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Search results 301 to 345 out of 345 for Aqp9

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0.011s

Type

Details

Score

Allele

Eif2b5<toy> | MGI:6780197

Name:	eukaryotic translation initiation factor 2B, subunit 5 epsilon; toy
Allele Type:	Spontaneous
Attribute String:	Not Specified

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Publication

31587290 | J:297496

First Author:	Terumitsu-Tsujita M
Year:	2020
Journal:	J Neurochem
Title:	Glial pathology in a novel spontaneous mutant mouse of the Eif2b5 gene: a vanishing white matter disease model.
Volume:	154
Issue:	1
Pages:	25-40

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Strain

MGI:6353617 | C3H.Cg-Eif2b5<toy>/Rbrc

Attribute String:

congenic, mutant strain, spontaneous mutation

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Strain

MGI:6353276 | B6.Cg-Eif2b5<toy>/Rbrc

Attribute String:

congenic, mutant strain, spontaneous mutation

•

HT Experiment

E-MTAB-5849 | Microarray expression analysis of Aquaporin-9 (AQP9) knockout effect in fasted C57Bl/6 mice


Experiment Type:	transcription profiling by array
Study Type:	WT vs. Mutant
Source:	ArrayExpress

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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.

•

Publication

18606867 | J:140244

First Author:	Okada S
Year:	2008
Journal:	FASEB J
Title:	Aquaporin-11 knockout mice and polycystic kidney disease animals share a common mechanism of cyst formation.
Volume:	22
Issue:	10
Pages:	3672-84

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Protein Domain

IPR023266 | Aquaporin_11

Type:

Family

Description:

The aquaporins (AQPs) are a family of integral membrane proteins composed of two subfamilies: the orthodox aquaporins, which transport only water, and the aquaglyceroporins, which transport glycerol, urea, or other small solutes []. AQP1 in pleural mesothelial cells participate in the formation of pleural fluid [], renal AQP2 is involved in levels of solutes []and changes in AQP9 in the hippocampus are related to delayed neuronal death []. Aquaporins contain two tandem repeats, each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA).Aquaporin-11 (AQP11) and aquaporin-12 belong to a new aquaporin subfamily termed superaquaporins []. AQP11 is found in the endoplasmic reticulum and has been connected to policystic kidney disease through knock-out experiments []. It has also been shown that although the characteristic NPA motif may not be fully conserved in both tandem repeats, the molecule nevertheless preserves its water-transport function [].

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Publication

17178102 | J:188552

First Author:	Yakata K
Year:	2007
Journal:	Biochim Biophys Acta
Title:	Aquaporin-11 containing a divergent NPA motif has normal water channel activity.
Volume:	1768
Issue:	3
Pages:	688-93

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Publication

19096782 | -

First Author:	Ishibashi K
Year:	2009
Journal:	Handb Exp Pharmacol
Title:	New members of mammalian aquaporins: AQP10-AQP12.

Issue:	190
Pages:	251-62

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Publication

9733774 | J:69559

First Author:	Tsukaguchi H
Year:	1998
Journal:	J Biol Chem
Title:	Molecular characterization of a broad selectivity neutral solute channel.
Volume:	273
Issue:	38
Pages:	24737-43

•

Publication

18067818 | -

First Author:	Zhang W
Year:	2007
Journal:	Zhonghua Yi Xue Za Zhi
Title:	[Effect of hypertonic medium on expression of aquaporin-1 in pleural mesothelial cells: experiment with rats].
Volume:	87
Issue:	35
Pages:	2508-11

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Publication

18419953 | -

First Author:	Wang Y
Year:	2008
Journal:	Zhongguo Wei Zhong Bing Ji Jiu Yi Xue
Title:	[Expression of renal aquaporin 2 after circulatory arrest].
Volume:	20
Issue:	4
Pages:	210-3

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Publication

17526024 | -

First Author:	Hwang IK
Year:	2007
Journal:	J Neurosci Res
Title:	Aquaporin 9 changes in pyramidal cells before and is expressed in astrocytes after delayed neuronal death in the ischemic hippocampal CA1 region of the gerbil.
Volume:	85
Issue:	11
Pages:	2470-9

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Publication

15809071 | J:97446

First Author:	Itoh T
Year:	2005
Journal:	Biochem Biophys Res Commun
Title:	Identification of a novel aquaporin, AQP12, expressed in pancreatic acinar cells.
Volume:	330
Issue:	3
Pages:	832-8

•

Protein Domain

IPR016697 | Aquaporin_11/12

Type:

Family

Description:

The aquaporins (AQPs) are a family of integral membrane proteins composed of two subfamilies: the orthodox aquaporins, which transport only water, and the aquaglyceroporins, which transport glycerol, urea, or other small solutes []. AQP1 in pleural mesothelial cells participate in the formation of pleural fluid [], renal AQP2 is involved in levels of solutes []and changes in AQP9 in the hippocampus are related to delayed neuronal death []. Aquaporins contain two tandem repeats, each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA).Aquaporins 11 and 12 are classified as members of a new AQP subfamily: the subcellular AQPs []. AQP 11 and 12 appear to be more distantly related to the other mammalian aquaporins and aquaglyceroporins. AQP11 is functionally distinct from other proteins of the aquaporin superfamily and could represent a new aquaporin subfamily []. In members of the subcellular AQPs, one of the two asparagine-proline-alanine (NPA) motifs are not completely conserved. They play a crucial role in selective water conduction and function as water channels []. This group represents an aquaporin types 11 and 12.

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Protein Domain

IPR023265 | Aquaporin_12

Type:

Family

Description:

The aquaporins (AQPs) are a family of integral membrane proteins composed of two subfamilies: the orthodox aquaporins, which transport only water, and the aquaglyceroporins, which transport glycerol, urea, or other small solutes []. AQP1 in pleural mesothelial cells participate in the formation of pleural fluid [], renal AQP2 is involved in levels of solutes []and changes in AQP9 in the hippocampus are related to delayed neuronal death []. Aquaporins contain two tandem repeats, each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA).Aquaporin-11 and aquaporin-12 (AQP12) belong to a new aquaporin subfamily termed superaquaporins []. AQP12 is exclusively found in pancreatic acinar cells [], and is not localised in the plasma membrane. No specific localisation has yet been established for this subfamily, but its presence in the pancreas implies some role in the secretion of digestive enzymes []and fluids in the pancreatic cells []. A structural characteristic of AQP12 is the lack of a cytoplasmic N-terminal region, by contrast with all other known aquaporins.

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Publication

17257750 | J:123606

First Author:	Shields SD
Year:	2007
Journal:	Pain
Title:	Anatomical and functional analysis of aquaporin 1, a water channel in primary afferent neurons.
Volume:	131
Issue:	1-2
Pages:	8-20

•

Publication

23850520 | J:315508

First Author:	Blomberg Jensen M
Year:	2013
Journal:	Mol Cell Endocrinol
Title:	Characterization of the testicular, epididymal and endocrine phenotypes in the Leuven Vdr-deficient mouse model: targeting estrogen signalling.
Volume:	377
Issue:	1-2
Pages:	93-102

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Publication

18829704 | J:145790

First Author:	Yeung CH
Year:	2009
Journal:	Biol Reprod
Title:	Aquaporin isoforms involved in physiological volume regulation of murine spermatozoa.
Volume:	80
Issue:	2
Pages:	350-7

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Publication

15003543 | J:88614

First Author:	Felszeghy S
Year:	2004
Journal:	Arch Oral Biol
Title:	Expression of aquaporin isoforms during human and mouse tooth development.
Volume:	49
Issue:	4
Pages:	247-57

•

Publication

19429018 | J:161881

First Author:	Ding JY
Year:	2009
Journal:	Neurosci Lett
Title:	Hypoxia-inducible factor-1alpha signaling in aquaporin upregulation after traumatic brain injury.
Volume:	453
Issue:	1
Pages:	68-72

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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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Protein

Q9JJJ3

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

•

Publication

33529207 | J:302275

First Author:	Kimball E
Year:	2021
Journal:	PLoS One
Title:	The role of aquaporin-4 in optic nerve head astrocytes in experimental glaucoma.
Volume:	16
Issue:	2
Pages:	e0244123

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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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Protein

Q8BYF0

Organism:	Mus musculus/domesticus
Length:	225
Fragment?:	true

•

Protein

A0A0X1KG63

Organism:	Mus musculus/domesticus
Length:	216
Fragment?:	true

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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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Protein

Q8BHH1

Organism:	Mus musculus/domesticus
Length:	271
Fragment?:	false

•

Protein

Q8CHJ2

Organism:	Mus musculus/domesticus
Length:	290
Fragment?:	false

•

Protein

Q3V2I1

Organism:	Mus musculus/domesticus
Length:	289
Fragment?:	false

•

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

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

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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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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Publication

15489334 | -

First Author:	Gerhard DS
Year:	2004
Journal:	Genome Res
Title:	The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Volume:	14
Issue:	10B
Pages:	2121-7

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MouseMine is a collaboration between MGI at The Jackson Laboratory and the InterMine project at the Cambridge Systems Biology Centre. MouseMine is funded through a grant from the NIH/NHGRI.The Jackson Laboratory makes no representation about the suitability or accuracy of this software or data for any purpose, and makes no warranties, either express or implied, including merchantability and fitness for a particular purpose or that the use of this software or data will not infringe any third party patents, copyrights, trademarks, or other rights. the software and data are provided "as is". This software and data are provided to enhance knowledge and encourage progress in the scientific community and are to be used only for research and educational purposes. Any reproduction or use for commercial purpose is prohibited without the prior express written permission of the Jackson Laboratory.

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