no genetically linked form of any [[wikt:Special:Search/dystrophy|dystrophy]] or [[myopathy]] can be safely excluded from being caused by a mutation on the TTN gene.<ref name="pmid15728284">{{cite journal | vauthors = Udd B, Vihola A, Sarparanta J, Richard I, Hackman P | title = Titinopathies and extension of the M-line mutation phenotype beyond distal myopathy and LGMD2J | journal = Neurology | volume = 64 | issue = 4 | pages = 636–42 | date = February 2005 | pmid = 15728284 | doi = 10.1212/01.WNL.0000151853.50144.82 }}</ref> Truncating mutations in dilated cardiomyopathy patients are most commonly found in the A region; although truncations in the upstream I region might be expected to prevent translation of the A region entirely, [[alternative splicing]] creates some transcripts that do not encounter the premature stop codon, ameliorating its effect.<ref name="pmid26315439">{{cite journal | vauthors = Hinson JT, Chopra A, Nafissi N, Polacheck WJ, Benson CC, Swist S, Gorham J, Yang L, Schafer S, Sheng CC, Haghighi A, Homsy J, Hubner N, Church G, Cook SA, Linke WA, Chen CS, Seidman JG, Seidman CE | title = HEART DISEASE. Titin mutations in iPS cells define sarcomere insufficiency as a cause of dilated cardiomyopathy | journal = Science | volume = 349 | issue = 6251 | pages = 982–6 | date = August 2015 | pmid = 26315439 | doi = 10.1126/science.aaa5458 | pmc=4618316}}</ref>
Autoantibodies to titin are produced in patients with the autoimmune disease [[scleroderma]].<ref name="Machado_1998">{{cite journal | vauthors = Machado C, Sunkel CE, Andrew DJ | title = Human autoantibodies reveal titin as a chromosomal protein | journal = The Journal of Cell Biology | volume = 141 | issue = 2 | pages = 321–33 | date = April 1998 | pmid = 9548712 | pmc = 2148454 | doi = 10.1083/jcb.141.2.321 }}</ref>
== Interactions ==
Titin has been shown to [[Protein-protein interaction|interact]] with:
{{div col|colwidth=20em}}
* [[ANK1]],<ref name="pmid12444090">{{cite journal | vauthors = Kontrogianni-Konstantopoulos A, Bloch RJ | title = The hydrophilic domain of small ankyrin-1 interacts with the two N-terminal immunoglobulin domains of titin | journal = The Journal of Biological Chemistry | volume = 278 | issue = 6 | pages = 3985–91 | date = February 2003 | pmid = 12444090 | doi = 10.1074/jbc.M209012200 }}</ref>
* [[ANKRD1]],<ref name="pmid14583192">{{cite journal | vauthors = Miller MK, Bang ML, Witt CC, Labeit D, Trombitas C, Watanabe K, Granzier H, McElhinny AS, Gregorio CC, Labeit S | title = The muscle ankyrin repeat proteins: CARP, ankrd2/Arpp and DARP as a family of titin filament-based stress response molecules | journal = Journal of Molecular Biology | volume = 333 | issue = 5 | pages = 951–64 | date = November 2003 | pmid = 14583192 | doi = 10.1016/j.jmb.2003.09.012 }}</ref>
* [[ANKRD23]]<ref name=pmid14583192/>
* [[CAPN3]],<ref name="pmid9642272">{{cite journal | vauthors = Ono Y, Shimada H, Sorimachi H, Richard I, Saido TC, Beckmann JS, Ishiura S, Suzuki K | title = Functional defects of a muscle-specific calpain, p94, caused by mutations associated with limb-girdle muscular dystrophy type 2A | journal = The Journal of Biological Chemistry | volume = 273 | issue = 27 | pages = 17073–8 | date = July 1998 | pmid = 9642272 | doi = 10.1074/jbc.273.27.17073 }}</ref><ref name="pmid8537379">{{cite journal | vauthors = Sorimachi H, Kinbara K, Kimura S, Takahashi M, Ishiura S, Sasagawa N, Sorimachi N, Shimada H, Tagawa K, Maruyama K | title = Muscle-specific calpain, p94, responsible for limb girdle muscular dystrophy type 2A, associates with connectin through IS2, a p94-specific sequence | journal = The Journal of Biological Chemistry | volume = 270 | issue = 52 | pages = 31158–62 | date = December 1995 | pmid = 8537379 | doi = 10.1074/jbc.270.52.31158 }}</ref>
* [[FHL2]],<ref name="pmid12432079">{{cite journal | vauthors = Lange S, Auerbach D, McLoughlin P, Perriard E, Schäfer BW, Perriard JC, Ehler E | title = Subcellular targeting of metabolic enzymes to titin in heart muscle may be mediated by DRAL/FHL-2 | journal = Journal of Cell Science | volume = 115 | issue = Pt 24 | pages = 4925–36 | date = December 2002 | pmid = 12432079 | doi = 10.1242/jcs.00181 }}</ref>
* [[OBSCN]],<ref name="pmid11448995">{{cite journal | vauthors = Young P, Ehler E, Gautel M | title = Obscurin, a giant sarcomeric Rho guanine nucleotide exchange factor protein involved in sarcomere assembly | journal = The Journal of Cell Biology | volume = 154 | issue = 1 | pages = 123–36 | date = July 2001 | pmid = 11448995 | pmc = 2196875 | doi = 10.1083/jcb.200102110 }}</ref>
* [[Telethonin|TCAP]],<ref name="pmid9817758">{{cite journal | vauthors = Gregorio CC, Trombitás K, Centner T, Kolmerer B, Stier G, Kunke K, Suzuki K, Obermayr F, Herrmann B, Granzier H, Sorimachi H, Labeit S | title = The NH2 terminus of titin spans the Z-disc: its interaction with a novel 19-kD ligand (T-cap) is required for sarcomeric integrity | journal = The Journal of Cell Biology | volume = 143 | issue = 4 | pages = 1013–27 | date = November 1998 | pmid = 9817758 | pmc = 2132961 | doi = 10.1083/jcb.143.4.1013 }}</ref><ref name="pmid9804419">{{cite journal | vauthors = Mayans O, van der Ven PF, Wilm M, Mues A, Young P, Fürst DO, Wilmanns M, Gautel M | title = Structural basis for activation of the titin kinase domain during myofibrillogenesis | journal = Nature | volume = 395 | issue = 6705 | pages = 863–9 | date = October 1998 | pmid = 9804419 | doi = 10.1038/27603 }}</ref><ref name="pmid12446666">{{cite journal | vauthors = Zou P, Gautel M, Geerlof A, Wilmanns M, Koch MH, Svergun DI | title = Solution scattering suggests cross-linking function of telethonin in the complex with titin | journal = The Journal of Biological Chemistry | volume = 278 | issue = 4 | pages = 2636–44 | date = January 2003 | pmid = 12446666 | doi = 10.1074/jbc.M210217200 }}</ref><ref name="pmid9645487">{{cite journal | vauthors = Mues A, van der Ven PF, Young P, Fürst DO, Gautel M | title = Two immunoglobulin-like domains of the Z-disc portion of titin interact in a conformation-dependent way with telethonin | journal = FEBS Letters | volume = 428 | issue = 1–2 | pages = 111–4 | date = May 1998 | pmid = 9645487 | doi = 10.1016/S0014-5793(98)00501-8 }}</ref> and
* [[TRIM63]].<ref name="pmid11243782">{{cite journal | vauthors = Centner T, Yano J, Kimura E, McElhinny AS, Pelin K, Witt CC, Bang ML, Trombitas K, Granzier H, Gregorio CC, Sorimachi H, Labeit S | title = Identification of muscle specific ring finger proteins as potential regulators of the titin kinase domain | journal = Journal of Molecular Biology | volume = 306 | issue = 4 | pages = 717–26 | date = March 2001 | pmid = 11243782 | doi = 10.1006/jmbi.2001.4448 }}</ref>
{{Div col end}}
== Linguistic significance ==
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This has been discussed extensively on this article's talk page and the consensus is to *not* provide the full chemical name of titin here. Please see the talk page for details.
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The name titin is derived from the Greek [[Titan (mythology)|Titan]] (a giant deity, anything of great size).<ref name="pmid291034"/>
As the largest known protein, titin also has the longest [[International Union of Pure and Applied Chemistry nomenclature|IUPAC name]] of a protein. The full chemical name of the human canonical form of titin, which starts ''[[Methionine|methionyl]]...'' and ends ''...[[isoleucine]]'', contains 189,819 letters and is sometimes stated to be the [[Longest word in English|longest word in the English language]], or [[longest words|any language]].<ref name="urlSarah McCulloch">{{cite web | url = http://www.sarahmcculloch.com/luminary-uprise/2009/longest-word/ | title = Longest word in English | vauthors = McCulloch S | work = Sarah McCulloch.com |archiveurl=https://web.archive.org/web/20100114221953/http://www.sarahmcculloch.com/luminaryuprise/longest-word.html |archivedate=2010-01-14 | accessdate = 2016-10-12 }}</ref> However, [[List of lexicographers|lexicographers]] regard generic names of [[chemical compound]]s as ''verbal [[Chemical formula|formulae]]'' rather than English words.<ref>{{cite web | author = Oxford Word and Language Service team | title = Ask the experts - What is the longest English word? | publisher = AskOxford.com / [[Oxford University Press]] | url = http://www.askoxford.com/asktheexperts/faq/aboutwords/longestword | accessdate = 2008-01-13 | archive-url = https://web.archive.org/web/20080913173417/http://www.askoxford.com/asktheexperts/faq/aboutwords/longestword | archive-date = 2008-09-13 | dead-url = yes}}</ref>
==See also==
*[[Longest word in English]]
== Referensi ==
{{Reflist|35em}}
== Bacaan lanjutan ==
{{refbegin|35em}}
* {{cite journal | vauthors = Tskhovrebova L, Trinick J | title = Titin: properties and family relationships | journal = Nature Reviews Molecular Cell Biology | volume = 4 | issue = 9 | pages = 679–89 | date = September 2003 | pmid = 14506471 | doi = 10.1038/nrm1198 }}
* {{cite journal | vauthors = Kinbara K, Sorimachi H, Ishiura S, Suzuki K | title = Skeletal muscle-specific calpain, p49: structure and physiological function | journal = Biochemical Pharmacology | volume = 56 | issue = 4 | pages = 415–20 | date = August 1998 | pmid = 9763216 | doi = 10.1016/S0006-2952(98)00095-1 }}
* {{cite journal | vauthors = Kolmerer B, Witt CC, Freiburg A, Millevoi S, Stier G, Sorimachi H, Pelin K, Carrier L, Schwartz K, Labeit D, Gregorio CC, Linke WA, Labeit S | title = The titin cDNA sequence and partial genomic sequences: insights into the molecular genetics, cell biology and physiology of the titin filament system | journal = Reviews of Physiology, Biochemistry and Pharmacology | volume = 138 | issue = | pages = 19–55 | year = 1999 | pmid = 10396137 | doi = 10.1007/BF02346659 }}
* {{cite journal | vauthors = Trinick J, Tskhovrebova L | title = Titin: a molecular control freak | journal = Trends in Cell Biology | volume = 9 | issue = 10 | pages = 377–80 | date = October 1999 | pmid = 10481174 | doi = 10.1016/S0962-8924(99)01641-4 }}
* {{cite journal | vauthors = Sorimachi H, Ono Y, Suzuki K | title = Skeletal muscle-specific calpain, p94, and connectin/titin: their physiological functions and relationship to limb-girdle muscular dystrophy type 2A | journal = Advances in Experimental Medicine and Biology | volume = 481 | issue = | pages = 383–95; discussion 395–7 | year = 2000 | pmid = 10987085 | doi = 10.1007/978-1-4615-4267-4_23 }}
* {{cite journal | vauthors = Tskhovrebova L, Trinick J | title = Role of titin in vertebrate striated muscle | journal = Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences | volume = 357 |issue = 1418 | pages = 199–206 | date = February 2002 | pmid = 11911777 | pmc = 1692937 | doi = 10.1098/rstb.2001.1028 }}
* {{cite journal | vauthors = Sela BA | title = [Titin: some aspects of the largest protein in the body] | journal = Harefuah | volume = 141 | issue = 7 | pages = 631–5, 665 | date = July 2002 | pmid = 12187564 | doi = }}
* {{cite journal | vauthors = Tskhovrebova L, Trinick J | title = Properties of titin immunoglobulin and fibronectin-3 domains | journal = The Journal of Biological Chemistry | volume = 279 | issue = 45 | pages = 46351–4 | date = November 2004 | pmid = 15322090 | doi = 10.1074/jbc.R400023200 }}
* {{cite journal | vauthors = Wu Y, Labeit S, Lewinter MM, Granzier H | title = Titin: an endosarcomeric protein that modulates myocardial stiffness in DCM | journal = Journal of Cardiac Failure | volume = 8 | issue = 6 Suppl | pages = S276-86 | date = December 2002 | pmid = 12555133 | doi = 10.1054/jcaf.2002.129278 }}
{{refend}}
== Pranala luar ==
{{Wiktionary pipe|Appendix:List of protologisms/Long words/Titin|the full chemical name of titin}}
* [https://www.ncbi.nlm.nih.gov/bookshelf/br.fcgi?book=gene&part=hyper-card GeneReviews/NIH/NCBI/UW entry on Familial Hypertrophic Cardiomyopathy Overview]
* [https://www.ncbi.nlm.nih.gov/bookshelf/br.fcgi?book=gene&part=udd GeneReviews/NCBI/NIH/UW entry on Udd Distal Myopathy, Tibial Muscular Dystrophy, Udd Myopathy]
* [https://www.ncbi.nlm.nih.gov/books/NBK83297/ GeneReviews/NIH/NCBI/UW entry on Salih Myopathy or Early-Onset Myopathy with Fatal Cardiomyopathy]
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[[Category:Protein struktural]]
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