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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Rh-associated glycoprotein''' ('''RHAG''') is an [[ammonia transporter]] [[protein]] that in humans is encoded by the ''RHAG'' [[gene]].<ref name="pmid9479501">{{cite journal | vauthors = Matassi G, Chérif-Zahar B, Raynal V, Rouger P, Cartron JP | title = Organization of the human RH50A gene (RHAG) and evolution of base composition of the RH gene family | journal = Genomics | volume = 47 | issue = 2 | pages = 286–93 | date = Jan 1998 | pmid = 9479501 | pmc =  | doi = 10.1006/geno.1997.5112 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: RHAG Rh-associated glycoprotein| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6005| accessdate = }}</ref> RHAG has also recently been designated '''CD241''' ([[cluster of differentiation]] 241). Mutations in the RHAG gene can cause [[Hereditary stomatocytosis|stomatocytosis]].<ref>{{cite journal | vauthors = Stewart AK, Shmukler BE, Vandorpe DH, Rivera A, Heneghan JF, Li X, Hsu A, Karpatkin M, O'Neill AF, Bauer DE, Heeney MM, John K, Kuypers FA, Gallagher PG, Lux SE, Brugnara C, Westhoff CM, Alper SL | title = Loss-of-function and gain-of-function phenotypes of stomatocytosis mutant RhAG F65S | journal = American Journal of Physiology. Cell Physiology | volume = 301 | issue = 6 | pages = C1325-43 | date = Dec 2011 | pmid = 21849667 | pmc = 3233792 | doi = 10.1152/ajpcell.00054.2011 }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Rh-associated glycoprotein
| HGNCid = 10006
| Symbol = RHAG
| AltSymbols =; CD241; RH2; RH50A; Rh50; Rh50 GP
| OMIM = 180297
| ECnumber = 
| Homologene = 68045
| MGIid = 1202713
| GeneAtlas_image1 = PBB_GE_RHAG_206145_at_tn.png
| GeneAtlas_image2 = PBB_GE_RHAG_206146_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_RHAG_211254_x_at_tn.png
| Function = {{GNF_GO|id=GO:0008519 |text = ammonium transmembrane transporter activity}} {{GNF_GO|id=GO:0030506 |text = ankyrin binding}}
| Component = {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}}
| Process = {{GNF_GO|id=GO:0006461 |text = protein complex assembly}} {{GNF_GO|id=GO:0006810 |text = transport}} {{GNF_GO|id=GO:0006873 |text = cell ion homeostasis}} {{GNF_GO|id=GO:0015696 |text = ammonium transport}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 6005
    | Hs_Ensembl = ENSG00000112077
    | Hs_RefseqProtein = NP_000315
    | Hs_RefseqmRNA = NM_000324
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 6
    | Hs_GenLoc_start = 49680830
    | Hs_GenLoc_end = 49712511
    | Hs_Uniprot = Q02094
    | Mm_EntrezGene = 19743
    | Mm_Ensembl = ENSMUSG00000023926
    | Mm_RefseqmRNA = NM_011269
    | Mm_RefseqProtein = NP_035399
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 17
    | Mm_GenLoc_start = 40274633
    | Mm_GenLoc_end = 40304238
    | Mm_Uniprot = 
  }}
}}
'''Rh-associated glycoprotein''', also known as '''RHAG''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: RHAG Rh-associated glycoprotein| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6005| accessdate = }}</ref> RHAG has also recently been designated '''CD241''' ([[cluster of differentiation]] 241).


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
The [[Rh blood group system|Rh blood group]] antigens (MIM 111700) are associated with human erythrocyte membrane proteins of approximately 30 kD, the so-called Rh30 polypeptides. Heterogeneously glycosylated membrane proteins of 50 and 45 kD, the Rh50 glycoproteins, are coprecipitated with the Rh30 polypeptides on immunoprecipitation with anti-Rh-specific mono- and polyclonal antibodies. The Rh antigens appear to exist as a multisubunit complex of CD47 (MIM 601028), LW (MIM 111250), glycophorin B (MIM 111740), and play a critical role in the Rh50 glycoprotein [supplied by OMIM].<ref name="entrez" />
{{PBB_Summary
| section_title =
| summary_text = The Rh blood group antigens (MIM 111700) are associated with human erythrocyte membrane proteins of approximately 30 kD, the so-called Rh30 polypeptides. Heterogeneously glycosylated membrane proteins of 50 and 45 kD, the Rh50 glycoproteins, are coprecipitated with the Rh30 polypeptides on immunoprecipitation with anti-Rh-specific mono- and polyclonal antibodies. The Rh antigens appear to exist as a multisubunit complex of CD47 (MIM 601028), LW (MIM 111250), glycophorin B (MIM 111740), and play a critical role in the Rh50 glycoprotein.[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: RHAG Rh-associated glycoprotein| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6005| accessdate = }}</ref>
}}


==References==
== Interactions ==
{{reflist|2}}


==Further reading==
RHAG has been shown to [[Protein-protein interaction|interact]] with [[ANK1]].<ref name=pmid12719424>{{cite journal | vauthors = Nicolas V, Le Van Kim C, Gane P, Birkenmeier C, Cartron JP, Colin Y, Mouro-Chanteloup I | title = Rh-RhAG/ankyrin-R, a new interaction site between the membrane bilayer and the red cell skeleton, is impaired by Rh(null)-associated mutation | journal = The Journal of Biological Chemistry | volume = 278 | issue = 28 | pages = 25526–33 | date = Jul 2003 | pmid = 12719424 | doi = 10.1074/jbc.M302816200 }}</ref>
 
== See also ==
* [[Rh deficiency syndrome]]
 
== References ==
{{reflist}}
{{NLM content}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Bakouh N, Benjelloun F, Cherif-Zahar B, Planelles G | title = The challenge of understanding ammonium homeostasis and the role of the Rh glycoproteins | journal = Transfusion Clinique Et Biologique | volume = 13 | issue = 1-2 | pages = 139–46 | year = 2006 | pmid = 16564724 | doi = 10.1016/j.tracli.2006.02.008 }}
| citations =
* {{cite journal | vauthors = Ripoche P, Goossens D, Devuyst O, Gane P, Colin Y, Verkman AS, Cartron JP | title = Role of RhAG and AQP1 in NH3 and CO2 gas transport in red cell ghosts: a stopped-flow analysis | journal = Transfusion Clinique Et Biologique | volume = 13 | issue = 1-2 | pages = 117–22 | year = 2006 | pmid = 16574458 | doi = 10.1016/j.tracli.2006.03.004 }}
*{{cite journal | author=Bakouh N, Benjelloun F, Cherif-Zahar B, Planelles G |title=The challenge of understanding ammonium homeostasis and the role of the Rh glycoproteins. |journal=Transfusion clinique et biologique : journal de la Société française de transfusion sanguine |volume=13 |issue= 1-2 |pages= 139-46 |year= 2006 |pmid= 16564724 |doi= 10.1016/j.tracli.2006.02.008 }}
* {{cite journal | vauthors = Ridgwell K, Spurr NK, Laguda B, MacGeoch C, Avent ND, Tanner MJ | title = Isolation of cDNA clones for a 50 kDa glycoprotein of the human erythrocyte membrane associated with Rh (rhesus) blood-group antigen expression | journal = The Biochemical Journal | volume = 287 | issue =  1| pages = 223–8 | date = Oct 1992 | pmid = 1417776 | pmc = 1133147 | doi =  | series = 287 }}
*{{cite journal | author=Ripoche P, Goossens D, Devuyst O, ''et al.'' |title=Role of RhAG and AQP1 in NH3 and CO2 gas transport in red cell ghosts: a stopped-flow analysis. |journal=Transfusion clinique et biologique : journal de la Société française de transfusion sanguine |volume=13 |issue= 1-2 |pages= 117-22 |year= 2006 |pmid= 16574458 |doi= 10.1016/j.tracli.2006.03.004 }}
* {{cite journal | vauthors = Avent ND, Ridgwell K, Mawby WJ, Tanner MJ, Anstee DJ, Kumpel B | title = Protein-sequence studies on Rh-related polypeptides suggest the presence of at least two groups of proteins which associate in the human red-cell membrane | journal = The Biochemical Journal | volume = 256 | issue = 3 | pages = 1043–6 | date = Dec 1988 | pmid = 3146980 | pmc = 1135522 | doi =  10.1042/bj2561043}}
*{{cite journal | author=Ridgwell K, Spurr NK, Laguda B, ''et al.'' |title=Isolation of cDNA clones for a 50 kDa glycoprotein of the human erythrocyte membrane associated with Rh (rhesus) blood-group antigen expression. |journal=Biochem. J. |volume=287 ( Pt 1) |issue=  |pages= 223-8 |year= 1992 |pmid= 1417776 |doi=  }}
* {{cite journal | vauthors = Cherif-Zahar B, Raynal V, Gane P, Mattei MG, Bailly P, Gibbs B, Colin Y, Cartron JP | title = Candidate gene acting as a suppressor of the RH locus in most cases of Rh-deficiency | journal = Nature Genetics | volume = 12 | issue = 2 | pages = 168–73 | date = Feb 1996 | pmid = 8563755 | doi = 10.1038/ng0296-168 }}
*{{cite journal | author=Avent ND, Ridgwell K, Mawby WJ, ''et al.'' |title=Protein-sequence studies on Rh-related polypeptides suggest the presence of at least two groups of proteins which associate in the human red-cell membrane. |journal=Biochem. J. |volume=256 |issue= 3 |pages= 1043-6 |year= 1989 |pmid= 3146980 |doi=  }}
* {{cite journal | vauthors = Huang CH | title = The human Rh50 glycoprotein gene. Structural organization and associated splicing defect resulting in Rh(null) disease | journal = The Journal of Biological Chemistry | volume = 273 | issue = 4 | pages = 2207–13 | date = Jan 1998 | pmid = 9442063 | doi = 10.1074/jbc.273.4.2207 }}
*{{cite journal | author=Cherif-Zahar B, Raynal V, Gane P, ''et al.'' |title=Candidate gene acting as a suppressor of the RH locus in most cases of Rh-deficiency. |journal=Nat. Genet. |volume=12 |issue= 2 |pages= 168-73 |year= 1996 |pmid= 8563755 |doi= 10.1038/ng0296-168 }}
* {{cite journal | vauthors = Hyland CA, Chérif-Zahar B, Cowley N, Raynal V, Parkes J, Saul A, Cartron JP | title = A novel single missense mutation identified along the RH50 gene in a composite heterozygous Rhnull blood donor of the regulator type | journal = Blood | volume = 91 | issue = 4 | pages = 1458–63 | date = Feb 1998 | pmid = 9454778 | doi =  }}
*{{cite journal | author=Huang CH |title=The human Rh50 glycoprotein gene. Structural organization and associated splicing defect resulting in Rh(null) disease. |journal=J. Biol. Chem. |volume=273 |issue= 4 |pages= 2207-13 |year= 1998 |pmid= 9442063 |doi= }}
* {{cite journal | vauthors = Iwamoto S, Omi T, Yamasaki M, Okuda H, Kawano M, Kajii E | title = Identification of 5' flanking sequence of RH50 gene and the core region for erythroid-specific expression | journal = Biochemical and Biophysical Research Communications | volume = 243 | issue = 1 | pages = 233–40 | date = Feb 1998 | pmid = 9473510 | doi = 10.1006/bbrc.1997.8023 }}
*{{cite journal | author=Hyland CA, Chérif-Zahar B, Cowley N, ''et al.'' |title=A novel single missense mutation identified along the RH50 gene in a composite heterozygous Rhnull blood donor of the regulator type. |journal=Blood |volume=91 |issue= 4 |pages= 1458-63 |year= 1998 |pmid= 9454778 |doi=  }}
* {{cite journal | vauthors = Huang CH, Liu Z, Cheng G, Chen Y | title = Rh50 glycoprotein gene and rhnull disease: a silent splice donor is trans to a Gly279-->Glu missense mutation in the conserved transmembrane segment | journal = Blood | volume = 92 | issue = 5 | pages = 1776–84 | date = Sep 1998 | pmid = 9716608 | doi = }}
*{{cite journal | author=Iwamoto S, Omi T, Yamasaki M, ''et al.'' |title=Identification of 5' flanking sequence of RH50 gene and the core region for erythroid-specific expression. |journal=Biochem. Biophys. Res. Commun. |volume=243 |issue= 1 |pages= 233-40 |year= 1998 |pmid= 9473510 |doi= 10.1006/bbrc.1997.8023 }}
* {{cite journal | vauthors = Chérif-Zahar B, Matassi G, Raynal V, Gane P, Delaunay J, Arrizabalaga B, Cartron JP | title = Rh-deficiency of the regulator type caused by splicing mutations in the human RH50 gene | journal = Blood | volume = 92 | issue = 7 | pages = 2535–40 | date = Oct 1998 | pmid = 9746795 | doi =  }}
*{{cite journal | author=Matassi G, Chérif-Zahar B, Raynal V, ''et al.'' |title=Organization of the human RH50A gene (RHAG) and evolution of base composition of the RH gene family. |journal=Genomics |volume=47 |issue= 2 |pages= 286-93 |year= 1998 |pmid= 9479501 |doi= 10.1006/geno.1997.5112 }}
* {{cite journal | vauthors = Huang C, Cheng GJ, Reid ME, Chen Y | title = Rhmod syndrome: a family study of the translation-initiator mutation in the Rh50 glycoprotein gene | journal = American Journal of Human Genetics | volume = 64 | issue = 1 | pages = 108–17 | date = Jan 1999 | pmid = 9915949 | pmc = 1377708 | doi = 10.1086/302215 }}
*{{cite journal | author=Huang CH, Liu Z, Cheng G, Chen Y |title=Rh50 glycoprotein gene and rhnull disease: a silent splice donor is trans to a Gly279-->Glu missense mutation in the conserved transmembrane segment. |journal=Blood |volume=92 |issue= 5 |pages= 1776-84 |year= 1998 |pmid= 9716608 |doi=  }}
* {{cite journal | vauthors = Huang CH, Cheng G, Liu Z, Chen Y, Reid ME, Halverson G, Okubo Y | title = Molecular basis for Rh(null) syndrome: identification of three new missense mutations in the Rh50 glycoprotein gene | journal = American Journal of Hematology | volume = 62 | issue = 1 | pages = 25–32 | date = Sep 1999 | pmid = 10467273 | doi = 10.1002/(SICI)1096-8652(199909)62:1<25::AID-AJH5>3.0.CO;2-K }}
*{{cite journal | author=Chérif-Zahar B, Matassi G, Raynal V, ''et al.'' |title=Rh-deficiency of the regulator type caused by splicing mutations in the human RH50 gene. |journal=Blood |volume=92 |issue= 7 |pages= 2535-40 |year= 1998 |pmid= 9746795 |doi= }}
* {{cite journal | vauthors = Iwamoto S, Suganuma H, Kamesaki T, Omi T, Okuda H, Kajii E | title = Cloning and characterization of erythroid-specific DNase I-hypersensitive site in human rhesus-associated glycoprotein gene | journal = The Journal of Biological Chemistry | volume = 275 | issue = 35 | pages = 27324–31 | date = Sep 2000 | pmid = 10862620 | doi = 10.1074/jbc.M003297200 }}
*{{cite journal | author=Huang C, Cheng GJ, Reid ME, Chen Y |title=Rhmod syndrome: a family study of the translation-initiator mutation in the Rh50 glycoprotein gene. |journal=Am. J. Hum. Genet. |volume=64 |issue= 1 |pages= 108-17 |year= 1999 |pmid= 9915949 |doi= }}
* {{cite journal | vauthors = Marini AM, Matassi G, Raynal V, André B, Cartron JP, Chérif-Zahar B | title = The human Rhesus-associated RhAG protein and a kidney homologue promote ammonium transport in yeast | journal = Nature Genetics | volume = 26 | issue = 3 | pages = 341–4 | date = Nov 2000 | pmid = 11062476 | doi = 10.1038/81656 }}
*{{cite journal | author=Huang CH, Cheng G, Liu Z, ''et al.'' |title=Molecular basis for Rh(null) syndrome: identification of three new missense mutations in the Rh50 glycoprotein gene. |journal=Am. J. Hematol. |volume=62 |issue= 1 |pages= 25-32 |year= 1999 |pmid= 10467273 |doi= }}
* {{cite journal | vauthors = Westhoff CM, Ferreri-Jacobia M, Mak DO, Foskett JK | title = Identification of the erythrocyte Rh blood group glycoprotein as a mammalian ammonium transporter | journal = The Journal of Biological Chemistry | volume = 277 | issue = 15 | pages = 12499–502 | date = Apr 2002 | pmid = 11861637 | doi = 10.1074/jbc.C200060200 }}
*{{cite journal | author=Iwamoto S, Suganuma H, Kamesaki T, ''et al.'' |title=Cloning and characterization of erythroid-specific DNase I-hypersensitive site in human rhesus-associated glycoprotein gene. |journal=J. Biol. Chem. |volume=275 |issue= 35 |pages= 27324-31 |year= 2000 |pmid= 10862620 |doi= 10.1074/jbc.M003297200 }}
* {{cite journal | vauthors = Mouro-Chanteloup I, D'Ambrosio AM, Gane P, Le Van Kim C, Raynal V, Dhermy D, Cartron JP, Colin Y | title = Cell-surface expression of RhD blood group polypeptide is posttranscriptionally regulated by the RhAG glycoprotein | journal = Blood | volume = 100 | issue = 3 | pages = 1038–47 | date = Aug 2002 | pmid = 12130520 | doi = }}
*{{cite journal | author=Marini AM, Matassi G, Raynal V, ''et al.'' |title=The human Rhesus-associated RhAG protein and a kidney homologue promote ammonium transport in yeast. |journal=Nat. Genet. |volume=26 |issue= 3 |pages= 341-4 |year= 2000 |pmid= 11062476 |doi= 10.1038/81656 }}
* {{cite journal | vauthors = Chen BS, Xu ZX, Xu X, Cai Y, Han YL, Wang J, Xia SH, Hu H, Wei F, Wu M, Wang MR | title = RhCG is downregulated in oesophageal squamous cell carcinomas, but expressed in multiple squamous epithelia | journal = European Journal of Cancer | volume = 38 | issue = 14 | pages = 1927–36 | date = Sep 2002 | pmid = 12204676 | doi = 10.1016/S0959-8049(02)00190-9 }}
*{{cite journal | author=Westhoff CM, Ferreri-Jacobia M, Mak DO, Foskett JK |title=Identification of the erythrocyte Rh blood group glycoprotein as a mammalian ammonium transporter. |journal=J. Biol. Chem. |volume=277 |issue= 15 |pages= 12499-502 |year= 2002 |pmid= 11861637 |doi= 10.1074/jbc.C200060200 }}
* {{cite journal | vauthors = Dahl KN, Westhoff CM, Discher DE | title = Fractional attachment of CD47 (IAP) to the erythrocyte cytoskeleton and visual colocalization with Rh protein complexes | journal = Blood | volume = 101 | issue = 3 | pages = 1194–9 | date = Feb 2003 | pmid = 12393442 | doi = 10.1182/blood-2002-04-1187 }}
*{{cite journal | author=Mouro-Chanteloup I, D'Ambrosio AM, Gane P, ''et al.'' |title=Cell-surface expression of RhD blood group polypeptide is posttranscriptionally regulated by the RhAG glycoprotein. |journal=Blood |volume=100 |issue= 3 |pages= 1038-47 |year= 2002 |pmid= 12130520 |doi= }}
*{{cite journal | author=Chen BS, Xu ZX, Xu X, ''et al.'' |title=RhCG is downregulated in oesophageal squamous cell carcinomas, but expressed in multiple squamous epithelia. |journal=Eur. J. Cancer |volume=38 |issue= 14 |pages= 1927-36 |year= 2002 |pmid= 12204676 |doi= }}
*{{cite journal  | author=Dahl KN, Westhoff CM, Discher DE |title=Fractional attachment of CD47 (IAP) to the erythrocyte cytoskeleton and visual colocalization with Rh protein complexes. |journal=Blood |volume=101 |issue= 3 |pages= 1194-9 |year= 2003 |pmid= 12393442 |doi= 10.1182/blood-2002-04-1187 }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
}}
{{refend}}
{{refend}}


==External links==
== External links ==
* {{MeshName|RHCE+protein,+human}}
* {{MeshName|RHCE+protein,+human}}
* [https://www.ncbi.nlm.nih.gov/projects/gv/mhc/xslcgi.cgi?cmd=bgmut/systems_info&system=rhag RhAG blood group system] in the [[BGMUT]] blood group antigen gene mutation database


{{membrane-protein-stub}}
{{Transfusion medicine}}
{{NLM content}}
{{Clusters of differentiation}}
{{Clusters of differentiation}}
{{Membrane transport proteins}}
[[Category:Clusters of differentiation]]
[[Category:Clusters of differentiation]]
{{WikiDoc Sources}}
[[Category:Solute carrier family]]
 
 
{{membrane-protein-stub}}
[[Category:Blood antigen systems]]

Latest revision as of 14:23, 12 January 2018

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Rh-associated glycoprotein (RHAG) is an ammonia transporter protein that in humans is encoded by the RHAG gene.[1][2] RHAG has also recently been designated CD241 (cluster of differentiation 241). Mutations in the RHAG gene can cause stomatocytosis.[3]

Function

The Rh blood group antigens (MIM 111700) are associated with human erythrocyte membrane proteins of approximately 30 kD, the so-called Rh30 polypeptides. Heterogeneously glycosylated membrane proteins of 50 and 45 kD, the Rh50 glycoproteins, are coprecipitated with the Rh30 polypeptides on immunoprecipitation with anti-Rh-specific mono- and polyclonal antibodies. The Rh antigens appear to exist as a multisubunit complex of CD47 (MIM 601028), LW (MIM 111250), glycophorin B (MIM 111740), and play a critical role in the Rh50 glycoprotein [supplied by OMIM].[2]

Interactions

RHAG has been shown to interact with ANK1.[4]

See also

References

  1. ↑ Matassi G, Chérif-Zahar B, Raynal V, Rouger P, Cartron JP (Jan 1998). "Organization of the human RH50A gene (RHAG) and evolution of base composition of the RH gene family". Genomics. 47 (2): 286–93. doi:10.1006/geno.1997.5112. PMID 9479501.
  2. ↑ 2.0 2.1 "Entrez Gene: RHAG Rh-associated glycoprotein".
  3. ↑ Stewart AK, Shmukler BE, Vandorpe DH, Rivera A, Heneghan JF, Li X, Hsu A, Karpatkin M, O'Neill AF, Bauer DE, Heeney MM, John K, Kuypers FA, Gallagher PG, Lux SE, Brugnara C, Westhoff CM, Alper SL (Dec 2011). "Loss-of-function and gain-of-function phenotypes of stomatocytosis mutant RhAG F65S". American Journal of Physiology. Cell Physiology. 301 (6): C1325–43. doi:10.1152/ajpcell.00054.2011. PMC 3233792. PMID 21849667.
  4. ↑ Nicolas V, Le Van Kim C, Gane P, Birkenmeier C, Cartron JP, Colin Y, Mouro-Chanteloup I (Jul 2003). "Rh-RhAG/ankyrin-R, a new interaction site between the membrane bilayer and the red cell skeleton, is impaired by Rh(null)-associated mutation". The Journal of Biological Chemistry. 278 (28): 25526–33. doi:10.1074/jbc.M302816200. PMID 12719424.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.


Further reading

External links


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