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  Vol. 58 No. 6, June 2001 TABLE OF CONTENTS
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Titin, Thymoma, and Myasthenia Gravis

Arch Neurol. 2001;58:869-870.

Since this article does not have an abstract, we have provided the first 150 words of the full text and any section headings.

TITIN WAS FIRST described in 1977 and given the name connectin.1 This giant, filamentous protein found in striated muscle was not demonstrated earlier because its size made it inaccessible to most techniques employed for protein identification. Titin is the largest molecule so far identified in the human body and has a molecular weight of about 3000 kd. Although abundant, it constitutes only approximately 10% of the total protein mass of striated muscle. Each titin molecule spans a half sarcomere, from the Z disk to the M line.2 The titin filaments contribute to muscle assembly and to the ability of muscle to spring back after it is stretched. Length changes in titin during stretching and contraction occur mainly in the I band, while the A band is functionally stiff and highly ordered.

Antibodies to titin were first discovered in the serum of patients with myasthenia gravis (MG) in 1990.3 Under immunoelectron . . . [Full Text of this Article]



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RELATED ARTICLE

Anti-Titin Antibodies in Myasthenia Gravis: Tight Association With Thymoma and Heterogeneity of Nonthymoma Patients
Ana Maria Yamamoto, Philippe Gajdos, Bruno Eymard, Christine Tranchant, Jean-Marie Warter, Lucienne Gomez, Charles Bourquin, Jean-François Bach, and Henri-Jean Garchon
Arch Neurol. 2001;58(6):885-890.
ABSTRACT | FULL TEXT  


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES

Classification of Myasthenia Gravis Based on Autoantibody Status
Suzuki et al.
Arch Neurol 2007;64:1121-1124.
ABSTRACT | FULL TEXT  





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