Myosin Binding Protein C, Cardiac (MYBPC3) ELISA Kits

Cow (Bovine) Myosin Binding Protein C, Cardiac (MYBPC3) Interaktionspartner

1. N terminus of cMyBP-C interacts with F-actin through multiple distinct binding sites and that binding at one or more sites is reduced by phosphorylation

Mouse (Murine) Myosin Binding Protein C, Cardiac (MYBPC3) Interaktionspartner

1. these findings suggest the possibility that Fhod3 contributes to the pathogenesis of cMyBP-C-related cardiomyopathy and that Fhod3 is critically involved in cMyBP-C-mediated regulation of cardiac function via direct interaction.

2. Diltiazem recently showed promising beneficial effects in pre-clinical HCM, particularly in patients carrying MYBPC3 mutations.

3. the widely observed phenomenon of slowed force development in the presence of cMyBP-C may actually be a manifestation of cooperative binding of this protein to the thin filament.

4. autophagy is impaired in Mybpc3-targeted knockin mice

5. cMyBP-C lacking the S2 binding site is incorporated normally into the sarcomere, although systolic function is compromised.

6. these data indicate a robust proinflammatory response in DCM hearts, likely in response to cellular damage triggered by MYBPC3 mutation and resultant contractile dysfunction.

7. We provide evidence that haploinsufficiency and poison polypeptide hypotheses are disease mechanisms and that EHTs can be used as a platform to evaluate the direct impact of (newly identified) MYBPC3 gene variants.

8. These results support the proposal that cMyBP-C stabilises the thick filament and that the loss of cMyBP-C results in an untethering of myosin heads.

9. Crypts are a normal part of cardiac development but, along with the mitral valve and trabeculae, their developmental trajectory is altered by the presence of HCM truncating Mybpc3 gene mutation

10. that in the homozygous hypertrophic cardiomyopathy mouse model, beta-AR stimulation leads to preferential PKA phosphorylation of phospholamban over cardiac troponin I, resulting in an impaired inotropic and lusitropic response

11. Phosphorylation of MYBPC3 contributes to the genesis of ventricular wall geometry, linking myofilament biology with multiscale cardiac mechanics and myoarchitecture.

12. The cMyBP-C hypertrophic cardiomyopathy variant L348P enhances thin filament activation through an increased shift in tropomyosin position.

13. The contributions of cardiac myosin binding protein C and troponin I phosphorylation to beta-adrenergic enhancement of in vivo cardiac function

14. calcium levels at the peak of contraction would allow cMyBP-C to remain a potent contractile modulator, regardless of cMyBP-C's phosphorylation state

15. Phosphorylation reduced the level of molecular disorder and the distribution of C0C2 intramolecular distances became more compact, with probes flanking either the motif between C1 and C2 or the Pro/Ala-rich linker (PAL) between C0 and C1

16. the phosphorylation pattern of sMyBP-C is differentially regulated following reversible (i.e. fatigue) and non-reversible (i.e. age and disease) (patho)physiological stressors.

17. The proline/alanine-rich region and the C1 domain of cMyBP-C are not critical for normal cardiac contraction in mice.

18. the phosphorylation pattern of sMyBP-C is differentially regulated in response to age and disease, suggesting that phosphorylation plays important roles in these processes.

19. MYBPC3 mutations is elevated oxidative stress that corresponded to severe cardiac dysfunction, myocyte damage, and myocardial remodeling.

20. MBPC and troponin-I phosphorylation modulate myofilament length-dependent activation

Human Myosin Binding Protein C, Cardiac (MYBPC3) Interaktionspartner

1. Conflicting interpretations of pathogenicity have been reported for the Pro873His MYBPC3 variant described here. Our patient, presenting with two copies of the variant and devoid of a normal allele, progressed to end-stage heart failure, which supports the notion of a deleterious effect of this variant in the homozygous form.

2. Of the 52 hypertrophic cardiomyopathy patients 11 (21.2%) had MYBPC3 variants.

3. MYBPC3 does not seem to play a role in anthracycline induced cardiotoxicity.

4. Mutation in MYBPC3 was identified as Restrictive Cardiomyopathy - causing mutation.

5. pathogenic gene mutations in LMNA and MYBPC3 alter RNA splicing and may have a role in heart disease

6. MYBPC3 mutation carriers had a high frequency of ventricular arrhythmia and syncope. An absence of family history of sudden death (SD) and past history of syncope are useful prognostic factors in patients with hypertrophic cardiomyopathy. MYH7 and MYBPC3 mutations did not significantly influence prognosis compared to non-carriers. The patients with the MYBPC3 mutation should be closely followed for the possibility of SD.

7. Replacement Fibrosis was most abundantly present in the hearts with a MYBPC3 mutation that first presented with a Hypertrophic Cardiomyopathy.

8. Mutations in the gene MYBPC3 coding for cardiac myosin-binding protein-C (cMyBP-C), a multi-domain protein, are the most common cause of hypertrophic cardiomyopathy ..This molecular insight suggests that key HCM-causing mutations might significantly modify the native affinity required for the assembly of the domains in cMyBP-C, which is essential for normal cardiac function.

9. Our data demonstrate a critical role of the MLP/MyBP-C complex during early myoblast differentiation. Its absence in muscles with mutations or aberrant expression of MLP or MyBP-C could be directly implicated in the development of cardiac and skeletal myopathies.

10. Five of the 19 patients (26.3%) had either a pathogenic variant or a likely pathogenic variant in MYBPC3 (n=1), MYH7 (n=1), RYR2 (n=2), or TNNT2 (n=1). All five variants were missense variants that have been reported previously in patients with channelopathies or cardiomyopathies

11. Double heterozygotes for mutations in DSP and MYBPC3 showed a variable clinical presentation of arrhythmogenic cardiomyopathy and hypertrophic cardiomyopathy.

12. Data provide evidence that MYBPC3 mutations constitute the preeminent cause of hypertrophic cardiomyopathy (HCM) and that they are phenotypically indistinguishable from HCM caused by MYH7 mutations.

13. In children and young adults, a 2-parameter 12-lead A-ECG score is retrospectively significantly more sensitive and specific than pooled, age-specific conventional ECG criteria for detecting MYBPC3-HCM and in distinguishing such patients from healthy controls, including endurance-trained athletes.

14. mutations associated with a reduced super-relaxed state in hypertrophic cardiomyopathy

15. Study showed that CACNB2 is a possible candidate hypertrophy-modifying gene contributing to disease variability of MYBPC3-associated familial hypertrophic cardiomyopathy

16. The authors demonstrate myosin tail (S2)-dependent functional regulation of actin-activated human beta-cardiac myosin ATPase. In addition, they show that both S2 and MyBP-C bind to S1 and that phosphorylation of either S1 or MyBP-C weakens these interactions.

17. Our study supports that mutations in MYH7 and MYBPC3 should be the first focus of moleculargenetic analysis in HCM, and that mutations in TNNT2 have a low prevalence in Brazilian population. All mutations detected were missense mutations, whereas two mutations in MYH7 had not been described before.

18. These findings point to the critical role of MYBPC3 during sarcomere assembly in cardiac myocyte differentiation and suggest developmental influences of MYBPC3 truncating mutations on the mature hypertrophic phenotype.

19. The p.Pro108Alafs*9 mutation is associated with HCM, high penetrance, and disease onset in middle age

20. Study shows lack of phenotypic differences between MYH7- and MYBPC3-associated hypertrophic cardiomyopathy when assessed by cardiac magnetic resonance imaging.

Rabbit Myosin Binding Protein C, Cardiac (MYBPC3) Interaktionspartner

1. small es, CyrillicMyBP-C modulates interaction of myosin with actin