Contractile properties of EDL and soleus muscles of myostatin-deficient mice. - Test2 - elhamkhani - TriplyDB

Contractile properties of EDL and soleus muscles of myostatin-deficient mice.

Contractile properties of EDL and soleus muscles of myostatin-deficient mice.

http://www.wikidata.org/entity/Q33869605

about

Decreased specific force and power production of muscle fibers from myostatin-deficient mice are associated with a suppression of protein degradation Effect of Postnatal Myostatin Inhibition on Bite Mechanics in Mice Dystrophin-deficient dogs with reduced myostatin have unequal muscle growth and greater joint contractures.Inflammation induced loss of skeletal muscle TGF-β family signaling in stem cells p38 MAPK signaling in postnatal tendon growth and remodeling Endocranial and masticatory muscle volumes in myostatin-deficient mice A PGC-1α isoform induced by resistance training regulates skeletal muscle hypertrophy Myostatin inhibition in muscle, but not adipose tissue, decreases fat mass and improves insulin sensitivity.Systemic myostatin inhibition via liver-targeted gene transfer in normal and dystrophic mice Combination of myostatin pathway interference and dystrophin rescue enhances tetanic and specific force in dystrophic mdx mice Intrinsic stiffness of extracellular matrix increases with age in skeletal muscles of mice.Grip force, EDL contractile properties, and voluntary wheel running after postdevelopmental myostatin depletion in mice.The muscle fiber type-fiber size paradox: hypertrophy or oxidative metabolism?Endurance exercise training in myostatin null mice.METABOLIC FUNCTIONS OF MYOSTATIN AND GDF11.Silencing Myostatin Using Cholesterol-conjugated siRNAs Induces Muscle Growth Inhibition of 5-LOX, COX-1, and COX-2 increases tendon healing and reduces muscle fibrosis and lipid accumulation after rotator cuff repair.Hindlimb skeletal muscle function in myostatin-deficient mice.Tendons of myostatin-deficient mice are small, brittle, and hypocellular.Simvastatin reduces fibrosis and protects against muscle weakness after massive rotator cuff tear.Increased energy expenditure and leptin sensitivity account for low fat mass in myostatin-deficient mice.Translational signalling, atrogenic and myogenic gene expression during unloading and reloading of skeletal muscle in myostatin-deficient mice.Symmorphosis through dietary regulation: a combinatorial role for proteolysis, autophagy and protein synthesis in normalising muscle metabolism and function of hypertrophic mice after acute starvation.Effect of pulmonary TNF-α overexpression on mouse isolated skeletal muscle function Mouse forepaw lumbrical muscles are resistant to age-related declines in force production.Long-term systemic myostatin inhibition via liver-targeted gene transfer in golden retriever muscular dystrophy.Transforming growth factor-beta induces skeletal muscle atrophy and fibrosis through the induction of atrogin-1 and scleraxis.Double Muscling in Cattle: Genes, Husbandry, Carcasses and Meat.Haploinsufficiency of myostatin protects against aging-related declines in muscle function and enhances the longevity of mice.Measurement of Maximum Isometric Force Generated by Permeabilized Skeletal Muscle Fibers.Activin Receptor Type IIB Inhibition Improves Muscle Phenotype and Function in a Mouse Model of Spinal Muscular Atrophy Excess TGF-β mediates muscle weakness associated with bone metastases in mice.Investigating mechanisms underpinning the detrimental impact of a high-fat diet in the developing and adult hypermuscular myostatin null mouse.Atrogin-1, MuRF-1, and sarcopenia.Deletion of Mbtps1 (Pcsk8, S1p, Ski-1) Gene in Osteocytes Stimulates Soleus Muscle Regeneration and Increased Size and Contractile Force with Age.Age-dependent alteration in muscle regeneration: the critical role of tissue niche.Targeted inhibition of TGF-β results in an initial improvement but long-term deficit in force production after contraction-induced skeletal muscle injury.Myostatin in the pathophysiology of skeletal muscle.Enhanced exercise and regenerative capacity in a mouse model that violates size constraints of oxidative muscle fibres

P2860

Q24632867-0C32B906-A05A-4A6C-83C5-C129FD0504E1 Q27301008-B5F81584-99CF-46CA-ACAE-148A831F6BC7 Q27321253-CF3E9A0F-F5DA-48C7-95E9-F5906B13389A Q28083759-FEFC33B0-86D0-4497-AE55-B3D3E38FED12 Q28274611-B320F6DF-A9B8-4583-80CD-3A9FC1486D76 Q28544034-F53982A0-2FAA-49C2-A340-19123FAA44BB Q28646797-436FBA8C-0611-4A98-A0C9-0948A7E03357 Q30415879-33B1CD08-E97C-46A1-8563-AED603C097A4 Q33419373-D9050879-B552-4407-A024-0629683DFE21 Q33531816-EC0A3EDF-CCCC-4AFB-9A51-5E8ED634FDCE Q33931629-823E02A1-4833-4D53-982C-6A28189A3B3B Q34063148-1E691BD6-AD29-4BC8-8045-00368C031B07 Q34151237-93801A68-B8E3-4C81-850D-F3F8C6817E96 Q34213640-CFC5C978-218F-432F-A176-4A4D2EFE6558 Q34291438-B165CBE5-AF48-4336-B510-DCEADD62EC3D Q34447001-F6F4FB0A-0AE9-4A90-B576-7C10D03C9ED6 Q34536058-89695EB6-7936-47CC-925D-3EEFF822CDD0 Q34579999-DA4BE255-B0F2-455E-B06B-FB166A2496D1 Q34642974-77141D20-2333-4199-B204-E40E351A4C02 Q34730991-EB971547-BB19-4D52-8C50-45803253FA30 Q34921512-842934AB-0986-4C64-AD97-BBFAC0CA827E Q35055457-4EFF63F3-80F8-409C-992B-815F91AED8B9 Q35144174-9E5C2A96-77F9-4138-82AA-786616704B0E Q35217500-18629147-6ACF-48A1-9D64-EFB55B14C218 Q35396763-EA293915-FC25-4FF3-8ABC-446294C63565 Q35418023-0974C8A5-FDFD-4F5A-A978-0A7FB2CE1B9F Q35612576-B43017F5-F2CF-429D-A89B-07D3E9CF92BD Q35632615-7DEF41BC-F187-4D78-BF02-6E67A5711B8A Q35826856-F455C11E-B005-406A-ADAE-C8C3DEFC9B3F Q35935212-38CECCD9-E01F-464B-B1A9-34F8CCF8F7BE Q35983285-8AA560B2-7DF1-43DF-ACE4-DDFED8AD6289 Q36199822-DDB3C14B-93B1-4B3F-B9E5-9C7070ED606B Q36258000-A0DA6C92-AEDB-44C5-8465-CB2A33E7B2ED Q36350797-D7BDBA1C-2D74-48BA-82BE-672ACE060964 Q36651458-3B619B24-DEB9-4339-B687-CFDE545CC089 Q36744463-D611423A-9AFA-4E89-9E81-0DEB932E17E3 Q37034374-3473FCDD-AF80-477C-B7B9-36E3555CA9ED Q37093970-D3889317-CB5B-4DE0-AC1E-1F90037E0738 Q37108137-A7162116-1DA9-43C6-91A5-21ABF9B6220F Q37155835-48674003-4004-42CA-A2D6-75A4A2CC5E25

P2860

Contractile properties of EDL and soleus muscles of myostatin-deficient mice.

http://www.wikidata.org/entity/Q33869605

description

2006 nî lūn-bûn

@nan

2006 թուականի Մայիսին հրատարակուած գիտական յօդուած

@hyw

2006 թվականի մայիսին հրատարակված գիտական հոդված

@hy

2006年の論文

@ja

2006年論文

@yue

2006年論文

@zh-hant

2006年論文

@zh-hk

2006年論文

@zh-mo

2006年論文

@zh-tw

2006年论文

@wuu

name

Contractile properties of EDL and soleus muscles of myostatin-deficient mice.

@ast

Contractile properties of EDL and soleus muscles of myostatin-deficient mice.

@en

type

label

Contractile properties of EDL and soleus muscles of myostatin-deficient mice.

@ast

Contractile properties of EDL and soleus muscles of myostatin-deficient mice.

@en

prefLabel

Contractile properties of EDL and soleus muscles of myostatin-deficient mice.

@ast

Contractile properties of EDL and soleus muscles of myostatin-deficient mice.

@en

P1433

Q33869605-3C2C6778-E8EB-493F-85C3-95806316DD5B

P1476

Q33869605-2EDCD058-C7CF-4D31-8115-15D8A99FAD05

P2093

Q33869605-389DB0FB-4383-49A1-8345-2E334BC71624

Q33869605-5E30681F-BB27-477A-9096-453835B6FA54

Q33869605-68614E4A-BD58-4E47-9946-F07C001869AD

P2860

Q33869605-0499D36B-779C-44BD-8C9C-693A111945EC

Q33869605-083CB75E-CEF6-40E1-A52B-D734D5D7CABD

Q33869605-17CEA97A-20CB-4BD3-83BA-EC436E13A8C4

Q33869605-1C7C6ED6-CF57-4186-B343-82FF09351598

Q33869605-1D159C1A-26EF-4062-B5C0-C93077B9A4F3

Q33869605-1ECFAA4D-4C1D-4D0C-AB95-25DF1FD7F70E

Q33869605-23679E3D-8CB5-464A-A98C-7544FB8FE998

Q33869605-25DA0309-2FB0-42EE-91BD-7BE1F69CEDB4

Q33869605-2916C012-235B-4C5F-8C43-BBC74D7EA0B3

Q33869605-2A8420A1-E873-4167-B80A-24D7E108EF6D

P304

Q33869605-480F8B97-405A-42C4-AD2B-C6B91CE26256

P31

Q33869605-A5FE483C-ED68-4602-B8DA-0FEF29DE251B

P356

Q33869605-1B4422DA-B7BA-4C2B-B8EF-DB34F673C82D

P407

Q33869605-8F7C8062-A4B1-40C0-A6C2-9D6EFB22DBBF

P433

Q33869605-ED79ED5A-416A-4608-B64F-005D2E227FE6

P478

Q33869605-3A395C1D-E43E-4838-8F6A-FE634C4F4280

P50

Q33869605-CC9C7412-3BD4-4281-9B11-269040A807AE

P577

Q33869605-E577CEA2-30DB-4C5F-999E-0FBBA3919CDA

P5875

Q33869605-EC966F51-9D47-4DB9-B851-C13ECB0B700F

P698

Q33869605-124A1DBD-7E85-458D-8CB4-99B8AB152DCA

P932

Q33869605-5EE50E36-8D79-483D-85D3-AF5920208892

P356

JAPPLPHYSIOL.00126.2006

P1433

Journal of Applied Physiology

P1476

Contractile properties of EDL and soleus muscles of myostatin-deficient mice.

@en

P2093

Daniel R Calerdon

http://www.w3.org/2001/XMLSchema#string

James E Marcin

http://www.w3.org/2001/XMLSchema#string

John A Faulkner

http://www.w3.org/2001/XMLSchema#string

P2860

Myostatin signals through a transforming growth factor beta-like signaling pathway to block adipogenesis

Myostatin mutation associated with gross muscle hypertrophy in a child

Regulation of myostatin activity and muscle growth

Myostatin negatively regulates satellite cell activation and self-renewal

Analysis of Relative Gene Expression Data Using Real-Time Quantitative PCR and the 2−ΔΔCT Method

Regulation of skeletal muscle mass in mice by a new TGF-beta superfamily member

Mutations in myostatin (GDF8) in double-muscled Belgian Blue and Piedmontese cattle

Short-term endurance training results in a muscle-specific decrease of myostatin mRNA content in the rat

Myostatin levels in regenerating rat muscles and in myogenic cell cultures

Myostatin inhibits cell proliferation and protein synthesis in C2C12 muscle cells.

P304

898-905

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1152/JAPPLPHYSIOL.00126.2006

http://www.w3.org/2001/XMLSchema#string

P407

P433

3

http://www.w3.org/2001/XMLSchema#string

P478

101

http://www.w3.org/2001/XMLSchema#string

P50

Christopher L. Mendias

P577

2006-05-18T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

7071409

http://www.w3.org/2001/XMLSchema#string

P698

16709649

http://www.w3.org/2001/XMLSchema#string

P932

4088255

http://www.w3.org/2001/XMLSchema#string