Journal•ISSN: 1548-9221
Physiology
American Physiological Society
About: Physiology is an academic journal. The journal publishes majorly in the area(s): Skeletal muscle & Ion channel. It has an ISSN identifier of 1548-9221. Over the lifetime, 1848 publications have been published receiving 90754 citations.
Topics: Skeletal muscle, Ion channel, Receptor, Kidney, Blood pressure
Papers published on a yearly basis
Papers
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TL;DR: 2D and 3D cell culture methods are reviewed, advantages and limitations of these techniques in modeling physiologically and pathologically relevant processes are discussed, and directions for future research are suggested.
Abstract: Cell culture has become an indispensable tool to help uncover fundamental biophysical and biomolecular mechanisms by which cells assemble into tissues and organs, how these tissues function, and how that function becomes disrupted in disease. Cell culture is now widely used in biomedical research, tissue engineering, regenerative medicine, and industrial practices. Although flat, two-dimensional (2D) cell culture has predominated, recent research has shifted toward culture using three-dimensional (3D) structures, and more realistic biochemical and biomechanical microenvironments. Nevertheless, in 3D cell culture, many challenges remain, including the tissue-tissue interface, the mechanical microenvironment, and the spatiotemporal distributions of oxygen, nutrients, and metabolic wastes. Here, we review 2D and 3D cell culture methods, discuss advantages and limitations of these techniques in modeling physiologically and pathologically relevant processes, and suggest directions for future research.
1,048 citations
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TL;DR: The discovery of the transcription factor HIF-1 has led to the identification of protein hydroxylation as a mechanism by which changes in PO2 are transduced to effect changes in gene expression.
Abstract: The ability to sense and respond to changes in oxygenation represents a fundamental property of all metazoan cells. The discovery of the transcription factor HIF-1 has led to the identification of protein hydroxylation as a mechanism by which changes in Po2 are transduced to effect changes in gene expression.
874 citations
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TL;DR: Hypoxia-inducible factor 1 (HIF-1) mediates adaptive responses to hypoxia, including erythropoiesis, angiogenesis, and metabolic reprogramming, and mediates maladaptive responses to chronic continuous and intermittent hypoxIA, which underlie the development of pulmonary and systemic hypertension.
Abstract: Metazoan organisms are dependent on a continuous supply of O2 for survival. Hypoxia-inducible factor 1 (HIF-1) is a transcription factor that regulates oxygen homeostasis and plays key roles in dev...
821 citations
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TL;DR: Understanding the signaling that regulates muscle mass may provide potential therapeutic targets for the prevention and treatment of muscle wasting in metabolic and neuromuscular diseases.
Abstract: Muscle performance is influenced by turnover of contractile proteins. Production of new myofibrils and degradation of existing proteins is a delicate balance, which, depending on the condition, can promote muscle growth or loss. Protein synthesis and protein degradation are coordinately regulated by pathways that are influenced by mechanical stress, physical activity, availability of nutrients, and growth factors. Understanding the signaling that regulates muscle mass may provide potential therapeutic targets for the prevention and treatment of muscle wasting in metabolic and neuromuscular diseases.
777 citations
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TL;DR: Signaling through mammalian target of rapamycin (mTOR) is activated by amino acids, insulin, and growth factors, and impaired by nutrient or energy deficiency.
Abstract: Signaling through mammalian target of rapamycin (mTOR) is activated by amino acids, insulin, and growth factors, and impaired by nutrient or energy deficiency. mTOR plays key roles in cell physiology. mTOR regulates numerous components involved in protein synthesis, including initiation and elongation factors, and the biogenesis of ribosomes themselves.
683 citations