Laminin, beta 1: Difference between revisions

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{{Infobox_gene}}
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'''Laminin subunit beta-1''' is a [[protein]] that in humans is encoded by the ''LAMB1'' [[gene]].<ref name="pmid2563160">{{cite journal |vauthors=Ikonen J, Pikkarainen T, Savolainen ER, Tryggvason K | title = A Hpa I polymorphism in the human laminin B1 chain gene on 7q22 | journal = Nucleic Acids Res | volume = 17 | issue = 1 | pages = 473 |date=Feb 1989 | pmid = 2563160 | pmc = 331592 | doi =10.1093/nar/17.1.473 }}</ref><ref name="pmid2704655">{{cite journal |vauthors=Roche KB, Moore JW, Surana RB, Wilson BE | title = Aortic root dilatation associated with partial trisomy 7(q31.2----qter) | journal = Pediatr Cardiol | volume = 10 | issue = 1 | pages = 53–5 |date=May 1989 | pmid = 2704655 | pmc = | doi =10.1007/BF02328637  }}</ref><ref name="pmid1864606">{{cite journal |vauthors=Bonneau D, Huret JL, Godeau G, Couet D, Putterman M, Tanzer J, Babin P, Larregue M | title = Recurrent ctb(7)(q31.3) and possible laminin involvement in a neonatal cutis laxa with a Marfan phenotype | journal = Hum Genet | volume = 87 | issue = 3 | pages = 317–9 |date=Sep 1991 | pmid = 1864606 | pmc =  | doi =  10.1007/bf00200911}}</ref><ref name="entrez">{{cite web | title = Entrez Gene: LAMB1 laminin, beta 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3912| accessdate = }}</ref>
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{{GNF_Protein_box
| image =
| image_source =
| PDB =  
| Name = Laminin, beta 1
| HGNCid = 6486
| Symbol = LAMB1
| AltSymbols =; CLM; MGC142015
| OMIM = 150240
| ECnumber =
| Homologene = 1722
| MGIid = 96743
| GeneAtlas_image1 = PBB_GE_LAMB1_201505_at_tn.png
| GeneAtlas_image2 = PBB_GE_LAMB1_211651_s_at_tn.png
  | Function = {{GNF_GO|id=GO:0005201 |text = extracellular matrix structural constituent}} {{GNF_GO|id=GO:0019899 |text = enzyme binding}}
| Component = {{GNF_GO|id=GO:0005604 |text = basement membrane}} {{GNF_GO|id=GO:0005606 |text = laminin-1 complex}} {{GNF_GO|id=GO:0005607 |text = laminin-2 complex}} {{GNF_GO|id=GO:0043257 |text = laminin-8 complex}} {{GNF_GO|id=GO:0043259 |text = laminin-10 complex}} {{GNF_GO|id=GO:0048471 |text = perinuclear region of cytoplasm}}
| Process = {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0007566 |text = embryo implantation}} {{GNF_GO|id=GO:0030335 |text = positive regulation of cell migration}} {{GNF_GO|id=GO:0031175 |text = neurite development}} {{GNF_GO|id=GO:0042476 |text = odontogenesis}} {{GNF_GO|id=GO:0050679 |text = positive regulation of epithelial cell proliferation}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 3912
    | Hs_Ensembl = ENSG00000091136
    | Hs_RefseqProtein = NP_002282
    | Hs_RefseqmRNA = NM_002291
    | Hs_GenLoc_db =   
    | Hs_GenLoc_chr = 7
    | Hs_GenLoc_start = 107351499
    | Hs_GenLoc_end = 107431040
    | Hs_Uniprot = P07942
    | Mm_EntrezGene = 16777
    | Mm_Ensembl = ENSMUSG00000002900
    | Mm_RefseqmRNA = NM_008482
    | Mm_RefseqProtein = NP_032508
    | Mm_GenLoc_db =   
    | Mm_GenLoc_chr = 12
    | Mm_GenLoc_start = 31851443
    | Mm_GenLoc_end = 31915700
    | Mm_Uniprot = Q0V927
  }}
}}
'''Laminin, beta 1''', also known as '''LAMB1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: LAMB1 laminin, beta 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3912| accessdate = }}</ref>


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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = Laminins, a family of extracellular matrix glycoproteins, are the major noncollagenous constituent of basement membranes.  They have been implicated in a wide variety of biological processes including cell adhesion, differentiation, migration, signaling, neurite outgrowth and metastasis.  Laminins are composed of 3 non identical chains: laminin alpha, beta and gamma (formerly A, B1, and B2, respectively) and they form a cruciform structure consisting of 3 short arms, each formed by a different chain, and a long arm composed of all 3 chains.  Each laminin chain is a multidomain protein encoded by a distinct gene.  Several isoforms of each chain have been described.  Different alpha, beta and gamma chain isomers combine to give rise to different heterotrimeric laminin isoforms which are designated by Arabic numerals in the order of their discovery, i.e. alpha1beta1gamma1 heterotrimer is laminin 1.  The biological functions of the different chains and trimer molecules are largely unknown, but some of the chains have been shown to differ with respect to their tissue distribution, presumably reflecting diverse functions in vivo.  This gene encodes the beta chain isoform laminin, beta 1.  The beta 1 chain has 7 structurally distinct domains which it shares with other beta chain isomers.  The C-terminal helical region containing domains I and II are separated by domain alpha, domains III and V contain several EGF-like repeats, and domains IV and VI have a globular conformation.  Laminin, beta 1 is expressed in most tissues that produce basement membranes, and is one of the 3 chains constituting laminin 1, the first laminin isolated from Engelbreth-Holm-Swarm (EHS) tumor.  A sequence in the beta 1 chain that is involved in cell attachment, chemotaxis, and binding to the laminin receptor was identified and shown to have the capacity to inhibit metastasis.<ref name="entrez">{{cite web | title = Entrez Gene: LAMB1 laminin, beta 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3912| accessdate = }}</ref>
| summary_text = [[Laminin]]s, a family of extracellular matrix glycoproteins, are the major noncollagenous constituent of basement membranes.  They have been implicated in a wide variety of biological processes including cell adhesion, differentiation, migration, signaling, neurite outgrowth and metastasis.  Laminins are composed of 3 non identical chains: laminin alpha, beta and gamma (formerly A, B1, and B2, respectively) and they form a cruciform structure consisting of 3 short arms, each formed by a different chain, and a long arm composed of all 3 chains.  Each laminin chain is a multidomain protein encoded by a distinct gene.  Several isoforms of each chain have been described.  Different alpha, beta and gamma chain isomers combine to give rise to different heterotrimeric laminin isoforms, which are designated by Arabic numerals in the order of their discovery, i.e. alpha1beta1gamma1 heterotrimer is laminin 1.  The biological functions of the different chains and trimer molecules are largely unknown, but some of the chains have been shown to differ with respect to their tissue distribution, presumably reflecting diverse functions in vivo.  This gene encodes the beta chain isoform laminin, beta 1.  The beta 1 chain has 7 structurally distinct domains, which it shares with other beta chain isomers.  The C-terminal helical region containing domains I and II are separated by domain alpha, domains III and V contain several EGF-like repeats, and domains IV and VI have a globular conformation.  Laminin, beta 1 is expressed in most tissues that produce basement membranes, and is one of the 3 chains constituting laminin 1, the first laminin isolated from Engelbreth-Holm-Swarm (EHS) tumor.  A sequence in the beta 1 chain that is involved in cell attachment, chemotaxis, and binding to the laminin receptor was identified and shown to have the capacity to inhibit metastasis.<ref name="entrez" />
}}
}}
5′-UTR of Laminin-B1 harbors IRES ([[internal ribosome entry site]]) between −293 and −1 upstream of the start codon.  IRES are involved in cancer malignancy. [Petz 2011 [http://nar.oxfordjournals.org/content/40/1/290.full]


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal | author=Ljubimova JY, Fujita M, Khazenzon NM, ''et al.'' |title=Changes in laminin isoforms associated with brain tumor invasion and angiogenesis. |journal=Front. Biosci. |volume=11 |issue=  |pages= 81-8 |year= 2006 |pmid= 16146715 |doi= }}
*{{cite journal   |vauthors=Ljubimova JY, Fujita M, Khazenzon NM, etal |title=Changes in laminin isoforms associated with brain tumor invasion and angiogenesis. |journal=Front. Biosci. |volume=11 |issue=  1|pages= 81–8 |year= 2006 |pmid= 16146715 |doi=10.2741/1781 |pmc=3506377}}
*{{cite journal  | author=Bonneau D, Huret JL, Godeau G, ''et al.'' |title=Recurrent ctb(7)(q31.3) and possible laminin involvement in a neonatal cutis laxa with a Marfan phenotype. |journal=Hum. Genet. |volume=87 |issue= 3 |pages= 317-9 |year= 1991 |pmid= 1864606 |doi=  }}
*{{cite journal  |vauthors=Vuolteenaho R, Chow LT, Tryggvason K |title=Structure of the human laminin B1 chain gene. |journal=J. Biol. Chem. |volume=265 |issue= 26 |pages= 15611–6 |year= 1990 |pmid= 1975589 |doi=  }}
*{{cite journal | author=Vuolteenaho R, Chow LT, Tryggvason K |title=Structure of the human laminin B1 chain gene. |journal=J. Biol. Chem. |volume=265 |issue= 26 |pages= 15611-6 |year= 1990 |pmid= 1975589 |doi=  }}
*{{cite journal   |vauthors=Sasaki M, Kato S, Kohno K, etal |title=Sequence of the cDNA encoding the laminin B1 chain reveals a multidomain protein containing cysteine-rich repeats. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 4 |pages= 935–9 |year= 1987 |pmid= 3493487 |doi=10.1073/pnas.84.4.935  | pmc=304334 }}
*{{cite journal | author=Ikonen J, Pikkarainen T, Savolainen ER, Tryggvason K |title=A Hpa I polymorphism in the human laminin B1 chain gene on 7q22. |journal=Nucleic Acids Res. |volume=17 |issue= 1 |pages= 473 |year= 1989 |pmid= 2563160 |doi=  }}
*{{cite journal   |vauthors=Pikkarainen T, Eddy R, Fukushima Y, etal |title=Human laminin B1 chain. A multidomain protein with gene (LAMB1) locus in the q22 region of chromosome 7. |journal=J. Biol. Chem. |volume=262 |issue= 22 |pages= 10454–62 |year= 1987 |pmid= 3611077 |doi=  }}
*{{cite journal | author=Roche KB, Moore JW, Surana RB, Wilson BE |title=Aortic root dilatation associated with partial trisomy 7(q31.2----qter). |journal=Pediatric cardiology |volume=10 |issue= 1 |pages= 53-5 |year= 1989 |pmid= 2704655 |doi=  }}
*{{cite journal   |vauthors=Jaye M, Modi WS, Ricca GA, etal |title=Isolation of a cDNA clone for the human laminin-B1 chain and its gene localization. |journal=Am. J. Hum. Genet. |volume=41 |issue= 4 |pages= 605–15 |year= 1987 |pmid= 3661559 |doi= | pmc=1684322 }}
*{{cite journal | author=Sasaki M, Kato S, Kohno K, ''et al.'' |title=Sequence of the cDNA encoding the laminin B1 chain reveals a multidomain protein containing cysteine-rich repeats. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 4 |pages= 935-9 |year= 1987 |pmid= 3493487 |doi= }}
*{{cite journal   |vauthors=Burgeson RE, Chiquet M, Deutzmann R, etal |title=A new nomenclature for the laminins. |journal=Matrix Biol. |volume=14 |issue= 3 |pages= 209–11 |year= 1994 |pmid= 7921537 |doi=10.1016/0945-053X(94)90184-8  }}
*{{cite journal  | author=Pikkarainen T, Eddy R, Fukushima Y, ''et al.'' |title=Human laminin B1 chain. A multidomain protein with gene (LAMB1) locus in the q22 region of chromosome 7. |journal=J. Biol. Chem. |volume=262 |issue= 22 |pages= 10454-62 |year= 1987 |pmid= 3611077 |doi=  }}
*{{cite journal  |vauthors=Lohi J, Leivo I, Franssila K, Virtanen I |title=Changes in the distribution of integrins and their basement membrane ligands during development of human thyroid follicular epithelium. |journal=Histochem. J. |volume=29 |issue= 4 |pages= 337–45 |year= 1997 |pmid= 9184849 |doi=10.1023/A:1026482700109 }}
*{{cite journal | author=Jaye M, Modi WS, Ricca GA, ''et al.'' |title=Isolation of a cDNA clone for the human laminin-B1 chain and its gene localization. |journal=Am. J. Hum. Genet. |volume=41 |issue= 4 |pages= 605-15 |year= 1987 |pmid= 3661559 |doi=  }}
*{{cite journal   |vauthors=Taylor J, Muntoni F, Robb S, etal |title=Early onset autosomal dominant myopathy with rigidity of the spine: a possible role for laminin beta 1? |journal=Neuromuscul. Disord. |volume=7 |issue= 4 |pages= 211–6 |year= 1997 |pmid= 9196901 |doi=10.1016/S0960-8966(97)00461-6 }}
*{{cite journal | author=Burgeson RE, Chiquet M, Deutzmann R, ''et al.'' |title=A new nomenclature for the laminins. |journal=Matrix Biol. |volume=14 |issue= 3 |pages= 209-11 |year= 1994 |pmid= 7921537 |doi= }}
*{{cite journal   |vauthors=Sewry CA, D'Alessandro M, Wilson LA, etal |title=Expression of laminin chains in skin in merosin-deficient congenital muscular dystrophy. |journal=Neuropediatrics |volume=28 |issue= 4 |pages= 217–22 |year= 1997 |pmid= 9309712 |doi=10.1055/s-2007-973703  }}
*{{cite journal | author=Lohi J, Leivo I, Franssila K, Virtanen I |title=Changes in the distribution of integrins and their basement membrane ligands during development of human thyroid follicular epithelium. |journal=Histochem. J. |volume=29 |issue= 4 |pages= 337-45 |year= 1997 |pmid= 9184849 |doi=  }}
*{{cite journal   |vauthors=Mahida YR, Beltinger J, Makh S, etal |title=Adult human colonic subepithelial myofibroblasts express extracellular matrix proteins and cyclooxygenase-1 and -2. |journal=Am. J. Physiol. |volume=273 |issue= 6 Pt 1 |pages= G1341–8 |year= 1998 |pmid= 9435560 |doi=  }}
*{{cite journal  | author=Taylor J, Muntoni F, Robb S, ''et al.'' |title=Early onset autosomal dominant myopathy with rigidity of the spine: a possible role for laminin beta 1? |journal=Neuromuscul. Disord. |volume=7 |issue= 4 |pages= 211-6 |year= 1997 |pmid= 9196901 |doi=  }}
*{{cite journal  |vauthors=O'Grady P, Thai TC, Saito H |title=The laminin-nidogen complex is a ligand for a specific splice isoform of the transmembrane protein tyrosine phosphatase LAR. |journal=J. Cell Biol. |volume=141 |issue= 7 |pages= 1675–84 |year= 1998 |pmid= 9647658 |doi=10.1083/jcb.141.7.1675  | pmc=2133008 }}
*{{cite journal | author=Sewry CA, D'Alessandro M, Wilson LA, ''et al.'' |title=Expression of laminin chains in skin in merosin-deficient congenital muscular dystrophy. |journal=Neuropediatrics |volume=28 |issue= 4 |pages= 217-22 |year= 1997 |pmid= 9309712 |doi=  }}
*{{cite journal   |vauthors=Koch M, Olson PF, Albus A, etal |title=Characterization and expression of the laminin gamma3 chain: a novel, non-basement membrane-associated, laminin chain. |journal=J. Cell Biol. |volume=145 |issue= 3 |pages= 605–18 |year= 1999 |pmid= 10225960 |doi=10.1083/jcb.145.3.605  | pmc=2185082 }}
*{{cite journal | author=Mahida YR, Beltinger J, Makh S, ''et al.'' |title=Adult human colonic subepithelial myofibroblasts express extracellular matrix proteins and cyclooxygenase-1 and -2. |journal=Am. J. Physiol. |volume=273 |issue= 6 Pt 1 |pages= G1341-8 |year= 1998 |pmid= 9435560 |doi=  }}
*{{cite journal   |vauthors=Merlini L, Villanova M, Sabatelli P, etal |title=Decreased expression of laminin beta 1 in chromosome 21-linked Bethlem myopathy. |journal=Neuromuscul. Disord. |volume=9 |issue= 5 |pages= 326–9 |year= 1999 |pmid= 10407855 |doi=10.1016/S0960-8966(99)00022-X }}
*{{cite journal | author=O'Grady P, Thai TC, Saito H |title=The laminin-nidogen complex is a ligand for a specific splice isoform of the transmembrane protein tyrosine phosphatase LAR. |journal=J. Cell Biol. |volume=141 |issue= 7 |pages= 1675-84 |year= 1998 |pmid= 9647658 |doi=  }}
*{{cite journal   |vauthors=Kikkawa Y, Sanzen N, Fujiwara H, etal |title=Integrin binding specificity of laminin-10/11: laminin-10/11 are recognized by alpha 3 beta 1, alpha 6 beta 1 and alpha 6 beta 4 integrins. | series=113 |journal=J. Cell Sci. |volume=( Pt 5) |issue= |pages= 869–76 |year= 2000 |pmid= 10671376 |doi=  }}
*{{cite journal | author=Koch M, Olson PF, Albus A, ''et al.'' |title=Characterization and expression of the laminin gamma3 chain: a novel, non-basement membrane-associated, laminin chain. |journal=J. Cell Biol. |volume=145 |issue= 3 |pages= 605-18 |year= 1999 |pmid= 10225960 |doi= }}
*{{cite journal   |vauthors=Hirosaki T, Mizushima H, Tsubota Y, etal |title=Structural requirement of carboxyl-terminal globular domains of laminin alpha 3 chain for promotion of rapid cell adhesion and migration by laminin-5. |journal=J. Biol. Chem. |volume=275 |issue= 29 |pages= 22495–502 |year= 2000 |pmid= 10801807 |doi= 10.1074/jbc.M001326200 }}
*{{cite journal | author=Merlini L, Villanova M, Sabatelli P, ''et al.'' |title=Decreased expression of laminin beta 1 in chromosome 21-linked Bethlem myopathy. |journal=Neuromuscul. Disord. |volume=9 |issue= 5 |pages= 326-9 |year= 1999 |pmid= 10407855 |doi= }}
*{{cite journal   |vauthors=Champliaud MF, Virtanen I, Tiger CF, etal |title=Posttranslational modifications and beta/gamma chain associations of human laminin alpha1 and laminin alpha5 chains: purification of laminin-3 from placenta. |journal=Exp. Cell Res. |volume=259 |issue= 2 |pages= 326–35 |year= 2000 |pmid= 10964500 |doi= 10.1006/excr.2000.4980 }}
*{{cite journal | author=Kikkawa Y, Sanzen N, Fujiwara H, ''et al.'' |title=Integrin binding specificity of laminin-10/11: laminin-10/11 are recognized by alpha 3 beta 1, alpha 6 beta 1 and alpha 6 beta 4 integrins. |journal=J. Cell. Sci. |volume=113 ( Pt 5) |issue= |pages= 869-76 |year= 2000 |pmid= 10671376 |doi=  }}
*{{cite journal   |vauthors=Pedraza C, Geberhiwot T, Ingerpuu S, etal |title=Monocytic cells synthesize, adhere to, and migrate on laminin-8 (alpha 4 beta 1 gamma 1). |journal=J. Immunol. |volume=165 |issue= 10 |pages= 5831–8 |year= 2000 |pmid= 11067943 |doi=  10.4049/jimmunol.165.10.5831}}
*{{cite journal  | author=Hirosaki T, Mizushima H, Tsubota Y, ''et al.'' |title=Structural requirement of carboxyl-terminal globular domains of laminin alpha 3 chain for promotion of rapid cell adhesion and migration by laminin-5. |journal=J. Biol. Chem. |volume=275 |issue= 29 |pages= 22495-502 |year= 2000 |pmid= 10801807 |doi= 10.1074/jbc.M001326200 }}
*{{cite journal  | author=Champliaud MF, Virtanen I, Tiger CF, ''et al.'' |title=Posttranslational modifications and beta/gamma chain associations of human laminin alpha1 and laminin alpha5 chains: purification of laminin-3 from placenta. |journal=Exp. Cell Res. |volume=259 |issue= 2 |pages= 326-35 |year= 2000 |pmid= 10964500 |doi= 10.1006/excr.2000.4980 }}
*{{cite journal  | author=Pedraza C, Geberhiwot T, Ingerpuu S, ''et al.'' |title=Monocytic cells synthesize, adhere to, and migrate on laminin-8 (alpha 4 beta 1 gamma 1). |journal=J. Immunol. |volume=165 |issue= 10 |pages= 5831-8 |year= 2000 |pmid= 11067943 |doi=  }}
}}
}}
{{refend}}
{{refend}}


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{{Fibrous proteins}}
 
[[Category:Laminins]]

Latest revision as of 20:15, 8 November 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
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View/Edit Human

Laminin subunit beta-1 is a protein that in humans is encoded by the LAMB1 gene.[1][2][3][4]

Laminins, a family of extracellular matrix glycoproteins, are the major noncollagenous constituent of basement membranes. They have been implicated in a wide variety of biological processes including cell adhesion, differentiation, migration, signaling, neurite outgrowth and metastasis. Laminins are composed of 3 non identical chains: laminin alpha, beta and gamma (formerly A, B1, and B2, respectively) and they form a cruciform structure consisting of 3 short arms, each formed by a different chain, and a long arm composed of all 3 chains. Each laminin chain is a multidomain protein encoded by a distinct gene. Several isoforms of each chain have been described. Different alpha, beta and gamma chain isomers combine to give rise to different heterotrimeric laminin isoforms, which are designated by Arabic numerals in the order of their discovery, i.e. alpha1beta1gamma1 heterotrimer is laminin 1. The biological functions of the different chains and trimer molecules are largely unknown, but some of the chains have been shown to differ with respect to their tissue distribution, presumably reflecting diverse functions in vivo. This gene encodes the beta chain isoform laminin, beta 1. The beta 1 chain has 7 structurally distinct domains, which it shares with other beta chain isomers. The C-terminal helical region containing domains I and II are separated by domain alpha, domains III and V contain several EGF-like repeats, and domains IV and VI have a globular conformation. Laminin, beta 1 is expressed in most tissues that produce basement membranes, and is one of the 3 chains constituting laminin 1, the first laminin isolated from Engelbreth-Holm-Swarm (EHS) tumor. A sequence in the beta 1 chain that is involved in cell attachment, chemotaxis, and binding to the laminin receptor was identified and shown to have the capacity to inhibit metastasis.[4]

5′-UTR of Laminin-B1 harbors IRES (internal ribosome entry site) between −293 and −1 upstream of the start codon. IRES are involved in cancer malignancy. [Petz 2011 [2]

References

  1. ↑ Ikonen J, Pikkarainen T, Savolainen ER, Tryggvason K (Feb 1989). "A Hpa I polymorphism in the human laminin B1 chain gene on 7q22". Nucleic Acids Res. 17 (1): 473. doi:10.1093/nar/17.1.473. PMC 331592. PMID 2563160.
  2. ↑ Roche KB, Moore JW, Surana RB, Wilson BE (May 1989). "Aortic root dilatation associated with partial trisomy 7(q31.2----qter)". Pediatr Cardiol. 10 (1): 53–5. doi:10.1007/BF02328637. PMID 2704655.
  3. ↑ Bonneau D, Huret JL, Godeau G, Couet D, Putterman M, Tanzer J, Babin P, Larregue M (Sep 1991). "Recurrent ctb(7)(q31.3) and possible laminin involvement in a neonatal cutis laxa with a Marfan phenotype". Hum Genet. 87 (3): 317–9. doi:10.1007/bf00200911. PMID 1864606.
  4. ↑ 4.0 4.1 "Entrez Gene: LAMB1 laminin, beta 1".

Further reading


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