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Search results 501 to 529 out of 529 for Aqp3

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0.018s

Type

Details

Score

Publication

23593143 | J:200038

First Author:	Bell CE
Year:	2013
Journal:	PLoS One
Title:	p38 MAPK regulates cavitation and tight junction function in the mouse blastocyst.
Volume:	8
Issue:	4
Pages:	e59528

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Publication

24236206 | J:209312

First Author:	Qin H
Year:	2013
Journal:	PLoS One
Title:	The caveolin-1 scaffolding domain peptide decreases phosphatidylglycerol levels and inhibits calcium-induced differentiation in mouse keratinocytes.
Volume:	8
Issue:	11
Pages:	e80946

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Publication

30862673 | J:277895

First Author:	Sonntag Y
Year:	2019
Journal:	J Biol Chem
Title:	Identification and characterization of potent and selective aquaporin-3 and aquaporin-7 inhibitors.
Volume:	294
Issue:	18
Pages:	7377-7387

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Publication

31649296 | J:284633

First Author:	Soler DC
Year:	2019
Journal:	Sci Rep
Title:	An uncharacterized region within the N-terminus of mouse TMC1 precludes trafficking to plasma membrane in a heterologous cell line.
Volume:	9
Issue:	1
Pages:	15263

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Protein

Q8R2N1

Organism:	Mus musculus/domesticus
Length:	292
Fragment?:	false

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Publication

9514918 | -

First Author:	Ishibashi K
Year:	1998
Journal:	Biochem Biophys Res Commun
Title:	Cloning and functional expression of a new aquaporin (AQP9) abundantly expressed in the peripheral leukocytes permeable to water and urea, but not to glycerol.
Volume:	244
Issue:	1
Pages:	268-74

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Publication

12594337 | -

First Author:	Carbrey JM
Year:	2003
Journal:	Proc Natl Acad Sci U S A
Title:	Aquaglyceroporin AQP9: solute permeation and metabolic control of expression in liver.
Volume:	100
Issue:	5
Pages:	2945-50

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Publication

30420639 | -

First Author:	Gotfryd K
Year:	2018
Journal:	Nat Commun
Title:	Human adipose glycerol flux is regulated by a pH gate in AQP10.
Volume:	9
Issue:	1
Pages:	4749

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Protein Domain

IPR015685 | Aquaporin_9

Type:

Family

Description:

Aquaporins are water channels, present in both higher and lower organisms, that belong to the major intrinsic protein family. Most aquaporins are highly selective for water, though some also facilitate the movement of small uncharged molecules such as glycerol []. In higher eukaryotes these proteins play diverse roles in the maintenance of water homeostasis, indicating that membrane water permeability can be regulated independently of solute permeability. In microorganisms however, many of which do not contain aquaporins, they do not appear to play such a broad role. Instead, they assist specific microbial lifestyles within the environment, e.g. they confer protection against freeze-thaw stress and may help maintain water permeability at low temperatures []. The regulation of aquaporins is complex, including transcriptional, post-translational, protein-trafficking and channel-gating mechanisms that are frequently distinct for each family member.Structural studies show that aquaporins are present in the membrane as tetramers, though each monomer contains its own channel [, , ]. The monomer has an overall "hourglass"structure made up of three structural elements: an external vestibule, an internal vestibule, and an extended pore which connects the two vestibules. Substrate selectivity is conferred by two mechanisms. Firstly, the diameter of the pore physically limits the size of molecules that can pass through the channel. Secondly, specific amino acids within the molecule regulate the preference for hydrophobic or hydrophilic substrates.Aquaporins are classified into two subgroups: the aquaporins (also known as orthodox aquaporins), which transport only water, and the aquaglyceroporins, which transport glycerol, urea, and other small solutes in addition to water [, ].Aquaporin-9 was identified from human leukocytes by homology cloning []. AQP9 has unusually broad solute permeability. It is expressed in hepatocyte plasma membranes and also in lung, small intestine and spleen cells []. Expression of AQP9 in liver was induced up to 20-fold in rats fasted for 24 to 96 hours, and the AQP9 level gradually declined after re-feeding []. AQP9 shares greater sequence identity with AQP3 and AQP7 than with other members of the family, suggesting that these 3 proteins belong to a subfamily.

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Publication

21880835 | J:180040

First Author:	Nørregaard R
Year:	2011
Journal:	Am J Physiol Renal Physiol
Title:	COX-2 disruption leads to increased central vasopressin stores and impaired urine concentrating ability in mice.
Volume:	301
Issue:	6
Pages:	F1303-13

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Publication

15713911 | J:98932

First Author:	Morris RG
Year:	2005
Journal:	Am J Physiol Renal Physiol
Title:	Altered expression profile of transporters in the inner medullary collecting duct of aquaporin-1 knockout mice.
Volume:	289
Issue:	1
Pages:	F194-9

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Publication

18434389 | J:148646

First Author:	Wang W
Year:	2008
Journal:	Am J Physiol Renal Physiol
Title:	Role of AQP1 in endotoxemia-induced acute kidney injury.
Volume:	294
Issue:	6
Pages:	F1473-80

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Publication

23359673 | J:208102

First Author:	Kortenoeven ML
Year:	2013
Journal:	J Physiol
Title:	Genetic ablation of aquaporin-2 in the mouse connecting tubules results in defective renal water handling.
Volume:	591
Issue:	8
Pages:	2205-19

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Publication

18718702 | J:173745

First Author:	Rubenwolf PC
Year:	2009
Journal:	Eur Urol
Title:	Expression and localisation of aquaporin water channels in human urothelium in situ and in vitro.
Volume:	56
Issue:	6
Pages:	1013-23

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Publication

9124401 | J:38826

First Author:	Ishibashi K
Year:	1997
Journal:	Am J Physiol
Title:	Immunolocalization and effect of dehydration on AQP3, a basolateral water channel of kidney collecting ducts.
Volume:	272
Issue:	2 Pt 2
Pages:	F235-41

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Publication

9950948 | J:53124

First Author:	Frøkiaer J
Year:	1999
Journal:	Am J Physiol
Title:	Low aquaporin-2 levels in polyuric DI +/+ severe mice with constitutively high cAMP-phosphodiesterase activity.
Volume:	276
Issue:	2 Pt 2
Pages:	F179-90

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Publication

17576812 | J:125011

First Author:	Matsumura K
Year:	2007
Journal:	Mol Cell Biol
Title:	Aquaporin 7 is a beta-cell protein and regulator of intraislet glycerol content and glycerol kinase activity, beta-cell mass, and insulin production and secretion.
Volume:	27
Issue:	17
Pages:	6026-37

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Publication

15377788 | -

First Author:	Harries WE
Year:	2004
Journal:	Proc Natl Acad Sci U S A
Title:	The channel architecture of aquaporin 0 at a 2.2-A resolution.
Volume:	101
Issue:	39
Pages:	14045-50

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Publication

15340377 | -

First Author:	King LS
Year:	2004
Journal:	Nat Rev Mol Cell Biol
Title:	From structure to disease: the evolving tale of aquaporin biology.
Volume:	5
Issue:	9
Pages:	687-98

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Publication

16406529 | -

First Author:	Tanghe A
Year:	2006
Journal:	Trends Microbiol
Title:	Why do microorganisms have aquaporins?
Volume:	14
Issue:	2
Pages:	78-85

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Publication

14691544 | -

First Author:	Savage DF
Year:	2003
Journal:	PLoS Biol
Title:	Architecture and selectivity in aquaporins: 2.5 a X-ray structure of aquaporin Z.
Volume:	1
Issue:	3
Pages:	E72

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Publication

16650285 | -

First Author:	Gorelick DA
Year:	2006
Journal:	BMC Biochem
Title:	Aquaporin-11: a channel protein lacking apparent transport function expressed in brain.
Volume:	7

Pages:	14

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Publication

10872456 | -

First Author:	Borgnia M
Year:	1999
Journal:	Annu Rev Biochem
Title:	Cellular and molecular biology of the aquaporin water channels.
Volume:	68

Pages:	425-58

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Protein

Q9JJJ3

Organism:	Mus musculus/domesticus
Length:	295
Fragment?:	false

•

Protein

Q4FK77

Organism:	Mus musculus/domesticus
Length:	295
Fragment?:	false

•

Protein

E9Q8P3

Organism:	Mus musculus/domesticus
Length:	192
Fragment?:	false

•

Protein

D3YYD6

Organism:	Mus musculus/domesticus
Length:	321
Fragment?:	false

•

Protein

Q8R1T7

Organism:	Mus musculus/domesticus
Length:	192
Fragment?:	false

•

Publication

11780053 | -

First Author:	Sui H
Year:	2001
Journal:	Nature
Title:	Structural basis of water-specific transport through the AQP1 water channel.
Volume:	414
Issue:	6866
Pages:	872-8

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