About: Various Jobs of Proteolytic Enzymes in Skeletal Muscle during Unloading: Facts and Speculations

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An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Various Jobs of Proteolytic Enzymes in Skeletal Muscle during Unloading: Facts and Speculations
Creator	Kachaeva, E Shenkman, B
Source	Medline; PMC
abstract	Skeletal muscles, namely, postural muscles, as soleus, suffer from atrophy under disuse. Muscle atrophy development caused by unloading differs from that induced by denervation or other stimuli. Disuse atrophy is supposed to be the result of shift of protein synthesis/proteolysis balance towards protein degradation increase. Maintaining of the balance involves many systems of synthesis and proteolysis, whose activation leads to muscle adaptation to disuse rather than muscle degeneration. Here, we review recent data on activity of signaling systems involved in muscle atrophy development under unloading and muscle adaptation to the lack of support.
has issue date	2012-02-08(xsd:dateTime)
bibo:doi	10.1155/2012/493618
bibo:pmid	22496611
has license	no-cc
sha1sum (hex)	1fc9112680d92bbd17a4837986679f7c26bf638b
schema:url	https://doi.org/10.1155/2012/493618
resource representing a document's title	Various Jobs of Proteolytic Enzymes in Skeletal Muscle during Unloading: Facts and Speculations
has PubMed Central identifier	PMC3303694
has PubMed identifier	22496611
schema:publication	J Biomed Biotechnol
resource representing a document's body	covid:1fc9112680d92bbd17a4837986679f7c26bf638b#body_text
is schema:about of	named entity 'PROTEOLYSIS' named entity 'SYNTHESIS' named entity 'UNLOADING' named entity 'BALANCE' named entity 'SKELETAL MUSCLES' named entity 'INCREASE' named entity 'SUFFER' named entity 'RESULT' named entity 'DENERVATION' named entity 'signaling systems' named entity 'Muscle atrophy' named entity 'systems' named entity 'muscle degeneration' named entity 'protein degradation' named entity 'protein synthesis' named entity 'Proteolytic Enzymes' named entity 'involved' named entity 'Akt' named entity 'ligase' named entity 'FoxO' named entity 'cachexia' named entity 'M-line' named entity 'UPS' named entity 'skeletal muscle' named entity 'IkB' named entity 'F-box' named entity 'sarcoplasmic reticulum' named entity 'protein' named entity 'FoxO' named entity 'molecule' named entity 'anabolic steroids' named entity 'proteolytic activity' named entity 'IGF-1' named entity 'proteolysis' named entity 'cathepsin' named entity 'mTOR' named entity 'muscle atrophy' named entity 'molecule' named entity 'caspase' named entity 'hindlimb' named entity 'calpains' named entity 'dephosphorylation' named entity 'calcium' named entity 'molecule' named entity 'interact' named entity 'eukaryotic' named entity 'caffeine' named entity 'E3 ubiquitin ligases' named entity 'myosin heavy chain' named entity 'molecule' named entity 'ubiquitin ligase' named entity 'posttranslational modifications' named entity 'myosin' named entity 'muscle cells' named entity 'terminal differentiation' named entity 'soleus' named entity 'titin' named entity 'vastus lateralis' named entity 'Akt' named entity 'transcription' named entity 'eIF3' named entity 'lysosomal' named entity 'IkB' named entity 'eIF3' named entity 'peptides' named entity 'eIF3' named entity 'NFkB' named entity 'Akt' named entity 'cytokine' named entity 'fatigue' named entity 'titin' named entity 'protein' named entity 'titin' named entity 'titin' named entity 'dephosphorylation' named entity 'yeasts' named entity 'c-fos' named entity 'TNFα' named entity 'lipid peroxidation' named entity 'atrophy'

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