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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 24 Oct 2014.

Titin

titin
This gene encodes a large abundant protein of striated muscle. The product of this gene is divided into two regions, a N-terminal I-band and a C-terminal A-band. The I-band, which is the elastic part of the molecule, contains two regions of tandem immunoglobulin domains on either side of a PEVK region that is rich in proline, glutamate, valine and lysine. The A-band, which is thought to act as a protein-ruler, contains a mixture of immunoglobulin and fibronectin repeats, and possesses kinase activity. 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 chromosomes. Alternative splicing of this gene results in multiple transcript variants. 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. Mutations in this gene are associated with familial hypertrophic cardiomyopathy 9, and autoantibodies to titin are produced in patients with the autoimmune disease scleroderma. [provided by RefSeq, Feb 2012] (from NCBI)
Top mentioned proteins: CAN, Actin, HAD, nebulin, V1a
Papers using titin antibodies
Obscurin, a giant sarcomeric Rho guanine nucleotide exchange factor protein involved in sarcomere assembly
Supplier
Gautel Mathias et al., In The Journal of Cell Biology, 1998
... For titin total human cardiac cDNA (CLONTECH Laboratories, Inc.) was used ...
M line–deficient titin causes cardiac lethality through impaired maturation of the sarcomere
Supplier
Gotthardt Michael et al., In The Journal of Cell Biology, 1997
... Generation of titin M-line knockout miceThe transgenic mice with loxP sites ...
Papers on titin
Effect of supraspinatus tendon injury on supraspinatus and infraspinatus muscle passive tension and associated biochemistry.
New
Ward et al., San Diego, United States. In J Bone Joint Surg Am, 15 Nov 2014
Passive mechanical tests of both individual fibers and fiber bundles as well as analysis of titin molecular weight and collagen content were performed.
FORCE ENHANCEMENT AFTER STRETCH IN MAMMALIAN MUSCLE FIBRE: NO EVIDENCE OF CROSSBRIDGE INVOLVEMENT.
New
Colombini et al., Florence, Italy. In Am J Physiol Cell Physiol, 08 Nov 2014
All our data indicate that ST, or RFE, is independent of the crossbridge presence and it is due to the Ca(2+)-induced stiffening of a sarcomeric structure identifiable with titin.
Ablation of Plasma Membrane Ca(2+)-ATPase Isoform 4 Prevents Development of Hypertrophy in a Model of Hypertrophic Cardiomyopathy.
New
Shull et al., Cincinnati, United States. In J Mol Cell Cardiol, 30 Oct 2014
Expression of the metabolic substrate transporters glucose transporter 4 and carnitine palmitoyltransferase 1b was preserved and Tm180-related changes in mRNA levels of various contractile stress-related proteins including the cardiac ankyrin protein CARP and the N2B isoform of titin were reversed in Tm180/PMCA4-null hearts.
Genetic basis of limb-girdle muscular dystrophies: the 2014 update.
New
Savarese et al., In Acta Myol, May 2014
The autosomal recessive forms (LGMD2) are: LGMD2A (calpain 3), LGMD2B (dysferlin), LGMD2C (gamma sarcoglycan), LGMD2D (alpha sarcoglycan), LGMD2E (beta sarcoglycan), LGMD2F (delta sarcoglycan), LGMD2G (telethonin), LGMD2H (TRIM32), LGMD2I (FKRP), LGMD2J (titin), LGMD2K (POMT1), LGMD2L (anoctamin 5), LGMD2M (fukutin), LGMD2N (POMT2), LGMD2O (POMTnG1), LGMD2P (dystroglycan), LGMD2Q (plectin), LGMD2R (desmin), LGMD2S (TRAPPC11), LGMD2T (GMPPB), LGMD2U (ISPD), LGMD2V (Glucosidase, alpha ), LGMD2W (PINCH2).
Genetic basis of limb-girdle muscular dystrophies: the 2014 update.
Review
New
Savarese et al., Napoli, Italy. In Acta Myol, May 2014
The autosomal recessive forms (LGMD2) are: LGMD2A (calpain 3), LGMD2B (dysferlin), LGMD2C (γ sarcoglycan), LGMD2D (α sarcoglycan), LGMD2E (β sarcoglycan), LGMD2F (δ sarcoglycan), LGMD2G (telethonin), LGMD2H (TRIM32), LGMD2I (FKRP), LGMD2J (titin), LGMD2K (POMT1), LGMD2L (anoctamin 5), LGMD2M (fukutin), LGMD2N (POMT2), LGMD2O (POMTnG1), LGMD2P (dystroglycan), LGMD2Q (plectin), LGMD2R (desmin), LGMD2S (TRAPPC11), LGMD2T (GMPPB), LGMD2U (ISPD), LGMD2V (Glucosidase, alpha ), LGMD2W (PINCH2).
Gigantic business: titin properties and function through thick and thin.
Review
New
Hamdani et al., Bochum, Germany. In Circ Res, Apr 2014
TTN, which encodes titin, is also a major human disease gene.
S-glutathionylation of cryptic cysteines enhances titin elasticity by blocking protein folding.
New
Impact
Fernández et al., New York City, United States. In Cell, Apr 2014
The giant elastic protein titin is a determinant factor in how much blood fills the left ventricle during diastole and thus in the etiology of heart disease.
Titin (visco-) elasticity in skeletal muscle myofibrils.
New
Herzog et al., In Mol Cell Biomech, Mar 2014
Titin is the third most abundant protein in sarcomeres and fulfills a number of mechanical and signaling functions.
High-speed force spectroscopy unfolds titin at the velocity of molecular dynamics simulations.
New
Impact
Scheuring et al., Marseille, France. In Science, Dec 2013
The mechanical unfolding of the muscle protein titin by atomic force microscopy was a landmark in our understanding of single-biomolecule mechanics.
Mutational heterogeneity in cancer and the search for new cancer-associated genes.
New
Impact
Getz et al., Cambridge, United States. In Nature, Aug 2013
The list includes many implausible genes (such as those encoding olfactory receptors and the muscle protein titin), suggesting extensive false-positive findings that overshadow true driver events.
Three-dimensional structure of the human myosin thick filament: clinical implications.
Review
Al-Khayat, Doha, Qatar. In Glob Cardiol Sci Pract, 2012
titin and myosin binding protein C) are known to be associated with a number of familial human cardiomyopathies (e.g.
Intracellular regulation of matrix metalloproteinase-2 activity: new strategies in treatment and protection of heart subjected to oxidative stress.
Review
Sawicki, Saskatoon, Canada. In Scientifica (cairo), 2012
One such mechanism involves the proteolytic degradation of contractile proteins, such as troponin I (TnI), myosin heavy chain, titin, and the myosin light chains (MLC1 and MLC2) by matrix metalloproteinase-2 (MMP-2).
Structure of giant muscle proteins.
Review
Wright et al., Harrisonburg, United States. In Front Physiol, 2012
Giant muscle proteins (e.g., titin, nebulin, and obscurin) play a seminal role in muscle elasticity, stretch response, and sarcomeric organization.
A novel mechanism involving four-and-a-half LIM domain protein-1 and extracellular signal-regulated kinase-2 regulates titin phosphorylation and mechanics.
GeneRIF
Sheikh et al., San Diego, United States. In J Biol Chem, 2012
A novel mechanism involving four-and-a-half LIM domain protein-1 and extracellular signal-regulated kinase-2 regulates titin phosphorylation and mechanics.
Independent evolution of striated muscles in cnidarians and bilaterians.
Impact
Technau et al., Vienna, Austria. In Nature, 2012
Cnidarians and ctenophores possess striated muscle myhc orthologues but lack crucial components of bilaterian striated muscles, such as genes that code for titin and the troponin complex, suggesting the convergent evolution of striated muscles.
Spontaneous dimerization of titin protein Z1Z2 domains induces strong nanomechanical anchoring.
GeneRIF
Fernández et al., London, United Kingdom. In J Biol Chem, 2012
Spontaneous dimerization of titin protein Z1Z2 domains induces strong nanomechanical anchoring.
Titin mutation segregates with hereditary myopathy with early respiratory failure.
GeneRIF
Chinnery et al., Newcastle upon Tyne, United Kingdom. In Brain, 2012
This study presented that patients with hereditary myopathy with early respiratory failure linke with Titin mutation.
Hereditary myopathy with early respiratory failure associated with a mutation in A-band titin.
GeneRIF
Oldfors et al., Göteborg, Sweden. In Brain, 2012
This study identified three different Swedish Hereditary myopathy with early respiratory failure families with a new mutation in the A-band titin.
The Sjögren-Larsson syndrome gene encodes a hexadecenal dehydrogenase of the sphingosine 1-phosphate degradation pathway.
GeneRIF
Kihara et al., Sapporo, Japan. In Mol Cell, 2012
the Sjogren-Larsson syndrome-causative gene ALDH3A2 is responsible for conversion of the sphingosine 1-phosphate degradation product hexadecenal to hexadecenoic acid
RBM20, a gene for hereditary cardiomyopathy, regulates titin splicing.
Impact
GeneRIF
Gotthardt et al., Madison, United States. In Nat Med, 2012
In addition to titin (TTN), we identified a set of 30 genes with conserved splicing regulation between humans and rats
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