Similar articles for PMID: 23886664

Year	Number of Results
1996	1
1999	2
2000	2
2001	5
2002	2
2003	2
2004	3
2005	3
2006	3
2007	6
2008	7
2009	7
2010	5
2011	4
2012	7
2013	8
2014	8
2015	8
2016	6
2017	4
2018	9
2019	4
2020	9
2021	6
2022	2
2023	1
2024	0

1

Mutations in repeating structural motifs of tropomyosin cause gain of function in skeletal muscle myopathy patients.

Marston S, Memo M, Messer A, Papadaki M, Nowak K, McNamara E, Ong R, El-Mezgueldi M, Li X, Lehman W. Marston S, et al. Hum Mol Genet. 2013 Dec 15;22(24):4978-87. doi: 10.1093/hmg/ddt345. Epub 2013 Jul 25. Hum Mol Genet. 2013. PMID: 23886664 Free PMC article.

2

Skeletal muscle myopathy mutations at the actin tropomyosin interface that cause gain- or loss-of-function.

Memo M, Marston S. Memo M, et al. J Muscle Res Cell Motil. 2013 Aug;34(3-4):165-9. doi: 10.1007/s10974-013-9344-y. Epub 2013 May 30. J Muscle Res Cell Motil. 2013. PMID: 23719967

3

Mutation update and genotype-phenotype correlations of novel and previously described mutations in TPM2 and TPM3 causing congenital myopathies.

Marttila M, Lehtokari VL, Marston S, Nyman TA, Barnerias C, Beggs AH, Bertini E, Ceyhan-Birsoy O, Cintas P, Gerard M, Gilbert-Dussardier B, Hogue JS, Longman C, Eymard B, Frydman M, Kang PB, Klinge L, Kolski H, Lochmüller H, Magy L, Manel V, Mayer M, Mercuri E, North KN, Peudenier-Robert S, Pihko H, Probst FJ, Reisin R, Stewart W, Taratuto AL, de Visser M, Wilichowski E, Winer J, Nowak K, Laing NG, Winder TL, Monnier N, Clarke NF, Pelin K, Grönholm M, Wallgren-Pettersson C. Marttila M, et al. Hum Mutat. 2014 Jul;35(7):779-90. doi: 10.1002/humu.22554. Epub 2014 May 1. Hum Mutat. 2014. PMID: 24692096 Free PMC article.

4

Congenital myopathies: diseases of the actin cytoskeleton.

Clarkson E, Costa CF, Machesky LM. Clarkson E, et al. J Pathol. 2004 Nov;204(4):407-17. doi: 10.1002/path.1648. J Pathol. 2004. PMID: 15495263 Review.

5

The Primary Causes of Muscle Dysfunction Associated with the Point Mutations in Tpm3.12; Conformational Analysis of Mutant Proteins as a Tool for Classification of Myopathies.

Borovikov YS, Karpicheva OE, Simonyan AO, Avrova SV, Rogozovets EA, Sirenko VV, Redwood CS. Borovikov YS, et al. Int J Mol Sci. 2018 Dec 10;19(12):3975. doi: 10.3390/ijms19123975. Int J Mol Sci. 2018. PMID: 30544720 Free PMC article.

6

Aberrant movement of β-tropomyosin associated with congenital myopathy causes defective response of myosin heads and actin during the ATPase cycle.

Borovikov YS, Avrova SV, Rysev NA, Sirenko VV, Simonyan AO, Chernev AA, Karpicheva OE, Piers A, Redwood CS. Borovikov YS, et al. Arch Biochem Biophys. 2015 Jul;577-578:11-23. doi: 10.1016/j.abb.2015.05.002. Epub 2015 May 13. Arch Biochem Biophys. 2015. PMID: 25978979

7

Congenital myopathy-causing tropomyosin mutations induce thin filament dysfunction via distinct physiological mechanisms.

Ochala J, Gokhin DS, Pénisson-Besnier I, Quijano-Roy S, Monnier N, Lunardi J, Romero NB, Fowler VM. Ochala J, et al. Hum Mol Genet. 2012 Oct 15;21(20):4473-85. doi: 10.1093/hmg/dds289. Epub 2012 Jul 13. Hum Mol Genet. 2012. PMID: 22798622 Free PMC article.

8

Myopathy-causing Q147P TPM2 mutation shifts tropomyosin strands further towards the open position and increases the proportion of strong-binding cross-bridges during the ATPase cycle.

Karpicheva OE, Simonyan AO, Kuleva NV, Redwood CS, Borovikov YS. Karpicheva OE, et al. Biochim Biophys Acta. 2016 Mar;1864(3):260-267. doi: 10.1016/j.bbapap.2015.12.004. Epub 2015 Dec 17. Biochim Biophys Acta. 2016. PMID: 26708479

9

The reason for the low Ca²⁺-sensitivity of thin filaments associated with the Glu41Lys mutation in the TPM2 gene is "freezing" of tropomyosin near the outer domain of actin and inhibition of actin monomer switching off during the ATPase cycle.

Avrova SV, Karpicheva OE, Rysev NA, Simonyan AO, Sirenko VV, Redwood CS, Borovikov YS. Avrova SV, et al. Biochem Biophys Res Commun. 2018 Jul 12;502(2):209-214. doi: 10.1016/j.bbrc.2018.05.145. Epub 2018 May 26. Biochem Biophys Res Commun. 2018. PMID: 29792862

10

Congenital myopathy-related mutations in tropomyosin disrupt regulatory function through altered actin affinity and tropomodulin binding.

Moraczewska J, Robaszkiewicz K, Śliwinska M, Czajkowska M, Ly T, Kostyukova A, Wen H, Zheng W. Moraczewska J, et al. FEBS J. 2019 May;286(10):1877-1893. doi: 10.1111/febs.14787. Epub 2019 Mar 5. FEBS J. 2019. PMID: 30768849 Free PMC article.

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