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{{Infobox_gene}}
{{PBB_Controls
'''Integrin, alpha L (antigen CD11A (p180), lymphocyte function-associated antigen 1; alpha polypeptide)''', also known as '''ITGAL''', is a human [[gene]] which functions in the immune system. It is involved in cellular adhesion and costimulatory signaling. It is the target of the drug [[efalizumab]].
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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_ITGAL_image.jpg
ITGAL encodes the integrin alpha L chain. Integrins are heterodimeric integral membrane proteins composed of an alpha chain and a beta chain. This I-domain containing alpha integrin combines with the beta 2 chain (ITGB2) to form the integrin lymphocyte function-associated antigen-1 (LFA-1), which is expressed on all leukocytes. LFA-1 plays a central role in leukocyte intercellular adhesion through interactions with its ligands, ICAMs 1-3 (intercellular adhesion molecules 1 through 3), and also functions in lymphocyte costimulatory signaling.<ref>{{cite web | title = Entrez Gene: ITGAL integrin, alpha L (antigen CD11A (p180), lymphocyte function-associated antigen 1; alpha polypeptide)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3683| accessdate = }}</ref>
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1cqp.
| PDB = {{PDB2|1cqp}}, {{PDB2|1dgq}}, {{PDB2|1lfa}}, {{PDB2|1mjn}}, {{PDB2|1mq8}}, {{PDB2|1mq9}}, {{PDB2|1mqa}}, {{PDB2|1rd4}}, {{PDB2|1t0p}}, {{PDB2|1xdd}}, {{PDB2|1xdg}}, {{PDB2|1xuo}}, {{PDB2|1zon}}, {{PDB2|1zoo}}, {{PDB2|1zop}}, {{PDB2|2ica}}, {{PDB2|2o7n}}
| Name = Integrin, alpha L (antigen CD11A (p180), lymphocyte function-associated antigen 1; alpha polypeptide)
| HGNCid = 6148
| Symbol = ITGAL
| AltSymbols =; CD11A; LFA-1; LFA1A
| OMIM = 153370
| ECnumber =
| Homologene = 1666
| MGIid = 96606
| GeneAtlas_image1 = PBB_GE_ITGAL_213475_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000287 |text = magnesium ion binding}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0008305 |text = integrin complex}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{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:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007229 |text = integrin-mediated signaling pathway}} {{GNF_GO|id=GO:0050798 |text = activated T cell proliferation}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 3683
    | Hs_Ensembl = ENSG00000005844
    | Hs_RefseqProtein = NP_002200
    | Hs_RefseqmRNA = NM_002209
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 16
    | Hs_GenLoc_start = 30391551
    | Hs_GenLoc_end = 30441772
    | Hs_Uniprot = P20701
    | Mm_EntrezGene = 16408
    | Mm_Ensembl = ENSMUSG00000030830
    | Mm_RefseqmRNA = NM_008400
    | Mm_RefseqProtein = NP_032426
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 7
    | Mm_GenLoc_start = 127087558
    | Mm_GenLoc_end = 127124876
    | Mm_Uniprot = Q3T9N8
  }}
}}
'''Integrin, alpha L (antigen CD11A (p180), lymphocyte function-associated antigen 1; alpha polypeptide)''', also known as '''ITGAL''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = ITGAL encodes the integrin alpha L chain. Integrins are heterodimeric integral membrane proteins composed of an alpha chain and a beta chain. This I-domain containing alpha integrin combines with the beta 2 chain (ITGB2) to form the integrin lymphocyte function-associated antigen-1 (LFA-1), which is expressed on all leukocytes. LFA-1 plays a central role in leukocyte intercellular adhesion through interactions with its ligands, ICAMs 1-3 (intercellular adhesion molecules 1 through 3), and also functions in lymphocyte costimulatory signaling.<ref>{{cite web | title = Entrez Gene: ITGAL integrin, alpha L (antigen CD11A (p180), lymphocyte function-associated antigen 1; alpha polypeptide)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3683| accessdate = }}</ref>
}}


CD11a is one of the two components, along with [[CD18]], which form [[lymphocyte function-associated antigen-1]].
CD11a is one of the two components, along with [[CD18]], which form [[lymphocyte function-associated antigen-1]].


[[Efalizumab]] acts as an [[immunosuppressant]] by binding to CD11a.
[[Efalizumab]] acts as an [[immunosuppressant]] by binding to CD11a but was withdrawn in 2009 because it was associated with severe side effects.
 
== Interactions ==
 
CD11a has been shown to [[Protein-protein interaction|interact]] with [[ICAM-1]].<ref name=pmid11279101>{{cite journal | vauthors = Lu C, Takagi J, Springer TA | title = Association of the membrane proximal regions of the alpha and beta subunit cytoplasmic domains constrains an integrin in the inactive state | journal = J. Biol. Chem. | volume = 276 | issue = 18 | pages = 14642–8 | date = May 2001 | pmid = 11279101 | doi = 10.1074/jbc.M100600200 }}</ref><ref name=pmid12526797>{{cite journal | vauthors = Shimaoka M, Xiao T, Liu JH, Yang Y, Dong Y, Jun CD, McCormack A, Zhang R, Joachimiak A, Takagi J, Wang JH, Springer TA | title = Structures of the alpha L I domain and its complex with ICAM-1 reveal a shape-shifting pathway for integrin regulation | journal = Cell | volume = 112 | issue = 1 | pages = 99–111 | date = Jan 2003 | pmid = 12526797 | doi = 10.1016/S0092-8674(02)01257-6 }}</ref><ref name=pmid11786177>{{cite journal | vauthors = Yusuf-Makagiansar H, Makagiansar IT, Hu Y, Siahaan TJ | title = Synergistic inhibitory activity of alpha- and beta-LFA-1 peptides on LFA-1/ICAM-1 interaction | journal = Peptides | volume = 22 | issue = 12 | pages = 1955–62 | date = Dec 2001 | pmid = 11786177 | doi = 10.1016/S0196-9781(01)00546-0 }}</ref>


==See also==
== See also ==
* [[CD11c]]
* [[CD11c]]
* [[integrin]]
* [[integrin]]
* [[leukocyte adhesion deficiency]]
* [[leukocyte adhesion deficiency]]
* [[Cluster of differentiation]]


==References==
== References ==
{{reflist|2}}
{{reflist}}
==Further reading==
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Lub M, van Kooyk Y, Figdor CG | title = Ins and outs of LFA-1. | journal = Immunol. Today | volume = 16 | issue = 10 | pages = 479–83 | year = 1995 | pmid = 7576051 | doi = 10.1016/0167-5699(95)80031-X }}
| citations =
* {{cite journal | vauthors = Dickeson SK, Santoro SA | title = Ligand recognition by the I domain-containing integrins. | journal = Cell. Mol. Life Sci. | volume = 54 | issue = 6 | pages = 556–66 | year = 1998 | pmid = 9676575 | doi = 10.1007/s000180050184 }}
*{{cite journal | author=Lub M, van Kooyk Y, Figdor CG |title=Ins and outs of LFA-1. |journal=Immunol. Today |volume=16 |issue= 10 |pages= 479-83 |year= 1995 |pmid= 7576051 |doi= }}
* {{cite journal | vauthors = Porter JC, Hogg N | title = Integrins take partners: cross-talk between integrins and other membrane receptors. | journal = Trends Cell Biol. | volume = 8 | issue = 10 | pages = 390–6 | year = 1999 | pmid = 9789327 | doi = 10.1016/S0962-8924(98)01344-0 }}
*{{cite journal | author=Dickeson SK, Santoro SA |title=Ligand recognition by the I domain-containing integrins. |journal=Cell. Mol. Life Sci. |volume=54 |issue= 6 |pages= 556-66 |year= 1998 |pmid= 9676575 |doi= }}
* {{cite journal | vauthors = Giblin PA, Lemieux RM | title = LFA-1 as a key regulator of immune function: approaches toward the development of LFA-1-based therapeutics. | journal = Curr. Pharm. Des. | volume = 12 | issue = 22 | pages = 2771–95 | year = 2006 | pmid = 16918410 | doi = 10.2174/138161206777947731 }}
*{{cite journal | author=Porter JC, Hogg N |title=Integrins take partners: cross-talk between integrins and other membrane receptors. |journal=Trends Cell Biol. |volume=8 |issue= 10 |pages= 390-6 |year= 1999 |pmid= 9789327 |doi= }}
* {{cite journal | vauthors = Maurer D, Holter W, Majdic O, Fischer GF, Knapp W | title = CD27 expression by a distinct subpopulation of human B lymphocytes. | journal = Eur. J. Immunol. | volume = 20 | issue = 12 | pages = 2679–84 | year = 1991 | pmid = 1702722 | doi = 10.1002/eji.1830201223 }}
*{{cite journal | author=Giblin PA, Lemieux RM |title=LFA-1 as a key regulator of immune function: approaches toward the development of LFA-1-based therapeutics. |journal=Curr. Pharm. Des. |volume=12 |issue= 22 |pages= 2771-95 |year= 2006 |pmid= 16918410 |doi= }}
* {{cite journal | vauthors = Kalter DC, Gendelman HE, Meltzer MS | title = Inhibition of human immunodeficiency virus infection in monocytes by monoclonal antibodies against leukocyte adhesion molecules. | journal = Immunol. Lett. | volume = 30 | issue = 2 | pages = 219–27 | year = 1992 | pmid = 1757107 | doi = 10.1016/0165-2478(91)90029-A }}
*{{cite journal | author=Maurer D, Holter W, Majdic O, ''et al.'' |title=CD27 expression by a distinct subpopulation of human B lymphocytes. |journal=Eur. J. Immunol. |volume=20 |issue= 12 |pages= 2679-84 |year= 1991 |pmid= 1702722 |doi= }}
* {{cite journal | vauthors = Alvarez V, Pulido R, Campanero MR, Paraiso V, de Landázuri MO, Sánchez-Madrid F | title = Differentially regulated cell surface expression of leukocyte adhesion receptors on neutrophils. | journal = Kidney Int. | volume = 40 | issue = 5 | pages = 899–905 | year = 1992 | pmid = 1762294 | doi = 10.1038/ki.1991.291 }}
*{{cite journal | author=Kalter DC, Gendelman HE, Meltzer MS |title=Inhibition of human immunodeficiency virus infection in monocytes by monoclonal antibodies against leukocyte adhesion molecules. |journal=Immunol. Lett. |volume=30 |issue= 2 |pages= 219-27 |year= 1992 |pmid= 1757107 |doi= }}
* {{cite journal | vauthors = Valentin A, Lundin K, Patarroyo M, Asjö B | title = The leukocyte adhesion glycoprotein CD18 participates in HIV-1-induced syncytia formation in monocytoid and T cells. | journal = J. Immunol. | volume = 144 | issue = 3 | pages = 934–7 | year = 1990 | pmid = 1967280 | doi =  }}
*{{cite journal | author=Alvarez V, Pulido R, Campanero MR, ''et al.'' |title=Differentially regulated cell surface expression of leukocyte adhesion receptors on neutrophils. |journal=Kidney Int. |volume=40 |issue= 5 |pages= 899-905 |year= 1992 |pmid= 1762294 |doi= }}
* {{cite journal | vauthors = Larson RS, Corbi AL, Berman L, Springer T | title = Primary structure of the leukocyte function-associated molecule-1 alpha subunit: an integrin with an embedded domain defining a protein superfamily | journal = J. Cell Biol. | volume = 108 | issue = 2 | pages = 703–12 | year = 1989 | pmid = 2537322 | pmc = 2115430 | doi = 10.1083/jcb.108.2.703 }}
*{{cite journal | author=Valentin A, Lundin K, Patarroyo M, Asjö B |title=The leukocyte adhesion glycoprotein CD18 participates in HIV-1-induced syncytia formation in monocytoid and T cells. |journal=J. Immunol. |volume=144 |issue= 3 |pages= 934-7 |year= 1990 |pmid= 1967280 |doi=  }}
* {{cite journal | vauthors = Hildreth JE, Orentas RJ | title = Involvement of a leukocyte adhesion receptor (LFA-1) in HIV-induced syncytium formation | journal = Science | volume = 244 | issue = 4908 | pages = 1075–8 | year = 1989 | pmid = 2543075 | doi = 10.1126/science.2543075 }}
*{{cite journal | author=Larson RS, Corbi AL, Berman L, Springer T |title=Primary structure of the leukocyte function-associated molecule-1 alpha subunit: an integrin with an embedded domain defining a protein superfamily. |journal=J. Cell Biol. |volume=108 |issue= 2 |pages= 703-12 |year= 1989 |pmid= 2537322 |doi= }}
* {{cite journal | vauthors = Sanders ME, Makgoba MW, Sharrow SO, Stephany D, Springer TA, Young HA, Shaw S | title = Human memory T lymphocytes express increased levels of three cell adhesion molecules (LFA-3, CD2, and LFA-1) and three other molecules (UCHL1, CDw29, and Pgp-1) and have enhanced IFN-gamma production | journal = J. Immunol. | volume = 140 | issue = 5 | pages = 1401–7 | year = 1988 | pmid = 2894392 | doi =  }}
*{{cite journal | author=Hildreth JE, Orentas RJ |title=Involvement of a leukocyte adhesion receptor (LFA-1) in HIV-induced syncytium formation. |journal=Science |volume=244 |issue= 4908 |pages= 1075-8 |year= 1989 |pmid= 2543075 |doi= }}
* {{cite journal | vauthors = Corbi AL, Larson RS, Kishimoto TK, Springer TA, Morton CC | title = Chromosomal location of the genes encoding the leukocyte adhesion receptors LFA-1, Mac-1 and p150,95. Identification of a gene cluster involved in cell adhesion | journal = J. Exp. Med. | volume = 167 | issue = 5 | pages = 1597–607 | year = 1988 | pmid = 3284962 | pmc = 2188934 | doi = 10.1084/jem.167.5.1597 }}
*{{cite journal | author=Sanders ME, Makgoba MW, Sharrow SO, ''et al.'' |title=Human memory T lymphocytes express increased levels of three cell adhesion molecules (LFA-3, CD2, and LFA-1) and three other molecules (UCHL1, CDw29, and Pgp-1) and have enhanced IFN-gamma production. |journal=J. Immunol. |volume=140 |issue= 5 |pages= 1401-7 |year= 1988 |pmid= 2894392 |doi=  }}
* {{cite journal | vauthors = te Velde AA, Keizer GD, Figdor CG | title = Differential function of LFA-1 family molecules (CD11 and CD18) in adhesion of human monocytes to melanoma and endothelial cells | journal = Immunology | volume = 61 | issue = 3 | pages = 261–7 | year = 1987 | pmid = 3301632 | pmc = 1453405 | doi =  }}
*{{cite journal | author=Corbi AL, Larson RS, Kishimoto TK, ''et al.'' |title=Chromosomal location of the genes encoding the leukocyte adhesion receptors LFA-1, Mac-1 and p150,95. Identification of a gene cluster involved in cell adhesion. |journal=J. Exp. Med. |volume=167 |issue= 5 |pages= 1597-607 |year= 1988 |pmid= 3284962 |doi= }}
* {{cite journal | vauthors = Qu A, Leahy DJ | title = Crystal structure of the I-domain from the CD11a/CD18 (LFA-1, alpha L beta 2) integrin | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 92 | issue = 22 | pages = 10277–81 | year = 1995 | pmid = 7479767 | pmc = 40779 | doi = 10.1073/pnas.92.22.10277 }}
*{{cite journal | author=te Velde AA, Keizer GD, Figdor CG |title=Differential function of LFA-1 family molecules (CD11 and CD18) in adhesion of human monocytes to melanoma and endothelial cells. |journal=Immunology |volume=61 |issue= 3 |pages= 261-7 |year= 1987 |pmid= 3301632 |doi=  }}
* {{cite journal | vauthors = Turner ML, McIlwaine K, Anthony RS, Parker AC | title = Differential expression of cell adhesion molecules by human hematopoietic progenitor cells from bone marrow and mobilized adult peripheral blood | journal = Stem Cells | volume = 13 | issue = 3 | pages = 311–6 | year = 1995 | pmid = 7542116 | doi = 10.1002/stem.5530130312 }}
*{{cite journal | author=Qu A, Leahy DJ |title=Crystal structure of the I-domain from the CD11a/CD18 (LFA-1, alpha L beta 2) integrin. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 22 |pages= 10277-81 |year= 1995 |pmid= 7479767 |doi= }}
* {{cite journal | vauthors = Marzusch K, Ruck P, Geiselhart A, Handgretinger R, Dietl JA, Kaiserling E, Horny HP, Vince G, Redman CW | title = Distribution of cell adhesion molecules on CD56++, CD3-, CD16- large granular lymphocytes and endothelial cells in first-trimester human decidua | journal = Hum. Reprod. | volume = 8 | issue = 8 | pages = 1203–8 | year = 1993 | pmid = 7691868 | doi =  }}
*{{cite journal | author=Turner ML, McIlwaine K, Anthony RS, Parker AC |title=Differential expression of cell adhesion molecules by human hematopoietic progenitor cells from bone marrow and mobilized adult peripheral blood. |journal=Stem Cells |volume=13 |issue= 3 |pages= 311-6 |year= 1995 |pmid= 7542116 |doi= }}
* {{cite journal | vauthors = Capobianchi MR, Ameglio F, Cordiali Fei P, Castilletti C, Mercuri F, Fais S, Dianzani F | title = Coordinate induction of interferon alpha and gamma by recombinant HIV-1 glycoprotein 120 | journal = AIDS Res. Hum. Retroviruses | volume = 9 | issue = 10 | pages = 957–62 | year = 1994 | pmid = 7904170 | doi = 10.1089/aid.1993.9.957 }}
*{{cite journal | author=Marzusch K, Ruck P, Geiselhart A, ''et al.'' |title=Distribution of cell adhesion molecules on CD56++, CD3-, CD16- large granular lymphocytes and endothelial cells in first-trimester human decidua. |journal=Hum. Reprod. |volume=8 |issue= 8 |pages= 1203-8 |year= 1993 |pmid= 7691868 |doi=  }}
* {{cite journal | vauthors = Berman PW, Nakamura GR | title = Adhesion mediated by intercellular adhesion molecule 1 attenuates the potency of antibodies that block HIV-1 gp160-dependent syncytium formation | journal = AIDS Res. Hum. Retroviruses | volume = 10 | issue = 5 | pages = 585–93 | year = 1994 | pmid = 7917519 | doi = 10.1089/aid.1994.10.585 }}
*{{cite journal | author=Capobianchi MR, Ameglio F, Cordiali Fei P, ''et al.'' |title=Coordinate induction of interferon alpha and gamma by recombinant HIV-1 glycoprotein 120. |journal=AIDS Res. Hum. Retroviruses |volume=9 |issue= 10 |pages= 957-62 |year= 1994 |pmid= 7904170 |doi= }}
* {{cite journal | vauthors = Chirmule N, Oyaizu N, Saxinger C, Pahwa S | title = Nef protein of HIV-1 has B-cell stimulatory activity | journal = AIDS | volume = 8 | issue = 6 | pages = 733–4 | year = 1994 | pmid = 8086129 | doi = 10.1097/00002030-199406000-00002 }}
*{{cite journal | author=Berman PW, Nakamura GR |title=Adhesion mediated by intercellular adhesion molecule 1 attenuates the potency of antibodies that block HIV-1 gp160-dependent syncytium formation. |journal=AIDS Res. Hum. Retroviruses |volume=10 |issue= 5 |pages= 585-93 |year= 1994 |pmid= 7917519 |doi= }}
*{{cite journal | author=Chirmule N, Oyaizu N, Saxinger C, Pahwa S |title=Nef protein of HIV-1 has B-cell stimulatory activity. |journal=AIDS |volume=8 |issue= 6 |pages= 733-4 |year= 1994 |pmid= 8086129 |doi= }}
}}
{{refend}}
{{refend}}
{{PDB Gallery|geneid=3683}}


==External links==
== External links ==
* {{MeshName|CD11a+Antigen}}
* {{MeshName|CD11a+Antigen}}
*[http://cmkb.cellmigration.org/report.cgi?report=orth_overview&gene_id=3683 ITGAL] Info with links in the [http://www.cellmigration.org/index.shtml Cell Migration Gateway]
* {{UCSC gene info|ITGAL}}


{{Clusters of differentiation}}
{{Integrins}}
{{DEFAULTSORT:Cd11a}}
[[Category:Integrins]]
[[Category:Clusters of differentiation]]


{{Clusters of differentiation}}
{{protein-stub}}


[[it:CD11a]]
{{gene-16-stub}}
[[Category:integrins]]
{{WikiDoc Sources}}

Latest revision as of 21:32, 29 November 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

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

Integrin, alpha L (antigen CD11A (p180), lymphocyte function-associated antigen 1; alpha polypeptide), also known as ITGAL, is a human gene which functions in the immune system. It is involved in cellular adhesion and costimulatory signaling. It is the target of the drug efalizumab.

Function

ITGAL encodes the integrin alpha L chain. Integrins are heterodimeric integral membrane proteins composed of an alpha chain and a beta chain. This I-domain containing alpha integrin combines with the beta 2 chain (ITGB2) to form the integrin lymphocyte function-associated antigen-1 (LFA-1), which is expressed on all leukocytes. LFA-1 plays a central role in leukocyte intercellular adhesion through interactions with its ligands, ICAMs 1-3 (intercellular adhesion molecules 1 through 3), and also functions in lymphocyte costimulatory signaling.[1]

CD11a is one of the two components, along with CD18, which form lymphocyte function-associated antigen-1.

Efalizumab acts as an immunosuppressant by binding to CD11a but was withdrawn in 2009 because it was associated with severe side effects.

Interactions

CD11a has been shown to interact with ICAM-1.[2][3][4]

See also

References

  1. "Entrez Gene: ITGAL integrin, alpha L (antigen CD11A (p180), lymphocyte function-associated antigen 1; alpha polypeptide)".
  2. Lu C, Takagi J, Springer TA (May 2001). "Association of the membrane proximal regions of the alpha and beta subunit cytoplasmic domains constrains an integrin in the inactive state". J. Biol. Chem. 276 (18): 14642–8. doi:10.1074/jbc.M100600200. PMID 11279101.
  3. Shimaoka M, Xiao T, Liu JH, Yang Y, Dong Y, Jun CD, McCormack A, Zhang R, Joachimiak A, Takagi J, Wang JH, Springer TA (Jan 2003). "Structures of the alpha L I domain and its complex with ICAM-1 reveal a shape-shifting pathway for integrin regulation". Cell. 112 (1): 99–111. doi:10.1016/S0092-8674(02)01257-6. PMID 12526797.
  4. Yusuf-Makagiansar H, Makagiansar IT, Hu Y, Siahaan TJ (Dec 2001). "Synergistic inhibitory activity of alpha- and beta-LFA-1 peptides on LFA-1/ICAM-1 interaction". Peptides. 22 (12): 1955–62. doi:10.1016/S0196-9781(01)00546-0. PMID 11786177.

Further reading

External links