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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 10 Dec 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, Calpain, nebulin
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
The Crystal Structure of the Human Titin:Obscurin Complex Reveals a Conserved Yet Specific Muscle M-band Zipper Module.
New
Steiner et al., London, United Kingdom. In J Mol Biol, 06 Jan 2015
UNLABELLED: M10 is the most C-terminal immunoglobulin (Ig) domain of the giant protein titin and a frequent target of disease-linked mutations.
The Structure and Regulation of Human Muscle α-Actinin.
New
Impact
Djinović-Carugo et al., Vienna, Austria. In Cell, 04 Jan 2015
The structure provides insight into the phosphoinositide-based mechanism controlling its interaction with sarcomeric proteins such as titin, lays a foundation for studying the impact of pathogenic mutations at molecular resolution, and is likely to be broadly relevant for the regulation of spectrin-like proteins.
α-Synemin localizes to the M-band of the sarcomere through interaction with the M10 region of titin.
New
Russell et al., Kent, United States. In Febs Lett, 11 Dec 2014
Yeast-two hybrid analysis indicated that this region is a binding site for the M10 region of titin.
Increased myocardial stiffness due to cardiac titin isoform switching in a mouse model of volume overload limits eccentric remodeling.
New
Granzier et al., Tucson, United States. In J Mol Cell Cardiol, 08 Dec 2014
Titin-based passive tensions were significantly increased; a result of the decreased N2BA/N2B ratio.
Sarcomeric protein isoform transitions in cardiac muscle: A journey to heart failure.
Review
New
Guo et al., Laramie, United States. In Biochim Biophys Acta, 08 Dec 2014
In this mini-review, we summarized isoform transitions of several most widely examined sarcomeric proteins including myosin, actin, troponin, tropomyosin, titin and myosin binding protein-C, and the consequence of these abnormal isoform transitions.
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.
Acute exercise modifies titin phosphorylation and increases cardiac myofilament stiffness.
New
Krüger et al., Düsseldorf, Germany. In Front Physiol, Dec 2013
UNLABELLED: Titin-based myofilament stiffness is largely modulated by phosphorylation of its elastic I-band regions N2-Bus (decreases passive stiffness, PT) and PEVK (increases PT).
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.
[Comparative studies of amyloid properties of muscles proteins and brain Abeta-peptides and identification of approaches to destruction of their amyloids in vitro].
New
In Biofizika, Nov 2013
In this review our data on the comparative study of amyloid properties of titin family proteins and brain Abeta-peptides are represented.
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).
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
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