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LDB3 encodes a PDZ domain-containing protein. Additionally we are shipping LIM Domain Binding 3 Protein Proteins (5) and many more products for this protein.
Showing 10 out of 60 products:
Human Monoclonal LIM Domain Binding 3 Protein Primary Antibody for WB - ABIN393692
Zimmerman, Cox, Lakdawala, Cirino, Mancini-DiNardo, Clark, Leon, Duffy, White, Baxter, Alaamery, Farwell, Weiss, Seidman, Seidman, Ho, Rehm, Funke: A novel custom resequencing array for dilated cardiomyopathy. in Genetics in medicine : official journal of the American College of Medical Genetics 2010
Show all 5 references for ABIN393692
Human Monoclonal LIM Domain Binding 3 Protein Primary Antibody for IF, RNAi - ABIN524582
Arimura, Inagaki, Hayashi, Shichi, Sato, Hinohara, Vatta, Towbin, Chikamori, Yamashina, Kimura: Impaired binding of ZASP/Cypher with phosphoglucomutase 1 is associated with dilated cardiomyopathy. in Cardiovascular research 2009
Show all 2 references for ABIN524582
Dog (Canine) Polyclonal LIM Domain Binding 3 Protein Primary Antibody for WB - ABIN374603
Selcen, Engel: Mutations in ZASP define a novel form of muscular dystrophy in humans. in Annals of neurology 2005
this is the first family with Arrhythmogenic right ventricular cardiomyopathy where a mutation in LDB3 is associated with Arrhythmogenic right ventricular cardiomyopathy
Study identified abnormal inclusion of LDB3 exon 11 specific to myotonic dystrophy type at the RNA and protein level; inclusion changed the affinity of LDB3 for PKC, indicating that exon 11 may contribute to the activation of PKC in DM1
results show that MFM-associated ZASP mutations in the actin-binding domain have deleterious effects on the core structure of the Z-discs in skeletal muscle.
Z-band alternatively spliced PDZ motif protein (ZASP) is the major O-linked beta-N-acetylglucosamine-substituted protein in human heart myofibrils
This results of this indicted that One patient harbored the missense mutation c.1719G>A (p.V566M) in the ZASP gene.
ZASP1 can form protein complex with telethonin/T-Cap (show TCAP Antibodies) and Na(v)1.5. The left ventricular noncompaction-specific ZASP1 mutation can cause loss of function of Na(v)1.5, without significant alteration of the cytoskeletal protein (show ACTN1 Antibodies) complex.
TNNT3 and LDB3 showed abnormal splicing and appeared more pronounced in myotonic dystrophies type 2 relative to myotonic dystrophies type 1.
the D626N mutation of Cypher/ZASP increases the affinity of the LIM (show PDLIM5 Antibodies) domain for protein kinase C (show PKC Antibodies), which may be related to pathogenesis of dilated cardiomyopathy
ZASP/Cypher internal fragments containing either ZM exon 4 or 6 co-localized with alpha-actinin (show ACTN1 Antibodies) in cultured myoblasts and nonmuscle cells.
ZASP/Cypher anchors PGM1 (show PGM1 Antibodies) to Z-disc under conditions of stress. The impaired binding of PGM1 (show PGM1 Antibodies) to ZASP/Cypher might be involved in the pathogenesis of dilated cardiomyopathy.
Cypher and ENH (show PDLIM5 Antibodies) redundantly play an essential role in sustaining Z-line structure from the earliest stages of cardiac function, and are redundantly required to maintain normal embryonic heart function and embryonic viability.
Results indicte that Cypher/ZASP interacted with the regulatory subunit RIIalpha of PKA.
Data demonstrated that the Z-disk proteins, ZASP, titin (show TTN Antibodies) and vinculin (show VCL Antibodies) preferentially bind to alpha-actinin-2 (show ACTN2 Antibodies).
Deletion of long but not short Cypher isoforms leads to late-onset dilated cardiomyopathy.
mutations of a structural/cytoskeletal protein (show ADD3 Antibodies), such as ZASP, lead to cardiac functional and electric abnormalities.
Cypher isoforms are developmentally regulated in both skeletal and cardiac muscle
Cypher plays a pivotal role in adult cardiac structure and function through protein-protein interactions with other Z-line proteins.
This gene encodes a PDZ domain-containing protein. PDZ motifs are modular protein-protein interaction domains consisting of 80-120 amino acid residues. PDZ domain-containing proteins interact with each other in cytoskeletal assembly or with other proteins involved in targeting and clustering of membrane proteins. The protein encoded by this gene interacts with alpha-actinin-2 through its N-terminal PDZ domain and with protein kinase C via its C-terminal LIM domains. The LIM domain is a cysteine-rich motif defined by 50-60 amino acids containing two zinc-binding modules. This protein also interacts with all three members of the myozenin family. Mutations in this gene have been associated with myofibrillar myopathy and dilated cardiomyopathy. Alternatively spliced transcript variants encoding different isoforms have been identified\; all isoforms have N-terminal PDZ domains while only longer isoforms (1, 2 and 5) have C-terminal LIM domains.
LIM domain binding 3
, LIM domain binding 3 like
, LIM domain-binding protein 3
, PDZ and LIM domain 6
, Z-band alternatively spliced PDZ-motif protein
, protein cypher
, PDZ-LIM domain protein
, oracle protein
, protein oracle