F11 receptor: Difference between revisions

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{{Infobox_gene}}
{{PBB_Controls
'''Junctional adhesion molecule A''' is a [[protein]] that in humans is encoded by the ''F11R'' [[gene]].<ref name="pmid10395639">{{cite journal | vauthors = Ozaki H, Ishii K, Horiuchi H, Arai H, Kawamoto T, Okawa K, Iwamatsu A, Kita T | title = Cutting edge: combined treatment of TNF-alpha and IFN-gamma causes redistribution of junctional adhesion molecule in human endothelial cells | journal = Journal of Immunology | volume = 163 | issue = 2 | pages = 553–7 | date = Jul 1999 | pmid = 10395639 | pmc =  | doi =  }}</ref><ref name="pmid7646439">{{cite journal | vauthors = Naik UP, Ehrlich YH, Kornecki E | title = Mechanisms of platelet activation by a stimulatory antibody: cross-linking of a novel platelet receptor for monoclonal antibody F11 with the Fc gamma RII receptor | journal = The Biochemical Journal | volume = 310 ( Pt 1) | issue = 1 | pages = 155–62 | date = Aug 1995 | pmid = 7646439 | pmc = 1135867 | doi = }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: F11R F11 receptor| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=50848| accessdate = }}</ref> It has also been designated as '''CD321''' ([[cluster of differentiation]] 321).
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| 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 = PBB_Protein_F11R_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1nbq.
| PDB = {{PDB2|1nbq}}
| Name = F11 receptor
| HGNCid = 14685
| Symbol = F11R
| AltSymbols =; KAT; CD321; JAM; JAM-1; JAM-A; JAM1; JAMA; JCAM; PAM-1
| OMIM = 605721
| ECnumber = 
| Homologene = 14255
| MGIid = 1321398
| GeneAtlas_image1 = PBB_GE_F11R_221664_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_F11R_222354_at_tn.png
| Function = {{GNF_GO|id=GO:0004792 |text = thiosulfate sulfurtransferase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005923 |text = tight junction}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006928 |text = cell motility}} {{GNF_GO|id=GO:0006954 |text = inflammatory response}} {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0030855 |text = epithelial cell differentiation}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 50848
    | Hs_Ensembl = ENSG00000158769
    | Hs_RefseqProtein = NP_058642
    | Hs_RefseqmRNA = NM_016946
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 1
    | Hs_GenLoc_start = 159231625
    | Hs_GenLoc_end = 159275404
    | Hs_Uniprot = Q9Y624
    | Mm_EntrezGene = 16456
    | Mm_Ensembl = ENSMUSG00000038235
    | Mm_RefseqmRNA = NM_172647
    | Mm_RefseqProtein = NP_766235
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 1
    | Mm_GenLoc_start = 173274236
    | Mm_GenLoc_end = 173301268
    | Mm_Uniprot = Q8VC39
  }}
}}
'''F11 receptor''', also known as '''F11R''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: F11R F11 receptor| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=50848| accessdate = }}</ref> KDR has also been designated as '''CD321''' ([[cluster of differentiation]] 321).


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
Tight junctions represent one mode of cell-to-cell adhesion in epithelial or endothelial cell sheets, forming continuous seals around cells and serving as a physical barrier to prevent solutes and water from passing freely through the paracellular space. The protein encoded by this immunoglobulin superfamily gene member is an important regulator of tight junction assembly in epithelia. In addition, the encoded protein can act as (1) a receptor for reovirus, (2) a ligand for the integrin LFA1, involved in leukocyte transmigration, and (3) a platelet receptor. Multiple transcript variants encoding two different isoforms have been found for this gene.<ref name="entrez"/>
{{PBB_Summary
| section_title =
| summary_text = Tight junctions represent one mode of cell-to-cell adhesion in epithelial or endothelial cell sheets, forming continuous seals around cells and serving as a physical barrier to prevent solutes and water from passing freely through the paracellular space. The protein encoded by this immunoglobulin superfamily gene member is an important regulator of tight junction assembly in epithelia. In addition, the encoded protein can act as (1) a receptor for reovirus, (2) a ligand for the integrin LFA1, involved in leukocyte transmigration, and (3) a platelet receptor. Multiple transcript variants encoding two different isoforms have been found for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: F11R F11 receptor| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=50848| accessdate = }}</ref>
}}


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


==Further reading==
F11 receptor has been shown to [[Protein-protein interaction|interact]] with [[MLLT4]],<ref name=pmid10856295>{{cite journal | vauthors = Ebnet K, Schulz CU, Meyer Zu Brickwedde MK, Pendl GG, Vestweber D | title = Junctional adhesion molecule interacts with the PDZ domain-containing proteins AF-6 and ZO-1 | journal = The Journal of Biological Chemistry | volume = 275 | issue = 36 | pages = 27979–88 | date = Sep 2000 | pmid = 10856295 | doi = 10.1074/jbc.M002363200 }}</ref> [[CASK]]<ref name=pmid10856295/><ref name=pmid11120739>{{cite journal | vauthors = Martinez-Estrada OM, Villa A, Breviario F, Orsenigo F, Dejana E, Bazzoni G | title = Association of junctional adhesion molecule with calcium/calmodulin-dependent serine protein kinase (CASK/LIN-2) in human epithelial caco-2 cells | journal = The Journal of Biological Chemistry | volume = 276 | issue = 12 | pages = 9291–6 | date = Mar 2001 | pmid = 11120739 | doi = 10.1074/jbc.M006991200 }}</ref> and [[Tight junction protein 1]].<ref name=pmid10856295/><ref name=pmid12953056>{{cite journal | vauthors = Ebnet K, Aurrand-Lions M, Kuhn A, Kiefer F, Butz S, Zander K, Meyer zu Brickwedde MK, Suzuki A, Imhof BA, Vestweber D | title = The junctional adhesion molecule (JAM) family members JAM-2 and JAM-3 associate with the cell polarity protein PAR-3: a possible role for JAMs in endothelial cell polarity | journal = Journal of Cell Science | volume = 116 | issue = Pt 19 | pages = 3879–91 | date = Oct 2003 | pmid = 12953056 | doi = 10.1242/jcs.00704 }}</ref>
 
== References ==
{{reflist}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Muller WA | title = Leukocyte-endothelial-cell interactions in leukocyte transmigration and the inflammatory response | journal = Trends in Immunology | volume = 24 | issue = 6 | pages = 327–34 | date = Jun 2003 | pmid = 12810109 | doi = 10.1016/S1471-4906(03)00117-0 }}
| citations =
* {{cite journal | vauthors = Bazzoni G | title = The JAM family of junctional adhesion molecules | journal = Current Opinion in Cell Biology | volume = 15 | issue = 5 | pages = 525–30 | date = Oct 2003 | pmid = 14519386 | doi = 10.1016/S0955-0674(03)00104-2 }}
*{{cite journal | author=Muller WA |title=Leukocyte-endothelial-cell interactions in leukocyte transmigration and the inflammatory response. |journal=Trends Immunol. |volume=24 |issue= 6 |pages= 327-34 |year= 2003 |pmid= 12810109 |doi= }}
* {{cite journal | vauthors = Naik UP, Eckfeld K | title = Junctional adhesion molecule 1 (JAM-1) | journal = Journal of Biological Regulators and Homeostatic Agents | volume = 17 | issue = 4 | pages = 341–7 | year = 2004 | pmid = 15065765 | doi =  }}
*{{cite journal | author=Bazzoni G |title=The JAM family of junctional adhesion molecules. |journal=Curr. Opin. Cell Biol. |volume=15 |issue= 5 |pages= 525-30 |year= 2004 |pmid= 14519386 |doi= }}
* {{cite journal | vauthors = Kornecki E, Walkowiak B, Naik UP, Ehrlich YH | title = Activation of human platelets by a stimulatory monoclonal antibody | journal = The Journal of Biological Chemistry | volume = 265 | issue = 17 | pages = 10042–8 | date = Jun 1990 | pmid = 2351647 | doi =  }}
*{{cite journal | author=Naik UP, Eckfeld K |title=Junctional adhesion molecule 1 (JAM-1). |journal=J. Biol. Regul. Homeost. Agents |volume=17 |issue= 4 |pages= 341-7 |year= 2004 |pmid= 15065765 |doi=  }}
* {{cite journal | vauthors = Williams LA, Martin-Padura I, Dejana E, Hogg N, Simmons DL | title = Identification and characterisation of human Junctional Adhesion Molecule (JAM) | journal = Molecular Immunology | volume = 36 | issue = 17 | pages = 1175–88 | date = Dec 1999 | pmid = 10698320 | doi = 10.1016/S0161-5890(99)00122-4 }}
*{{cite journal | author=Kornecki E, Walkowiak B, Naik UP, Ehrlich YH |title=Activation of human platelets by a stimulatory monoclonal antibody. |journal=J. Biol. Chem. |volume=265 |issue= 17 |pages= 10042-8 |year= 1990 |pmid= 2351647 |doi=  }}
* {{cite journal | vauthors = Sobocka MB, Sobocki T, Banerjee P, Weiss C, Rushbrook JI, Norin AJ, Hartwig J, Salifu MO, Markell MS, Babinska A, Ehrlich YH, Kornecki E | title = Cloning of the human platelet F11 receptor: a cell adhesion molecule member of the immunoglobulin superfamily involved in platelet aggregation | journal = Blood | volume = 95 | issue = 8 | pages = 2600–9 | date = Apr 2000 | pmid = 10753840 | doi =  }}
*{{cite journal | author=Naik UP, Ehrlich YH, Kornecki E |title=Mechanisms of platelet activation by a stimulatory antibody: cross-linking of a novel platelet receptor for monoclonal antibody F11 with the Fc gamma RII receptor. |journal=Biochem. J. |volume=310 ( Pt 1) |issue= |pages= 155-62 |year= 1995 |pmid= 7646439 |doi= }}
* {{cite journal | vauthors = Liu Y, Nusrat A, Schnell FJ, Reaves TA, Walsh S, Pochet M, Parkos CA | title = Human junction adhesion molecule regulates tight junction resealing in epithelia | journal = Journal of Cell Science | volume = 113 ( Pt 13) | issue = 13 | pages = 2363–74 | date = Jul 2000 | pmid = 10852816 | doi =  }}
*{{cite journal | author=Ozaki H, Ishii K, Horiuchi H, ''et al.'' |title=Cutting edge: combined treatment of TNF-alpha and IFN-gamma causes redistribution of junctional adhesion molecule in human endothelial cells. |journal=J. Immunol. |volume=163 |issue= 2 |pages= 553-7 |year= 1999 |pmid= 10395639 |doi=  }}
* {{cite journal | vauthors = Ebnet K, Schulz CU, Meyer Zu Brickwedde MK, Pendl GG, Vestweber D | title = Junctional adhesion molecule interacts with the PDZ domain-containing proteins AF-6 and ZO-1 | journal = The Journal of Biological Chemistry | volume = 275 | issue = 36 | pages = 27979–88 | date = Sep 2000 | pmid = 10856295 | doi = 10.1074/jbc.M002363200 }}
*{{cite journal | author=Williams LA, Martin-Padura I, Dejana E, ''et al.'' |title=Identification and characterisation of human Junctional Adhesion Molecule (JAM). |journal=Mol. Immunol. |volume=36 |issue= 17 |pages= 1175-88 |year= 2000 |pmid= 10698320 |doi=  }}
* {{cite journal | vauthors = Bazzoni G, Martinez-Estrada OM, Orsenigo F, Cordenonsi M, Citi S, Dejana E | title = Interaction of junctional adhesion molecule with the tight junction components ZO-1, cingulin, and occludin | journal = The Journal of Biological Chemistry | volume = 275 | issue = 27 | pages = 20520–6 | date = Jul 2000 | pmid = 10877843 | doi = 10.1074/jbc.M905251199 }}
*{{cite journal | author=Sobocka MB, Sobocki T, Banerjee P, ''et al.'' |title=Cloning of the human platelet F11 receptor: a cell adhesion molecule member of the immunoglobulin superfamily involved in platelet aggregation. |journal=Blood |volume=95 |issue= 8 |pages= 2600-9 |year= 2000 |pmid= 10753840 |doi= }}
* {{cite journal | vauthors = Gupta SK, Pillarisetti K, Ohlstein EH | title = Platelet agonist F11 receptor is a member of the immunoglobulin superfamily and identical with junctional adhesion molecule (JAM): regulation of expression in human endothelial cells and macrophages | journal = IUBMB Life | volume = 50 | issue = 1 | pages = 51–6 | date = Jul 2000 | pmid = 11087121 | doi = 10.1080/15216540050176593 }}
*{{cite journal | author=Liu Y, Nusrat A, Schnell FJ, ''et al.'' |title=Human junction adhesion molecule regulates tight junction resealing in epithelia. |journal=J. Cell. Sci. |volume=113 ( Pt 13) |issue= |pages= 2363-74 |year= 2000 |pmid= 10852816 |doi= }}
* {{cite journal | vauthors = Martinez-Estrada OM, Villa A, Breviario F, Orsenigo F, Dejana E, Bazzoni G | title = Association of junctional adhesion molecule with calcium/calmodulin-dependent serine protein kinase (CASK/LIN-2) in human epithelial caco-2 cells | journal = The Journal of Biological Chemistry | volume = 276 | issue = 12 | pages = 9291–6 | date = Mar 2001 | pmid = 11120739 | doi = 10.1074/jbc.M006991200 }}
*{{cite journal | author=Ebnet K, Schulz CU, Meyer Zu Brickwedde MK, ''et al.'' |title=Junctional adhesion molecule interacts with the PDZ domain-containing proteins AF-6 and ZO-1. |journal=J. Biol. Chem. |volume=275 |issue= 36 |pages= 27979-88 |year= 2000 |pmid= 10856295 |doi= 10.1074/jbc.M002363200 }}
* {{cite journal | vauthors = Naik UP, Naik MU, Eckfeld K, Martin-DeLeon P, Spychala J | title = Characterization and chromosomal localization of JAM-1, a platelet receptor for a stimulatory monoclonal antibody | journal = Journal of Cell Science | volume = 114 | issue = Pt 3 | pages = 539–47 | date = Feb 2001 | pmid = 11171323 | doi =  }}
*{{cite journal | author=Bazzoni G, Martinez-Estrada OM, Orsenigo F, ''et al.'' |title=Interaction of junctional adhesion molecule with the tight junction components ZO-1, cingulin, and occludin. |journal=J. Biol. Chem. |volume=275 |issue= 27 |pages= 20520-6 |year= 2000 |pmid= 10877843 |doi= 10.1074/jbc.M905251199 }}
* {{cite journal | vauthors = Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Böcher M, Blöcker H, Bauersachs S, Blum H, Lauber J, Düsterhöft A, Beyer A, Köhrer K, Strack N, Mewes HW, Ottenwälder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A | title = Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs | journal = Genome Research | volume = 11 | issue = 3 | pages = 422–35 | date = Mar 2001 | pmid = 11230166 | pmc = 311072 | doi = 10.1101/gr.GR1547R }}
*{{cite journal | author=Gupta SK, Pillarisetti K, Ohlstein EH |title=Platelet agonist F11 receptor is a member of the immunoglobulin superfamily and identical with junctional adhesion molecule (JAM): regulation of expression in human endothelial cells and macrophages. |journal=IUBMB Life |volume=50 |issue= 1 |pages= 51-6 |year= 2001 |pmid= 11087121 |doi=  }}
* {{cite journal | vauthors = Barton ES, Forrest JC, Connolly JL, Chappell JD, Liu Y, Schnell FJ, Nusrat A, Parkos CA, Dermody TS | title = Junction adhesion molecule is a receptor for reovirus | journal = Cell | volume = 104 | issue = 3 | pages = 441–51 | date = Feb 2001 | pmid = 11239401 | doi = 10.1016/S0092-8674(01)00231-8 }}
*{{cite journal | author=Martinez-Estrada OM, Villa A, Breviario F, ''et al.'' |title=Association of junctional adhesion molecule with calcium/calmodulin-dependent serine protein kinase (CASK/LIN-2) in human epithelial caco-2 cells. |journal=J. Biol. Chem. |volume=276 |issue= 12 |pages= 9291-6 |year= 2001 |pmid= 11120739 |doi= 10.1074/jbc.M006991200 }}
* {{cite journal | vauthors = Simpson JC, Wellenreuther R, Poustka A, Pepperkok R, Wiemann S | title = Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing | journal = EMBO Reports | volume = 1 | issue = 3 | pages = 287–92 | date = Sep 2000 | pmid = 11256614 | pmc = 1083732 | doi = 10.1093/embo-reports/kvd058 }}
*{{cite journal | author=Naik UP, Naik MU, Eckfeld K, ''et al.'' |title=Characterization and chromosomal localization of JAM-1, a platelet receptor for a stimulatory monoclonal antibody. |journal=J. Cell. Sci. |volume=114 |issue= Pt 3 |pages= 539-47 |year= 2001 |pmid= 11171323 |doi= }}
* {{cite journal | vauthors = Ebnet K, Suzuki A, Horikoshi Y, Hirose T, Meyer Zu Brickwedde MK, Ohno S, Vestweber D | title = The cell polarity protein ASIP/PAR-3 directly associates with junctional adhesion molecule (JAM) | journal = The EMBO Journal | volume = 20 | issue = 14 | pages = 3738–48 | date = Jul 2001 | pmid = 11447115 | pmc = 125258 | doi = 10.1093/emboj/20.14.3738 }}
*{{cite journal | author=Wiemann S, Weil B, Wellenreuther R, ''et al.'' |title=Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. |journal=Genome Res. |volume=11 |issue= 3 |pages= 422-35 |year= 2001 |pmid= 11230166 |doi= 10.1101/gr.154701 }}
* {{cite journal | vauthors = Itoh M, Sasaki H, Furuse M, Ozaki H, Kita T, Tsukita S | title = Junctional adhesion molecule (JAM) binds to PAR-3: a possible mechanism for the recruitment of PAR-3 to tight junctions | journal = The Journal of Cell Biology | volume = 154 | issue = 3 | pages = 491–7 | date = Aug 2001 | pmid = 11489913 | pmc = 2196413 | doi = 10.1083/jcb.200103047 }}
*{{cite journal | author=Barton ES, Forrest JC, Connolly JL, ''et al.'' |title=Junction adhesion molecule is a receptor for reovirus. |journal=Cell |volume=104 |issue= 3 |pages= 441-51 |year= 2001 |pmid= 11239401 |doi= }}
* {{cite journal | vauthors = Hamazaki Y, Itoh M, Sasaki H, Furuse M, Tsukita S | title = Multi-PDZ domain protein 1 (MUPP1) is concentrated at tight junctions through its possible interaction with claudin-1 and junctional adhesion molecule | journal = The Journal of Biological Chemistry | volume = 277 | issue = 1 | pages = 455–61 | date = Jan 2002 | pmid = 11689568 | doi = 10.1074/jbc.M109005200 }}
*{{cite journal | author=Simpson JC, Wellenreuther R, Poustka A, ''et al.'' |title=Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing. |journal=EMBO Rep. |volume=1 |issue= 3 |pages= 287-92 |year= 2001 |pmid= 11256614 |doi= 10.1093/embo-reports/kvd058 }}
*{{cite journal | author=Ebnet K, Suzuki A, Horikoshi Y, ''et al.'' |title=The cell polarity protein ASIP/PAR-3 directly associates with junctional adhesion molecule (JAM). |journal=EMBO J. |volume=20 |issue= 14 |pages= 3738-48 |year= 2001 |pmid= 11447115 |doi= 10.1093/emboj/20.14.3738 }}
*{{cite journal  | author=Itoh M, Sasaki H, Furuse M, ''et al.'' |title=Junctional adhesion molecule (JAM) binds to PAR-3: a possible mechanism for the recruitment of PAR-3 to tight junctions. |journal=J. Cell Biol. |volume=154 |issue= 3 |pages= 491-7 |year= 2001 |pmid= 11489913 |doi= 10.1083/jcb.200103047 }}
*{{cite journal  | author=Hamazaki Y, Itoh M, Sasaki H, ''et al.'' |title=Multi-PDZ domain protein 1 (MUPP1) is concentrated at tight junctions through its possible interaction with claudin-1 and junctional adhesion molecule. |journal=J. Biol. Chem. |volume=277 |issue= 1 |pages= 455-61 |year= 2002 |pmid= 11689568 |doi= 10.1074/jbc.M109005200 }}
}}
{{refend}}
{{refend}}


==External links==
== External links ==
* {{MeshName|KDR+protein,+human}}
* {{MeshName|KDR+protein,+human}}


{{membrane-protein-stub}}
{{NLM content}}
{{NLM content}}
{{PDB Gallery|geneid=50848}}
{{Clusters of differentiation}}
{{Clusters of differentiation}}
[[Category:Clusters of differentiation]]
[[Category:Clusters of differentiation]]
{{WikiDoc Sources}}
 
 
{{membrane-protein-stub}}

Revision as of 04:30, 31 August 2017

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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

Junctional adhesion molecule A is a protein that in humans is encoded by the F11R gene.[1][2][3] It has also been designated as CD321 (cluster of differentiation 321).

Function

Tight junctions represent one mode of cell-to-cell adhesion in epithelial or endothelial cell sheets, forming continuous seals around cells and serving as a physical barrier to prevent solutes and water from passing freely through the paracellular space. The protein encoded by this immunoglobulin superfamily gene member is an important regulator of tight junction assembly in epithelia. In addition, the encoded protein can act as (1) a receptor for reovirus, (2) a ligand for the integrin LFA1, involved in leukocyte transmigration, and (3) a platelet receptor. Multiple transcript variants encoding two different isoforms have been found for this gene.[3]

Interactions

F11 receptor has been shown to interact with MLLT4,[4] CASK[4][5] and Tight junction protein 1.[4][6]

References

  1. ↑ Ozaki H, Ishii K, Horiuchi H, Arai H, Kawamoto T, Okawa K, Iwamatsu A, Kita T (Jul 1999). "Cutting edge: combined treatment of TNF-alpha and IFN-gamma causes redistribution of junctional adhesion molecule in human endothelial cells". Journal of Immunology. 163 (2): 553–7. PMID 10395639.
  2. ↑ Naik UP, Ehrlich YH, Kornecki E (Aug 1995). "Mechanisms of platelet activation by a stimulatory antibody: cross-linking of a novel platelet receptor for monoclonal antibody F11 with the Fc gamma RII receptor". The Biochemical Journal. 310 ( Pt 1) (1): 155–62. PMC 1135867. PMID 7646439.
  3. ↑ 3.0 3.1 "Entrez Gene: F11R F11 receptor".
  4. ↑ 4.0 4.1 4.2 Ebnet K, Schulz CU, Meyer Zu Brickwedde MK, Pendl GG, Vestweber D (Sep 2000). "Junctional adhesion molecule interacts with the PDZ domain-containing proteins AF-6 and ZO-1". The Journal of Biological Chemistry. 275 (36): 27979–88. doi:10.1074/jbc.M002363200. PMID 10856295.
  5. ↑ Martinez-Estrada OM, Villa A, Breviario F, Orsenigo F, Dejana E, Bazzoni G (Mar 2001). "Association of junctional adhesion molecule with calcium/calmodulin-dependent serine protein kinase (CASK/LIN-2) in human epithelial caco-2 cells". The Journal of Biological Chemistry. 276 (12): 9291–6. doi:10.1074/jbc.M006991200. PMID 11120739.
  6. ↑ Ebnet K, Aurrand-Lions M, Kuhn A, Kiefer F, Butz S, Zander K, Meyer zu Brickwedde MK, Suzuki A, Imhof BA, Vestweber D (Oct 2003). "The junctional adhesion molecule (JAM) family members JAM-2 and JAM-3 associate with the cell polarity protein PAR-3: a possible role for JAMs in endothelial cell polarity". Journal of Cell Science. 116 (Pt 19): 3879–91. doi:10.1242/jcs.00704. PMID 12953056.

Further reading

External links

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


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