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Titlebook: Urea Transporters; Baoxue Yang,Jeff M. Sands Book 2014 Springer Science+Business Media Dordrecht 2014 Membrane channel.Transporter protein

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發(fā)表于 2025-3-21 19:12:45 | 只看該作者 |倒序瀏覽 |閱讀模式
書目名稱Urea Transporters
編輯Baoxue Yang,Jeff M. Sands
視頻videohttp://file.papertrans.cn/945/944194/944194.mp4
概述Covers research advances in the study of urea transporter over the past 20 years.Provides a systematic and comprehensive insight into urea transporters.Introduces clinical and pharmaceutical aspects o
叢書名稱Subcellular Biochemistry
圖書封面Titlebook: Urea Transporters;  Baoxue Yang,Jeff M. Sands Book 2014 Springer Science+Business Media Dordrecht 2014 Membrane channel.Transporter protein
描述The mechanisms and physiological functions of urea transporters across biological membranes are subjects of long-standing interests. Although urea represents roughly 40% of all urinary solutes in normal human urine, the handling of urea in the tissues has been largely neglected in the past and few clinical or experimental studies now report data on urea. Most recent physiological text books include chapters on water and electrolyte physiology but no chapter on urea. Our aim in writing this book is to stimulate further research in new directions by providing novel and provocative insights into the further mechanisms and physiological significance of urea metabolism and transport in mammals. This book offers a state-of-the-art report on recent discoveries concerning urea transport and where the field is going. It mainly focuses on advances made over the past 20 years on the biophysics, genetics, protein structure, molecular biology, physiology, pathophysiology and pharmacology of urea transport in mammalian cell membranes. It will help graduate students and researchers to get an overall picture of mammalian urea transporters and may also yield benefits for pharmaceutical companies wi
出版日期Book 2014
關(guān)鍵詞Membrane channel; Transporter protein; Urea; Urea transporter; Urine concentration
版次1
doihttps://doi.org/10.1007/978-94-017-9343-8
isbn_softcover978-94-024-0227-8
isbn_ebook978-94-017-9343-8Series ISSN 0306-0225 Series E-ISSN 2542-8810
issn_series 0306-0225
copyrightSpringer Science+Business Media Dordrecht 2014
The information of publication is updating

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發(fā)表于 2025-3-22 00:06:00 | 只看該作者
Urea Transporters978-94-017-9343-8Series ISSN 0306-0225 Series E-ISSN 2542-8810
板凳
發(fā)表于 2025-3-22 01:19:04 | 只看該作者
Subcellular Biochemistryhttp://image.papertrans.cn/u/image/944194.jpg
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發(fā)表于 2025-3-22 05:26:30 | 只看該作者
https://doi.org/10.1007/978-94-017-9343-8Membrane channel; Transporter protein; Urea; Urea transporter; Urine concentration
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發(fā)表于 2025-3-22 09:50:57 | 只看該作者
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發(fā)表于 2025-3-22 16:10:35 | 只看該作者
0306-0225 ransporters.Introduces clinical and pharmaceutical aspects oThe mechanisms and physiological functions of urea transporters across biological membranes are subjects of long-standing interests. Although urea represents roughly 40% of all urinary solutes in normal human urine, the handling of urea in
7#
發(fā)表于 2025-3-22 17:20:55 | 只看該作者
Mathematical Modeling of Urea Transport in the Kidney,ly structured organization of tubules and vessels in the renal medulla on urea sequestration and cycling. The goal of this article is to show how physiological problems can be formulated and studied mathematically, and how such models may provide insights into renal functions.
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發(fā)表于 2025-3-22 22:01:51 | 只看該作者
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發(fā)表于 2025-3-23 02:12:52 | 只看該作者
Small-Molecule Inhibitors of Urea Transporters,n identified with different UT-A versus UT-B selectivity profiles and putative binding sites on UT proteins. Studies in rodent models support the utility of UT inhibitors in reducing urinary concentration, though testing in clinically relevant animal models of edema has not yet been done.
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發(fā)表于 2025-3-23 08:01:55 | 只看該作者
Structure of Urea Transporters,he pore, combined with crystal structures of ligand-bound proteins, molecular dynamics simulations, and functional data on permeation and inhibition by a broad range of urea analogs and other small molecules, provides insight into the structural basis of urea permeation and selectivity.
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