AHNAK, a novel component of the dysferlin protein complex, redistributes to the cytoplasm with dysferlin during skeletal muscle regeneration
about
Diabetic cardiomyopathy-associated dysfunction in spatially distinct mitochondrial subpopulationsAhnak1 is a tuneable modulator of cardiac Ca(v)1.2 calcium channel activityAhnak1 abnormally localizes in muscular dystrophies and contributes to muscle vesicle releaseCalpain 3 is a modulator of the dysferlin protein complex in skeletal muscleDysferlin at transverse tubules regulates Ca(2+) homeostasis in skeletal muscleFerlins: regulators of vesicle fusion for auditory neurotransmission, receptor trafficking and membrane repairLack of correlation between outcomes of membrane repair assay and correction of dystrophic changes in experimental therapeutic strategy in dysferlinopathyStructure of a C-terminal AHNAK peptide in a 1:2:2 complex with S100A10 and an acetylated N-terminal peptide of annexin A2Periaxin and AHNAK Nucleoprotein 2 Form Intertwined Homodimers through Domain SwappingNovel protein-protein interactions inferred from literature contextCaveolin regulates endocytosis of the muscle repair protein, dysferlinMembrane damage-induced vesicle-vesicle fusion of dysferlin-containing vesicles in muscle cells requires microtubules and kinesin.Comparison of dysferlin expression in human skeletal muscle with that in monocytes for the diagnosis of dysferlin myopathy.Dysferlin interacts with tubulin and microtubules in mouse skeletal muscle.Phylogenetic analysis of ferlin genes reveals ancient eukaryotic origins.Recessive mutations in the putative calcium-activated chloride channel Anoctamin 5 cause proximal LGMD2L and distal MMD3 muscular dystrophies.Proteomic analysis of the dysferlin protein complex unveils its importance for sarcolemmal maintenance and integrityAHNAK2 is a potential prognostic biomarker in patients with PDAC.The effects of MyD88 deficiency on disease phenotype in dysferlin-deficient A/J mice: role of endogenous TLR ligands.Clathrin-independent carriers form a high capacity endocytic sorting system at the leading edge of migrating cells.Dysferlin interacts with histone deacetylase 6 and increases alpha-tubulin acetylationModular dispensability of dysferlin C2 domains reveals rational design for mini-dysferlin molecules.GRAF1 deficiency blunts sarcolemmal injury repair and exacerbates cardiac and skeletal muscle pathology in dystrophin-deficient mice.Obesity Resistance and Enhanced Insulin Sensitivity in Ahnak-/- Mice Fed a High Fat Diet Are Related to Impaired Adipogenesis and Increased Energy Expenditure.Dysferlin and animal models for dysferlinopathyPlasma Membrane Repair: A Central Process for Maintaining Cellular Homeostasis.Dysferlin and muscle membrane repair.Intermolecular disulfide bond in the dimerization of S-periaxin mediated by Cys88 and Cys139Dynamic interactions between L-type voltage-sensitive calcium channel Cav1.2 subunits and ahnak in osteoblastic cells.Genetic manipulation of dysferlin expression in skeletal muscle: novel insights into muscular dystrophy.Dysferlin and myoferlin regulate transverse tubule formation and glycerol sensitivity.Proteome Changes Induced by Imatinib and Novel Imatinib Derivatives in K562 Human Chronic Myeloid Leukemia CellsTranslational research and therapeutic perspectives in dysferlinopathies.Ferlin proteins in myoblast fusion and muscle growth.Dysferlin-deficient muscular dystrophy and innate immune activation.Annexin A2 complexes with S100 proteins: structure, function and pharmacological manipulation.Identification of calcium-independent and calcium-enhanced binding between S100B and the dopamine D2 receptorIntrinsic indicators for specimen degradation.The S100A10-annexin A2 complex provides a novel asymmetric platform for membrane repair.The C type natriuretic peptide receptor tethers AHNAK1 at the plasma membrane to potentiate arachidonic acid-induced calcium mobilization.
P2860
0b3d51501082eddcde6c08f72c5c5cf0cc79329c4085aee21a2fa201a791dd2ff08281a108435e6b4109cb85d1440ae9cd8d706c79eeee9eb5ce05a356ebf1cb45daa171dcb241575017a70f024b25a45d3cf86af1a5ee8187ca6e5df827aa478a4b5a2e730381167dea90b8e7a309c151137a782e300ed896b3632a96e1de0d953c8854223a94c5201b8815a2dcfbf1f643594799109462e050e5bd445e6401a989baf3ab75bcd4ca04bef593d6d6f9d5619b9de92ed6ff09eb7c372af1d35da0f9c912349eec6f
P248
Q23912644-19E477CB-2C68-4FFC-9318-3FCDB9420205Q24295015-51FF3508-957D-4650-AA98-FBC5C43B6E3DQ24296220-B26F2071-3ECD-41C8-9EFB-9269CB685663Q24615708-8FDD3B84-3AD5-4D01-9C0A-788D8A827DB5Q26866519-DA9E2C84-6E72-4860-819C-B840E169D499Q27022787-86341DEE-8381-4FF3-80CC-1CE23FB547BEQ27301945-142D7695-B3AD-425D-A93B-1A9CB5CE4B36Q27675650-E8A7E0D3-8327-4CDD-8E58-FE8E4EA3FE4EQ27682578-D3499236-5925-48CF-A29E-D1DDE9588095Q27967980-9C4D82ED-52D2-4255-BA36-419F0D94F15CQ28261848-7D6C2516-2865-4148-8E7B-8AB6A45D272DQ28301480-433960C3-F8C5-47B7-B561-715B2C45510DQ31043843-2D7299A1-FD4D-478B-AF2B-91C4091129D1Q33559890-DD4057A1-FFF4-440C-8565-0F44FB1C90DDQ33643829-ECB9AA03-5D11-435F-BF91-5C75B9F5EB17Q33645910-E485A275-CC4B-4BD2-A4C1-BE04C1080B32Q33747737-39117884-0D9A-4057-BA8D-D3155BC38965Q33761904-1607758E-54D3-4BE7-B21F-235099999334Q33808490-7955ACC8-C24F-40BA-9B60-8DF639C23E5AQ34083148-A9A89202-0F09-49F0-9056-3EF412E26364Q34103199-FAED8962-F1AE-47A1-A8DD-492062527210Q34318021-D7EA5905-C535-4891-8315-806AB5C9AD0CQ35753474-5E6F61AF-FF78-4261-AE1C-46DB3277745DQ35806814-04A9C15C-9C57-4B0A-A11E-9CC8063191EBQ36085192-CFAB5CEB-66DD-4CBF-92BA-0D71817CD913Q36240722-6DD3BDE5-BE3B-4D1C-B167-E75D883773AEQ36282549-EBFE92F2-F9CA-485E-82CF-0057796B7277Q36949608-CEA2BBED-FB4A-45B1-BA27-747CFCF4555EQ37190325-FAD40596-5CE7-49AD-A82F-783EFB854649Q37413634-D35AB506-BFB5-42E7-A912-7C51172026EFQ37415471-89A7A0EF-BCDD-4B8A-8122-A4C7832441C1Q37636455-EBA1B31B-16A1-4B65-B221-25DD3A6DF8EAQ37873747-F786849B-FF83-4F80-A4AB-A4CC571C1B3EQ37881301-33F9D141-ACAC-413D-96F0-C913F3654913Q38092854-8B81AC9F-042E-4989-A141-5C9DC0171AA3Q38258912-BAB82B12-1026-4DA6-9998-A193547B0499Q38745891-C7E3EEC9-D085-49F5-8A22-D91C4BED8057Q39232322-898BFBF8-D69F-4803-BFBE-B180FE45577EQ39244179-3388B31C-C854-4EC4-8051-E1414DEBA5A7Q39807751-37D312A6-48D8-4771-91F0-9EB0277FD368
P2860
AHNAK, a novel component of the dysferlin protein complex, redistributes to the cytoplasm with dysferlin during skeletal muscle regeneration
description
2007 nî lūn-bûn
@nan
2007 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի մարտին հրատարակված գիտական հոդված
@hy
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
name
AHNAK, a novel component of th ...... g skeletal muscle regeneration
@ast
AHNAK, a novel component of th ...... g skeletal muscle regeneration
@en
AHNAK, a novel component of th ...... g skeletal muscle regeneration
@en-gb
AHNAK, a novel component of th ...... g skeletal muscle regeneration
@nl
type
label
AHNAK, a novel component of th ...... g skeletal muscle regeneration
@ast
AHNAK, a novel component of th ...... g skeletal muscle regeneration
@en
AHNAK, a novel component of th ...... g skeletal muscle regeneration
@en-gb
AHNAK, a novel component of th ...... g skeletal muscle regeneration
@nl
prefLabel
AHNAK, a novel component of th ...... g skeletal muscle regeneration
@ast
AHNAK, a novel component of th ...... g skeletal muscle regeneration
@en
AHNAK, a novel component of th ...... g skeletal muscle regeneration
@en-gb
AHNAK, a novel component of th ...... g skeletal muscle regeneration
@nl
P2093
P921
P356
P1433
P1476
AHNAK, a novel component of th ...... g skeletal muscle regeneration
@en
P2093
Alexandra van Remoortere
Andre Deelder
Chriselle Benaud
Jacques Baudier
Johan T den Dunnen
Kate Bushby
Louise V B Anderson
Rune R Frants
Steven H Laval
Yanchao Huang
P304
P356
10.1096/FJ.06-6628COM
P407
P577
2007-03-01T00:00:00Z