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{{Infobox_gene}}
{{PBB_Controls
'''MYH7''' is a [[gene]] encoding a [[myosin]] heavy chain beta (MHC-β) isoform (slow twitch) expressed primarily in the heart, but also in skeletal muscles (type I fibers).<ref>{{cite journal | vauthors = Quiat D, Voelker KA, Pei J, Grishin NV, Grange RW, Bassel-Duby R, Olson EN | title = Concerted regulation of myofiber-specific gene expression and muscle performance by the transcriptional repressor Sox6 | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 108 | issue = 25 | date = Jun 2011 | pmid = 21633012 | doi = 10.1073/pnas.1107413108 | pmc=3121857 | pages=10196–201}}</ref> This isoform is distinct from the fast isoform of cardiac myosin heavy chain, [[MYH6]], referred to as MHC-α. MHC-β is the major protein comprising the thick filament in cardiac muscle and plays a major role in cardiac [[muscle contraction]].
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| require_manual_inspection = no
| update_protein_box = yes
| update_summary = no
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Structure ==
{{GNF_Protein_box
| image = PBB_Protein_MYH7_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2fxm.
| PDB = {{PDB2|2fxm}}, {{PDB2|2fxo}}
| Name = Myosin, heavy chain 7, cardiac muscle, beta
| HGNCid = 7577
| Symbol = MYH7
| AltSymbols =; CMD1S; CMH1; MGC138376; MGC138378; MPD1; MYHCB
| OMIM = 160760
| ECnumber = 
| Homologene = 68044
| MGIid = 2155600
| GeneAtlas_image1 = PBB_GE_MYH7_204737_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_MYH7_216265_x_at_tn.png
| Function = {{GNF_GO|id=GO:0000146 |text = microfilament motor activity}} {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003779 |text = actin binding}} {{GNF_GO|id=GO:0005516 |text = calmodulin binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0008307 |text = structural constituent of muscle}} {{GNF_GO|id=GO:0016887 |text = ATPase activity}} {{GNF_GO|id=GO:0030898 |text = actin-dependent ATPase activity}}
| Component = {{GNF_GO|id=GO:0005859 |text = muscle myosin complex}} {{GNF_GO|id=GO:0005863 |text = striated muscle thick filament}} {{GNF_GO|id=GO:0016459 |text = myosin complex}}
| Process = {{GNF_GO|id=GO:0002027 |text = cardiac chronotropy}} {{GNF_GO|id=GO:0006941 |text = striated muscle contraction}} {{GNF_GO|id=GO:0007512 |text = adult heart development}} {{GNF_GO|id=GO:0030049 |text = muscle filament sliding}} {{GNF_GO|id=GO:0055010 |text = ventricular cardiac muscle morphogenesis}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 4625
    | Hs_Ensembl = ENSG00000092054
    | Hs_RefseqProtein = NP_000248
    | Hs_RefseqmRNA = NM_000257
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 14
    | Hs_GenLoc_start = 22951789
    | Hs_GenLoc_end = 22974690
    | Hs_Uniprot = P12883
    | Mm_EntrezGene = 140781
    | Mm_Ensembl = 
    | Mm_RefseqmRNA = NM_080728
    | Mm_RefseqProtein = NP_542766
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 
    | Mm_GenLoc_start = 
    | Mm_GenLoc_end = 
    | Mm_Uniprot = 
  }}
}}
'''MYH7''' is a [[gene]] encoding a [[myosin]] heavy chain beta (MHC-β) isoform (slow twitch) expressed primarily in the heart.


Changes in the relative abundance of MHC-β and MHC-α (MYH6, the fast isoform of cardiac myosin heavy chain) correlate with the contractile velocity of [[cardiac muscle]].<ref>{{cite web | title = Entrez Gene: MYH7 myosin, heavy chain 7, cardiac muscle, beta| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4625| accessdate = }}</ref> In early fetal development, MHC-β is predominately expressed in the ventricles, while MHC-α is predominantly expressed in the atria. In healthy adult hearts, MHC-α is predominantly expressed in the atria (>90%), while MHC-β (~50%) is expressed in the atria of failing adult hearts.
'''MHC-β''' is a 223 kDa protein composed of 1935 amino acids.<ref>{{cite web|url=http://www.heartproteome.org/copa/ProteinInfo.aspx?QType=Protein%20ID&QValue=P12883|accessdate=2015-10-14|website=heartproteome.org|title=Cardiac Organellar Protein Atlas Knowledgebase (COPaKB)}}</ref><ref>{{Cite journal
In vitro studies have demonstrated that newly formed cardiac myocytes express MHC-β, and after prolonged (1-5 weeks) contractile activity MHC-α becomes detectable.
| pmid = 23965338
An allelic variant of this gene is associated with approximately 40% of the cases of [[Hypertrophic cardiomyopathy]] (HCM). This condition is an [[autosomal-dominant disease]], in which a single copy of the variant gene causes enlargement of the left [[Ventricle (heart)|ventricle]] of the heart. Disease onset usually occurs later in life, perhaps triggered by changes in [[thyroid hormone]] function and/or physical stress.
| pmc = 4076475
| year = 2013
| author1 = Zong
| first1 = N. C.
| title = Integration of cardiac proteome biology and medicine by a specialized knowledgebase
| journal = Circulation Research
| volume = 113
| issue = 9
| pages = 1043–53
| last2 = Li
| first2 = H
| last3 = Li
| first3 = H
| last4 = Lam
| first4 = M. P.
| last5 = Jimenez
| first5 = R. C.
| last6 = Kim
| first6 = C. S.
| last7 = Deng
| first7 = N
| last8 = Kim
| first8 = A. K.
| last9 = Choi
| first9 = J. H.
| last10 = Zelaya
| first10 = I
| last11 = Liem
| first11 = D
| last12 = Meyer
| first12 = D
| last13 = Odeberg
| first13 = J
| last14 = Fang
| first14 = C
| last15 = Lu
| first15 = H. J.
| last16 = Xu
| first16 = T
| last17 = Weiss
| first17 = J
| last18 = Duan
| first18 = H
| last19 = Uhlen
| first19 = M
| last20 = Yates Jr
| first20 = 3rd
| last21 = Apweiler
| first21 = R
| last22 = Ge
| first22 = J
| last23 = Hermjakob
| first23 = H
| last24 = Ping
| first24 = P
| doi = 10.1161/CIRCRESAHA.113.301151
}}</ref> '''MHC-β''' is a hexameric, asymmetric motor forming the bulk of the thick filament in cardiac muscle. '''MHC-β''' is composed of N-terminal globular heads (20&nbsp;nm) that project laterally, and alpha helical tails (130&nbsp;nm) that dimerize and multimerize into a coiled-coil motif to form the light meromyosin (LMM), thick filament rod. The 9&nbsp;nm alpha-helical neck region of each MHC-β head non-covalently binds two light chains, essential light chain ([[MYL3]]) and regulatory light chain ([[MYL2]]).<ref>{{cite journal | vauthors = Palmer BM | title = Thick filament proteins and performance in human heart failure | journal = Heart Failure Reviews | volume = 10 | issue = 3 | date = Sep 2005 | pmid = 16416042 | doi = 10.1007/s10741-005-5249-1 | pages=187–97}}</ref>  Approximately 300 myosin molecules constitute one thick filament.<ref>{{cite journal | vauthors = Harris SP, Lyons RG, Bezold KL | title = In the thick of it: HCM-causing mutations in myosin binding proteins of the thick filament | journal = Circulation Research | volume = 108 | issue = 6 | date = Mar 2011 | pmid = 21415409 | doi = 10.1161/CIRCRESAHA.110.231670 | pmc=3076008 | pages=751–764}}</ref> There are two isoforms of cardiac MHC, α and β, which display 93% homology. MHC-α and MHC-β display significantly different enzymatic properties, with α having 150-300% the contractile velocity and 60-70% actin attachment time as that of β.<ref>{{cite journal | vauthors = Palmer BM | title = Thick filament proteins and performance in human heart failure | journal = Heart Failure Reviews | volume = 10 | issue = 3 | date = Sep 2005 | pmid = 16416042 | doi = 10.1007/s10741-005-5249-1 | pages=187–97}}</ref><ref>{{cite journal | vauthors = Alpert NR, Brosseau C, Federico A, Krenz M, Robbins J, Warshaw DM | title = Molecular mechanics of mouse cardiac myosin isoforms | journal = American Journal of Physiology. Heart and Circulatory Physiology | volume = 283 | issue = 4 | date = Oct 2002 | pmid = 12234796 | doi = 10.1152/ajpheart.00274.2002 | pages=H1446-54}}</ref> MHC-β is predominately expressed in the human ventricle, while MHC-α is predominantly expressed in human atria.{{citation needed|date=March 2015}}


==References==
== Function ==
 
It is the enzymatic activity of the ATPase in the myosin head that cyclically hydrolyzes ATP, fueling the myosin power stroke. This process converts chemical to mechanical energy, and propels shortening of the sarcomeres in order to generate intraventricular pressure and power. An accepted mechanism for this process is that ADP-bound myosin attaches to actin while thrusting tropomyosin inwards,<ref>{{cite journal | vauthors = McKillop DF, Geeves MA | title = Regulation of the interaction between actin and myosin subfragment 1: evidence for three states of the thin filament | journal = Biophysical Journal | volume = 65 | issue = 2 | date = Aug 1993 | pmid = 8218897 | doi = 10.1016/S0006-3495(93)81110-X | pmc=1225772 | pages=693–701}}</ref> then the S1-S2 myosin lever arm rotates ~70° about the converter domain and drives actin filaments towards the M-line.<ref>{{cite journal | vauthors = Tyska MJ, Warshaw DM | title = The myosin power stroke | journal = Cell Motility and the Cytoskeleton | volume = 51 | issue = 1 | date = Jan 2002 | pmid = 11810692 | doi = 10.1002/cm.10014 | pages=1–15}}</ref>
 
== Clinical significance ==
 
Several mutations in MYH7 have been associated with inherited cardiomyopathies. Lowrance et al. were the first to identify the causative mutation [[Arginine|Arg]]403[[Glutamine|Gln]] for [[hypertrophic cardiomyopathy]] (HCM) in the MYH7 gene.<ref>{{Cite journal
| pmid = 1975517
| year = 1990
| author1 = Geisterfer-Lowrance
| first1 = A. A.
| title = A molecular basis for familial hypertrophic cardiomyopathy: A beta cardiac myosin heavy chain gene missense mutation
| journal = Cell
| volume = 62
| issue = 5
| pages = 999–1006
| last2 = Kass
| first2 = S
| last3 = Tanigawa
| first3 = G
| last4 = Vosberg
| first4 = H. P.
| last5 = McKenna
| first5 = W
| last6 = Seidman
| first6 = C. E.
| last7 = Seidman
| first7 = J. G.
| doi=10.1016/0092-8674(90)90274-i
}}</ref> Studies have since identified several more MYH7 mutations, that are estimated to be causal in approximately 40% of [[hypertrophic cardiomyopathy|HCM]] cases. This condition is an [[autosomal-dominant disease]], in which a single copy of the variant gene causes enlargement of the left [[Ventricle (heart)|ventricle]] of the heart.  Disease onset usually occurs later in life, perhaps triggered by changes in [[thyroid hormone]] function and/or physical stress.
 
Another condition associated to mutations in this gene is paraspinal and proximal muscle atrophy.<ref>{{cite journal | vauthors = Park JM, Kim YJ, Yoo JH, Hong YB, Park JH, Koo H, Chung KW, Choi BO | title = A novel MYH7 mutation with prominent paraspinal and proximal muscle involvement | journal = Neuromuscular Disorders | volume = 23 | issue = 7 | date = Jul 2013 | pmid = 23707328 | doi = 10.1016/j.nmd.2013.04.003 | pages=580–6}}</ref>
 
[[File:A-de-novo-germline-mutation-in-MYH7-causes-a-progressive-dominant-myopathy-in-pigs-1471-2156-13-99-S1.ogv|thumb|left|250px|A [[myopathy]] caused by a MYH7 mutation in pigs.]]
{{Clear}}
 
== References ==
{{reflist|2}}
{{reflist|2}}
==Further reading==
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Jaaskelainen P, Miettinen R, Karkkainen P, Toivonen L, Laakso M, Kuusisto J | title = Genetics of hypertrophic cardiomyopathy in eastern Finland: few founder mutations with benign or intermediary phenotypes | journal = Annals of Medicine | volume = 36 | issue = 1 | pages = 23–32 | year = 2004 | pmid = 15000344 | doi = 10.1080/07853890310017161 }}
| citations =
* {{cite journal | vauthors = Kamisago M, Schmitt JP, McNamara D, Seidman C, Seidman JG | title = Sarcomere protein gene mutations and inherited heart disease: a beta-cardiac myosin heavy chain mutation causing endocardial fibroelastosis and heart failure | journal = Novartis Foundation Symposium | volume = 274 | issue =  | pages = 176–89; discussion 189–95, 272–6 | year = 2007 | pmid = 17019812 | doi = 10.1002/0470029331.ch11 }}
*{{cite journal | author=Jääskeläinen P, Miettinen R, Kärkkäinen P, ''et al.'' |title=Genetics of hypertrophic cardiomyopathy in eastern Finland: few founder mutations with benign or intermediary phenotypes. |journal=Ann. Med. |volume=36 |issue= 1 |pages= 23-32 |year= 2004 |pmid= 15000344 |doi= }}
*{{cite journal | author=Kamisago M, Schmitt JP, McNamara D, ''et al.'' |title=Sarcomere protein gene mutations and inherited heart disease: a beta-cardiac myosin heavy chain mutation causing endocardial fibroelastosis and heart failure. |journal=Novartis Found. Symp. |volume=274 |issue=  |pages= 176-89; discussion 189-95, 272-6 |year= 2007 |pmid= 17019812 |doi= }}
}}
{{refend}}
{{refend}}


==External links==
== External links ==
* [http://www.heartproteome.org/copa/ProteinInfo.aspx?QType=Protein%20ID&QValue=P12883 Mass spectrometry characterization of MYH7 at COPaKB] <ref>{{Cite journal
| pmid = 23965338
| pmc = 4076475
| year = 2013
| author1 = Zong
| first1 = N. C.
| title = Integration of cardiac proteome biology and medicine by a specialized knowledgebase
| journal = Circulation Research
| volume = 113
| issue = 9
| pages = 1043–53
| last2 = Li
| first2 = H
| last3 = Li
| first3 = H
| last4 = Lam
| first4 = M. P.
| last5 = Jimenez
| first5 = R. C.
| last6 = Kim
| first6 = C. S.
| last7 = Deng
| first7 = N
| last8 = Kim
| first8 = A. K.
| last9 = Choi
| first9 = J. H.
| last10 = Zelaya
| first10 = I
| last11 = Liem
| first11 = D
| last12 = Meyer
| first12 = D
| last13 = Odeberg
| first13 = J
| last14 = Fang
| first14 = C
| last15 = Lu
| first15 = H. J.
| last16 = Xu
| first16 = T
| last17 = Weiss
| first17 = J
| last18 = Duan
| first18 = H
| last19 = Uhlen
| first19 = M
| last20 = Yates Jr
| first20 = 3rd
| last21 = Apweiler
| first21 = R
| last22 = Ge
| first22 = J
| last23 = Hermjakob
| first23 = H
| last24 = Ping
| first24 = P
| doi = 10.1161/CIRCRESAHA.113.301151
}}</ref>
* [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=mpd1  GeneReviews/NCBI/NIH/UW entry on Laing Distal Myopathy]
* {{MeshName|MYH7+protein,+human}}
* {{MeshName|MYH7+protein,+human}}
{{PDB Gallery|geneid=4625}}
{{Cytoskeletal Proteins}}


[[Category:Motor proteins]]
[[Category:Motor proteins]]
 
[[Category:Articles containing video clips]]
{{protein-stub}}
{{WikiDoc Sources}}

Latest revision as of 07:12, 4 September 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

MYH7 is a gene encoding a myosin heavy chain beta (MHC-β) isoform (slow twitch) expressed primarily in the heart, but also in skeletal muscles (type I fibers).[1] This isoform is distinct from the fast isoform of cardiac myosin heavy chain, MYH6, referred to as MHC-α. MHC-β is the major protein comprising the thick filament in cardiac muscle and plays a major role in cardiac muscle contraction.

Structure

MHC-β is a 223 kDa protein composed of 1935 amino acids.[2][3] MHC-β is a hexameric, asymmetric motor forming the bulk of the thick filament in cardiac muscle. MHC-β is composed of N-terminal globular heads (20 nm) that project laterally, and alpha helical tails (130 nm) that dimerize and multimerize into a coiled-coil motif to form the light meromyosin (LMM), thick filament rod. The 9 nm alpha-helical neck region of each MHC-β head non-covalently binds two light chains, essential light chain (MYL3) and regulatory light chain (MYL2).[4] Approximately 300 myosin molecules constitute one thick filament.[5] There are two isoforms of cardiac MHC, α and β, which display 93% homology. MHC-α and MHC-β display significantly different enzymatic properties, with α having 150-300% the contractile velocity and 60-70% actin attachment time as that of β.[6][7] MHC-β is predominately expressed in the human ventricle, while MHC-α is predominantly expressed in human atria.[citation needed]

Function

It is the enzymatic activity of the ATPase in the myosin head that cyclically hydrolyzes ATP, fueling the myosin power stroke. This process converts chemical to mechanical energy, and propels shortening of the sarcomeres in order to generate intraventricular pressure and power. An accepted mechanism for this process is that ADP-bound myosin attaches to actin while thrusting tropomyosin inwards,[8] then the S1-S2 myosin lever arm rotates ~70° about the converter domain and drives actin filaments towards the M-line.[9]

Clinical significance

Several mutations in MYH7 have been associated with inherited cardiomyopathies. Lowrance et al. were the first to identify the causative mutation Arg403Gln for hypertrophic cardiomyopathy (HCM) in the MYH7 gene.[10] Studies have since identified several more MYH7 mutations, that are estimated to be causal in approximately 40% of HCM cases. This condition is an autosomal-dominant disease, in which a single copy of the variant gene causes enlargement of the left ventricle of the heart. Disease onset usually occurs later in life, perhaps triggered by changes in thyroid hormone function and/or physical stress.

Another condition associated to mutations in this gene is paraspinal and proximal muscle atrophy.[11]

File:A-de-novo-germline-mutation-in-MYH7-causes-a-progressive-dominant-myopathy-in-pigs-1471-2156-13-99-S1.ogv
A myopathy caused by a MYH7 mutation in pigs.

References

  1. ↑ Quiat D, Voelker KA, Pei J, Grishin NV, Grange RW, Bassel-Duby R, Olson EN (Jun 2011). "Concerted regulation of myofiber-specific gene expression and muscle performance by the transcriptional repressor Sox6". Proceedings of the National Academy of Sciences of the United States of America. 108 (25): 10196–201. doi:10.1073/pnas.1107413108. PMC 3121857. PMID 21633012.
  2. ↑ "Cardiac Organellar Protein Atlas Knowledgebase (COPaKB)". heartproteome.org. Retrieved 2015-10-14.
  3. ↑ Zong, N. C.; Li, H; Li, H; Lam, M. P.; Jimenez, R. C.; Kim, C. S.; Deng, N; Kim, A. K.; Choi, J. H.; Zelaya, I; Liem, D; Meyer, D; Odeberg, J; Fang, C; Lu, H. J.; Xu, T; Weiss, J; Duan, H; Uhlen, M; Yates Jr, 3rd; Apweiler, R; Ge, J; Hermjakob, H; Ping, P (2013). "Integration of cardiac proteome biology and medicine by a specialized knowledgebase". Circulation Research. 113 (9): 1043–53. doi:10.1161/CIRCRESAHA.113.301151. PMC 4076475. PMID 23965338.
  4. ↑ Palmer BM (Sep 2005). "Thick filament proteins and performance in human heart failure". Heart Failure Reviews. 10 (3): 187–97. doi:10.1007/s10741-005-5249-1. PMID 16416042.
  5. ↑ Harris SP, Lyons RG, Bezold KL (Mar 2011). "In the thick of it: HCM-causing mutations in myosin binding proteins of the thick filament". Circulation Research. 108 (6): 751–764. doi:10.1161/CIRCRESAHA.110.231670. PMC 3076008. PMID 21415409.
  6. ↑ Palmer BM (Sep 2005). "Thick filament proteins and performance in human heart failure". Heart Failure Reviews. 10 (3): 187–97. doi:10.1007/s10741-005-5249-1. PMID 16416042.
  7. ↑ Alpert NR, Brosseau C, Federico A, Krenz M, Robbins J, Warshaw DM (Oct 2002). "Molecular mechanics of mouse cardiac myosin isoforms". American Journal of Physiology. Heart and Circulatory Physiology. 283 (4): H1446–54. doi:10.1152/ajpheart.00274.2002. PMID 12234796.
  8. ↑ McKillop DF, Geeves MA (Aug 1993). "Regulation of the interaction between actin and myosin subfragment 1: evidence for three states of the thin filament". Biophysical Journal. 65 (2): 693–701. doi:10.1016/S0006-3495(93)81110-X. PMC 1225772. PMID 8218897.
  9. ↑ Tyska MJ, Warshaw DM (Jan 2002). "The myosin power stroke". Cell Motility and the Cytoskeleton. 51 (1): 1–15. doi:10.1002/cm.10014. PMID 11810692.
  10. ↑ Geisterfer-Lowrance, A. A.; Kass, S; Tanigawa, G; Vosberg, H. P.; McKenna, W; Seidman, C. E.; Seidman, J. G. (1990). "A molecular basis for familial hypertrophic cardiomyopathy: A beta cardiac myosin heavy chain gene missense mutation". Cell. 62 (5): 999–1006. doi:10.1016/0092-8674(90)90274-i. PMID 1975517.
  11. ↑ Park JM, Kim YJ, Yoo JH, Hong YB, Park JH, Koo H, Chung KW, Choi BO (Jul 2013). "A novel MYH7 mutation with prominent paraspinal and proximal muscle involvement". Neuromuscular Disorders. 23 (7): 580–6. doi:10.1016/j.nmd.2013.04.003. PMID 23707328.

Further reading

  • Jaaskelainen P, Miettinen R, Karkkainen P, Toivonen L, Laakso M, Kuusisto J (2004). "Genetics of hypertrophic cardiomyopathy in eastern Finland: few founder mutations with benign or intermediary phenotypes". Annals of Medicine. 36 (1): 23–32. doi:10.1080/07853890310017161. PMID 15000344.
  • Kamisago M, Schmitt JP, McNamara D, Seidman C, Seidman JG (2007). "Sarcomere protein gene mutations and inherited heart disease: a beta-cardiac myosin heavy chain mutation causing endocardial fibroelastosis and heart failure". Novartis Foundation Symposium. 274: 176–89, discussion 189–95, 272–6. doi:10.1002/0470029331.ch11. PMID 17019812.

External links

  1. ↑ Zong, N. C.; Li, H; Li, H; Lam, M. P.; Jimenez, R. C.; Kim, C. S.; Deng, N; Kim, A. K.; Choi, J. H.; Zelaya, I; Liem, D; Meyer, D; Odeberg, J; Fang, C; Lu, H. J.; Xu, T; Weiss, J; Duan, H; Uhlen, M; Yates Jr, 3rd; Apweiler, R; Ge, J; Hermjakob, H; Ping, P (2013). "Integration of cardiac proteome biology and medicine by a specialized knowledgebase". Circulation Research. 113 (9): 1043–53. doi:10.1161/CIRCRESAHA.113.301151. PMC 4076475. PMID 23965338.
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