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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
'''Lysyl oxidase homolog 2''' is an [[enzyme]] that in humans is encoded by the ''LOXL2'' [[gene]].<ref name="pmid9722957">{{cite journal | vauthors = Jourdan-Le Saux C, Le Saux O, Donlon T, Boyd CD, Csiszar K | title = The human lysyl oxidase-related gene (LOXL2) maps between markers D8S280 and D8S278 on chromosome 8p21.2-p21.3 | journal = Genomics | volume = 51 | issue = 2 | pages = 305–7 | date = July 1998 | pmid = 9722957 | pmc =  | doi = 10.1006/geno.1998.5356 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: LOXL2 lysyl oxidase-like 2| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4017| accessdate = }}</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
This gene encodes a member of the [[lysyl oxidase]] gene family. The prototypic member of the family is essential to the [[biogenesis]] of connective tissue, encoding an extracellular copper-dependent amine oxidase that catalyses the first step in the formation of crosslinks in [[collagen]]s and [[elastin]]. A highly conserved amino acid sequence at the [[C-terminus]] end appears to be sufficient for amine oxidase activity, suggesting that each family member may retain this function. The [[N-terminus]] is poorly conserved and may impart additional roles in developmental regulation, senescence, tumor suppression, cell growth control, and [[chemotaxis]] to each member of the family.<ref name="entrez" />
| image =
| image_source =
| PDB =  
| Name = Lysyl oxidase-like 2
| HGNCid = 6666
| Symbol = LOXL2
| AltSymbols =; LOR2; WS9-14
| OMIM = 606663
| ECnumber = 
| Homologene = 1742
| MGIid = 2137913
| GeneAtlas_image1 = PBB_GE_LOXL2_202998_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_LOXL2_202997_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_LOXL2_202999_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004720 |text = protein-lysine 6-oxidase activity}} {{GNF_GO|id=GO:0005044 |text = scavenger receptor activity}} {{GNF_GO|id=GO:0005507 |text = copper ion binding}} {{GNF_GO|id=GO:0009055 |text = electron carrier activity}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005615 |text = extracellular space}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006464 |text = protein modification process}} {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0007568 |text = aging}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 4017
    | Hs_Ensembl = ENSG00000134013
    | Hs_RefseqProtein = NP_002309
    | Hs_RefseqmRNA = NM_002318
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 8
    | Hs_GenLoc_start = 23211501
    | Hs_GenLoc_end = 23281809
    | Hs_Uniprot = Q9Y4K0
    | Mm_EntrezGene = 94352
    | Mm_Ensembl = ENSMUSG00000034205
    | Mm_RefseqmRNA = XM_985144
    | Mm_RefseqProtein = XP_990238
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 14
    | Mm_GenLoc_start = 68344248
    | Mm_GenLoc_end = 68428800
    | Mm_Uniprot = Q5PR71
  }}
}}
'''Lysyl oxidase-like 2''', also known as '''LOXL2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: LOXL2 lysyl oxidase-like 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4017| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
LOXL2 can also crosslink [[collagen type IV]] and hence influence the sprouting of new [[blood]] vessels.<ref>{{cite journal | vauthors = Bignon M, Pichol-Thievend C, Hardouin J, Malbouyres M, Bréchot N, Nasciutti L, Barret A, Teillon J, Guillon E, Etienne E, Caron M, Joubert-Caron R, Monnot C, Ruggiero F, Muller L, Germain S | title = Lysyl oxidase-like protein-2 regulates sprouting angiogenesis and type IV collagen assembly in the endothelial basement membrane | journal = Blood | volume = 118 | issue = | pages = 3979–89 | year = 2011 | pmid = 21835952 | doi = 10.1182/blood-2010-10-313296 }}</ref>
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a member of the lysyl oxidase gene family. The prototypic member of the family is essential to the biogenesis of connective tissue, encoding an extracellular copper-dependent amine oxidase that catalyses the first step in the formation of crosslinks in collagens and elastin. A highly conserved amino acid sequence at the C-terminus end appears to be sufficient for amine oxidase activity, suggesting that each family member may retain this function. The N-terminus is poorly conserved and may impart additional roles in developmental regulation, senescence, tumor suppression, cell growth control, and chemotaxis to each member of the family.<ref name="entrez">{{cite web | title = Entrez Gene: LOXL2 lysyl oxidase-like 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4017| accessdate = }}</ref>
}}


==References==
== Clinical significance ==
{{reflist|2}}
LOXL2 is an enzyme that is up-regulated in several types of cancer and is associated with a poorer prognosis.<ref name="pmid22453058">{{cite journal | vauthors = Nishioka T, Eustace A, West C | title = Lysyl oxidase: from basic science to future cancer treatment | journal = Cell Struct. Funct. | volume = 37 | issue = 1 | pages = 75–80 | year = 2012 | pmid = 22453058 | doi = 10.1247/csf.11015| url = }}</ref><ref name="pmid23030485">{{cite journal | vauthors = Cano A, Santamaría PG, Moreno-Bueno G | title = LOXL2 in epithelial cell plasticity and tumor progression | journal = Future Oncol | volume = 8 | issue = 9 | pages = 1095–108 | year = 2012 | pmid = 23030485 | doi = 10.2217/fon.12.105 }}</ref> LOXL2 changes the structure of [[histone]]s (proteins that are attached to DNA)<ref>{{cite journal | vauthors = Herranz N, Dave N, Millanes-Romero A, Morey L, Díaz VM, Lórenz-Fonfría V, Gutierrez-Gallego R, Jerónimo C, Di Croce L, García de Herreros A, Peiró S | title = Lysyl oxidase-like 2 deaminates lysine 4 in histone H3 | journal = Molecular Cell | volume = 46 | issue = 3 | pages = 369–376 | year = 2012 | pmid = 22483618 | doi = 10.1016/j.molcel.2012.03.002 }}</ref> and thus changes the shape of the cells, making it easier for the cancer cells to [[metastasis|metastasize]].<ref>{{cite journal | vauthors = Moreno-Bueno G, Salvador F, Martín A, Floristán A, Cuevas EP, Santos V, Montes A, Morales S, Castilla MA, Rojo-Sebastián A, Martínez A, Hardisson D, Csiszar K, Portillo F, Peinado H, Palacios J, Cano A | title = Lysyl oxidase-like 2 (LOXL2), a new regulator of cell polarity required for metastatic dissemination of basal-like breast carcinomas | journal = EMBO Mol Med | volume = 3 | issue = 9 | pages = 528–544 | year = 2011 | pmid = 21732535 | doi = 10.1002/emmm.201100156 | pmc=3377095}}</ref>
==Further reading==
 
An antibody that inhibits the activity of LOXL2, [[simtuzumab]] and is currently in clinical trials for the treatment of several types of cancer and fibrotic diseases such as [[liver fibrosis]].<ref name="urlSearch of: simtuzumab - List Results - ClinicalTrials.gov">{{cite web | url = https://www.clinicaltrials.gov/ct2/results?term=simtuzumab&Search=Search | title = Search of: simtuzumab - List Results  | format = | work = ClinicalTrials.gov | accessdate = 25 February 2015  }}</ref>
 
== See also ==
* [[LOXL1]]
* [[LOXL3]]
* [[LOXL4]]
 
== References ==
{{reflist}}
{{Clear}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Csiszar K | title = Lysyl oxidases: a novel multifunctional amine oxidase family | journal = Progress in Nucleic Acid Research and Molecular Biology | volume = 70 | issue =  | pages = 1–32 | year = 2001 | pmid = 11642359 | doi = 10.1016/S0079-6603(01)70012-8 | isbn = 978-0-12-540070-1 | series = Progress in Nucleic Acid Research and Molecular Biology }}
| citations =
* {{cite journal | vauthors = Molnar J, Fong KS, He QP, Hayashi K, Kim Y, Fong SF, Fogelgren B, Szauter KM, Mink M, Csiszar K | title = Structural and functional diversity of lysyl oxidase and the LOX-like proteins | journal = Biochimica et Biophysica Acta | volume = 1647 | issue = 1–2 | pages = 220–4 | date = April 2003 | pmid = 12686136 | doi = 10.1016/s1570-9639(03)00053-0 }}
*{{cite journal | author=Csiszar K |title=Lysyl oxidases: a novel multifunctional amine oxidase family. |journal=Prog. Nucleic Acid Res. Mol. Biol. |volume=70 |issue=  |pages= 1-32 |year= 2001 |pmid= 11642359 |doi= }}
* {{cite journal | vauthors = Maruyama K, Sugano S | title = Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides | journal = Gene | volume = 138 | issue = 1–2 | pages = 171–4 | date = Jan 1994 | pmid = 8125298 | doi = 10.1016/0378-1119(94)90802-8 }}
*{{cite journal | author=Molnar J, Fong KS, He QP, ''et al.'' |title=Structural and functional diversity of lysyl oxidase and the LOX-like proteins. |journal=Biochim. Biophys. Acta |volume=1647 |issue= 1-2 |pages= 220-4 |year= 2003 |pmid= 12686136 |doi= }}
* {{cite journal | vauthors = Saito H, Papaconstantinou J, Sato H, Goldstein S | title = Regulation of a novel gene encoding a lysyl oxidase-related protein in cellular adhesion and senescence | journal = The Journal of Biological Chemistry | volume = 272 | issue = 13 | pages = 8157–60 | date = March 1997 | pmid = 9079631 | doi = 10.1074/jbc.272.13.8157 }}
*{{cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi= }}
* {{cite journal | vauthors = Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S | title = Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library | journal = Gene | volume = 200 | issue = 1–2 | pages = 149–56 | date = October 1997 | pmid = 9373149 | doi = 10.1016/S0378-1119(97)00411-3 }}
*{{cite journal | author=Saito H, Papaconstantinou J, Sato H, Goldstein S |title=Regulation of a novel gene encoding a lysyl oxidase-related protein in cellular adhesion and senescence. |journal=J. Biol. Chem. |volume=272 |issue= 13 |pages= 8157-60 |year= 1997 |pmid= 9079631 |doi= }}
* {{cite journal | vauthors = Jourdan-Le Saux C, Tronecker H, Bogic L, Bryant-Greenwood GD, Boyd CD, Csiszar K | title = The LOXL2 gene encodes a new lysyl oxidase-like protein and is expressed at high levels in reproductive tissues | journal = The Journal of Biological Chemistry | volume = 274 | issue = 18 | pages = 12939–44 | date = April 1999 | pmid = 10212285 | doi = 10.1074/jbc.274.18.12939 }}
*{{cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi= }}
* {{cite journal | vauthors = Hein S, Yamamoto SY, Okazaki K, Jourdan-LeSaux C, Csiszar K, Bryant-Greenwood GD | title = Lysyl oxidases: expression in the fetal membranes and placenta | journal = Placenta | volume = 22 | issue = 1 | pages = 49–57 | date = Jan 2001 | pmid = 11162352 | doi = 10.1053/plac.2000.0580 }}
*{{cite journal  | author=Jourdan-Le Saux C, Le Saux O, Donlon T, ''et al.'' |title=The human lysyl oxidase-related gene (LOXL2) maps between markers D8S280 and D8S278 on chromosome 8p21.2-p21.3. |journal=Genomics |volume=51 |issue= 2 |pages= 305-7 |year= 1998 |pmid= 9722957 |doi= 10.1006/geno.1998.5356 }}
* {{cite journal | vauthors = Akiri G, Sabo E, Dafni H, Vadasz Z, Kartvelishvily Y, Gan N, Kessler O, Cohen T, Resnick M, Neeman M, Neufeld G | title = Lysyl oxidase-related protein-1 promotes tumor fibrosis and tumor progression in vivo | journal = Cancer Research | volume = 63 | issue = 7 | pages = 1657–66 | date = April 2003 | pmid = 12670920 | doi =  }}
*{{cite journal | author=Jourdan-Le Saux C, Tronecker H, Bogic L, ''et al.'' |title=The LOXL2 gene encodes a new lysyl oxidase-like protein and is expressed at high levels in reproductive tissues. |journal=J. Biol. Chem. |volume=274 |issue= 18 |pages= 12939-44 |year= 1999 |pmid= 10212285 |doi= }}
* {{cite journal | vauthors = Rost T, Pyritz V, Rathcke IO, Görögh T, Dünne AA, Werner JA | title = Reduction of LOX- and LOXL2-mRNA expression in head and neck squamous cell carcinomas | journal = Anticancer Research | volume = 23 | issue = 2B | pages = 1565–73 | year = 2003 | pmid = 12820424 | doi =  }}
*{{cite journal | author=Hein S, Yamamoto SY, Okazaki K, ''et al.'' |title=Lysyl oxidases: expression in the fetal membranes and placenta. |journal=Placenta |volume=22 |issue= 1 |pages= 49-57 |year= 2001 |pmid= 11162352 |doi= 10.1053/plac.2000.0580 }}
* {{cite journal | vauthors = Vadasz Z, Kessler O, Akiri G, Gengrinovitch S, Kagan HM, Baruch Y, Izhak OB, Neufeld G | title = Abnormal deposition of collagen around hepatocytes in Wilson's disease is associated with hepatocyte specific expression of lysyl oxidase and lysyl oxidase like protein-2 | journal = Journal of Hepatology | volume = 43 | issue = 3 | pages = 499–507 | date = September 2005 | pmid = 16023247 | doi = 10.1016/j.jhep.2005.02.052 }}
*{{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 }}
* {{cite journal | vauthors = Peinado H, Del Carmen Iglesias-de la Cruz M, Olmeda D, Csiszar K, Fong KS, Vega S, Nieto MA, Cano A, Portillo F | title = A molecular role for lysyl oxidase-like 2 enzyme in snail regulation and tumor progression | journal = The EMBO Journal | volume = 24 | issue = 19 | pages = 3446–58 | date = October 2005 | pmid = 16096638 | pmc = 1276164 | doi = 10.1038/sj.emboj.7600781 }}
*{{cite journal  | author=Akiri G, Sabo E, Dafni H, ''et al.'' |title=Lysyl oxidase-related protein-1 promotes tumor fibrosis and tumor progression in vivo. |journal=Cancer Res. |volume=63 |issue= 7 |pages= 1657-66 |year= 2003 |pmid= 12670920 |doi=  }}
* {{cite journal | vauthors = Akagawa H, Narita A, Yamada H, Tajima A, Krischek B, Kasuya H, Hori T, Kubota M, Saeki N, Hata A, Mizutani T, Inoue I | title = Systematic screening of lysyl oxidase-like (LOXL) family genes demonstrates that LOXL2 is a susceptibility gene to intracranial aneurysms | journal = Human Genetics | volume = 121 | issue = 3–4 | pages = 377–87 | date = May 2007 | pmid = 17287949 | doi = 10.1007/s00439-007-0333-3 }}
*{{cite journal | author=Rost T, Pyritz V, Rathcke IO, ''et al.'' |title=Reduction of LOX- and LOXL2-mRNA expression in head and neck squamous cell carcinomas. |journal=Anticancer Res. |volume=23 |issue= 2B |pages= 1565-73 |year= 2003 |pmid= 12820424 |doi=  }}
*{{cite journal | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal  | author=Vadasz Z, Kessler O, Akiri G, ''et al.'' |title=Abnormal deposition of collagen around hepatocytes in Wilson's disease is associated with hepatocyte specific expression of lysyl oxidase and lysyl oxidase like protein-2. |journal=J. Hepatol. |volume=43 |issue= 3 |pages= 499-507 |year= 2005 |pmid= 16023247 |doi= 10.1016/j.jhep.2005.02.052 }}
*{{cite journal | author=Peinado H, Del Carmen Iglesias-de la Cruz M, Olmeda D, ''et al.'' |title=A molecular role for lysyl oxidase-like 2 enzyme in snail regulation and tumor progression. |journal=EMBO J. |volume=24 |issue= 19 |pages= 3446-58 |year= 2006 |pmid= 16096638 |doi= 10.1038/sj.emboj.7600781 }}
*{{cite journal | author=Akagawa H, Narita A, Yamada H, ''et al.'' |title=Systematic screening of lysyl oxidase-like (LOXL) family genes demonstrates that LOXL2 is a susceptibility gene to intracranial aneurysms. |journal=Hum. Genet. |volume=121 |issue= 3-4 |pages= 377-87 |year= 2007 |pmid= 17287949 |doi= 10.1007/s00439-007-0333-3 }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
{{Use dmy dates|date=April 2017}}
{{WikiDoc Sources}}
 
[[Category:Lysyl oxidases]]
 
 
{{gene-8-stub}}

Latest revision as of 18:04, 2 September 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

n/a

n/a

Ensembl

n/a

n/a

UniProt

n/a

n/a

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

Lysyl oxidase homolog 2 is an enzyme that in humans is encoded by the LOXL2 gene.[1][2]

Function

This gene encodes a member of the lysyl oxidase gene family. The prototypic member of the family is essential to the biogenesis of connective tissue, encoding an extracellular copper-dependent amine oxidase that catalyses the first step in the formation of crosslinks in collagens and elastin. A highly conserved amino acid sequence at the C-terminus end appears to be sufficient for amine oxidase activity, suggesting that each family member may retain this function. The N-terminus is poorly conserved and may impart additional roles in developmental regulation, senescence, tumor suppression, cell growth control, and chemotaxis to each member of the family.[2]

LOXL2 can also crosslink collagen type IV and hence influence the sprouting of new blood vessels.[3]

Clinical significance

LOXL2 is an enzyme that is up-regulated in several types of cancer and is associated with a poorer prognosis.[4][5] LOXL2 changes the structure of histones (proteins that are attached to DNA)[6] and thus changes the shape of the cells, making it easier for the cancer cells to metastasize.[7]

An antibody that inhibits the activity of LOXL2, simtuzumab and is currently in clinical trials for the treatment of several types of cancer and fibrotic diseases such as liver fibrosis.[8]

See also

References

  1. ↑ Jourdan-Le Saux C, Le Saux O, Donlon T, Boyd CD, Csiszar K (July 1998). "The human lysyl oxidase-related gene (LOXL2) maps between markers D8S280 and D8S278 on chromosome 8p21.2-p21.3". Genomics. 51 (2): 305–7. doi:10.1006/geno.1998.5356. PMID 9722957.
  2. ↑ 2.0 2.1 "Entrez Gene: LOXL2 lysyl oxidase-like 2".
  3. ↑ Bignon M, Pichol-Thievend C, Hardouin J, Malbouyres M, Bréchot N, Nasciutti L, Barret A, Teillon J, Guillon E, Etienne E, Caron M, Joubert-Caron R, Monnot C, Ruggiero F, Muller L, Germain S (2011). "Lysyl oxidase-like protein-2 regulates sprouting angiogenesis and type IV collagen assembly in the endothelial basement membrane". Blood. 118: 3979–89. doi:10.1182/blood-2010-10-313296. PMID 21835952.
  4. ↑ Nishioka T, Eustace A, West C (2012). "Lysyl oxidase: from basic science to future cancer treatment". Cell Struct. Funct. 37 (1): 75–80. doi:10.1247/csf.11015. PMID 22453058.
  5. ↑ Cano A, Santamaría PG, Moreno-Bueno G (2012). "LOXL2 in epithelial cell plasticity and tumor progression". Future Oncol. 8 (9): 1095–108. doi:10.2217/fon.12.105. PMID 23030485.
  6. ↑ Herranz N, Dave N, Millanes-Romero A, Morey L, Díaz VM, Lórenz-Fonfría V, Gutierrez-Gallego R, Jerónimo C, Di Croce L, García de Herreros A, Peiró S (2012). "Lysyl oxidase-like 2 deaminates lysine 4 in histone H3". Molecular Cell. 46 (3): 369–376. doi:10.1016/j.molcel.2012.03.002. PMID 22483618.
  7. ↑ Moreno-Bueno G, Salvador F, Martín A, Floristán A, Cuevas EP, Santos V, Montes A, Morales S, Castilla MA, Rojo-Sebastián A, Martínez A, Hardisson D, Csiszar K, Portillo F, Peinado H, Palacios J, Cano A (2011). "Lysyl oxidase-like 2 (LOXL2), a new regulator of cell polarity required for metastatic dissemination of basal-like breast carcinomas". EMBO Mol Med. 3 (9): 528–544. doi:10.1002/emmm.201100156. PMC 3377095. PMID 21732535.
  8. ↑ "Search of: simtuzumab - List Results". ClinicalTrials.gov. Retrieved 25 February 2015.

Further reading

  • Csiszar K (2001). "Lysyl oxidases: a novel multifunctional amine oxidase family". Progress in Nucleic Acid Research and Molecular Biology. Progress in Nucleic Acid Research and Molecular Biology. 70: 1–32. doi:10.1016/S0079-6603(01)70012-8. ISBN 978-0-12-540070-1. PMID 11642359.
  • Molnar J, Fong KS, He QP, Hayashi K, Kim Y, Fong SF, Fogelgren B, Szauter KM, Mink M, Csiszar K (April 2003). "Structural and functional diversity of lysyl oxidase and the LOX-like proteins". Biochimica et Biophysica Acta. 1647 (1–2): 220–4. doi:10.1016/s1570-9639(03)00053-0. PMID 12686136.
  • Maruyama K, Sugano S (Jan 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
  • Saito H, Papaconstantinou J, Sato H, Goldstein S (March 1997). "Regulation of a novel gene encoding a lysyl oxidase-related protein in cellular adhesion and senescence". The Journal of Biological Chemistry. 272 (13): 8157–60. doi:10.1074/jbc.272.13.8157. PMID 9079631.
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (October 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
  • Jourdan-Le Saux C, Tronecker H, Bogic L, Bryant-Greenwood GD, Boyd CD, Csiszar K (April 1999). "The LOXL2 gene encodes a new lysyl oxidase-like protein and is expressed at high levels in reproductive tissues". The Journal of Biological Chemistry. 274 (18): 12939–44. doi:10.1074/jbc.274.18.12939. PMID 10212285.
  • Hein S, Yamamoto SY, Okazaki K, Jourdan-LeSaux C, Csiszar K, Bryant-Greenwood GD (Jan 2001). "Lysyl oxidases: expression in the fetal membranes and placenta". Placenta. 22 (1): 49–57. doi:10.1053/plac.2000.0580. PMID 11162352.
  • Akiri G, Sabo E, Dafni H, Vadasz Z, Kartvelishvily Y, Gan N, Kessler O, Cohen T, Resnick M, Neeman M, Neufeld G (April 2003). "Lysyl oxidase-related protein-1 promotes tumor fibrosis and tumor progression in vivo". Cancer Research. 63 (7): 1657–66. PMID 12670920.
  • Rost T, Pyritz V, Rathcke IO, Görögh T, Dünne AA, Werner JA (2003). "Reduction of LOX- and LOXL2-mRNA expression in head and neck squamous cell carcinomas". Anticancer Research. 23 (2B): 1565–73. PMID 12820424.
  • Vadasz Z, Kessler O, Akiri G, Gengrinovitch S, Kagan HM, Baruch Y, Izhak OB, Neufeld G (September 2005). "Abnormal deposition of collagen around hepatocytes in Wilson's disease is associated with hepatocyte specific expression of lysyl oxidase and lysyl oxidase like protein-2". Journal of Hepatology. 43 (3): 499–507. doi:10.1016/j.jhep.2005.02.052. PMID 16023247.
  • Peinado H, Del Carmen Iglesias-de la Cruz M, Olmeda D, Csiszar K, Fong KS, Vega S, Nieto MA, Cano A, Portillo F (October 2005). "A molecular role for lysyl oxidase-like 2 enzyme in snail regulation and tumor progression". The EMBO Journal. 24 (19): 3446–58. doi:10.1038/sj.emboj.7600781. PMC 1276164. PMID 16096638.
  • Akagawa H, Narita A, Yamada H, Tajima A, Krischek B, Kasuya H, Hori T, Kubota M, Saeki N, Hata A, Mizutani T, Inoue I (May 2007). "Systematic screening of lysyl oxidase-like (LOXL) family genes demonstrates that LOXL2 is a susceptibility gene to intracranial aneurysms". Human Genetics. 121 (3–4): 377–87. doi:10.1007/s00439-007-0333-3. PMID 17287949.


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