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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 1''', also known as '''LOXL1''', is an [[enzyme]] which in humans is encoded by the ''LOXL1'' [[gene]].<ref name="entrez"/><ref name="pmid">{{cite journal | vauthors = Kenyon K, Modi WS, Contente S, Friedman RM | title = A novel human cDNA with a predicted protein similar to lysyl oxidase maps to chromosome 15q24-q25 | journal = The Journal of Biological Chemistry | volume = 268 | issue = 25 | pages = 18435–7 | date = September 1993 | pmid = 7689553 | doi = | url = http://www.jbc.org/cgi/reprint/268/25/18435 }}</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 = Lysyl oxidase-like 1
| HGNCid = 6665
| Symbol = LOXL1
| AltSymbols =; LOL; LOXL
| OMIM = 153456
| ECnumber = 
| Homologene = 4074
| MGIid = 106096
| GeneAtlas_image1 = PBB_GE_LOXL1_203570_at_tn.png
| Function = {{GNF_GO|id=GO:0004720 |text = protein-lysine 6-oxidase activity}} {{GNF_GO|id=GO:0005507 |text = copper ion binding}} {{GNF_GO|id=GO:0016491 |text = oxidoreductase activity}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}}
| Process = {{GNF_GO|id=GO:0006118 |text = electron transport}} {{GNF_GO|id=GO:0018277 |text = protein amino acid deamination}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 4016
    | Hs_Ensembl = ENSG00000129038
    | Hs_RefseqProtein = XP_001133864
    | Hs_RefseqmRNA = XM_001133864
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 15
    | Hs_GenLoc_start = 72005842
    | Hs_GenLoc_end = 72031531
    | Hs_Uniprot = Q08397
    | Mm_EntrezGene = 16949
    | Mm_Ensembl = ENSMUSG00000032334
    | Mm_RefseqmRNA = NM_010729
    | Mm_RefseqProtein = NP_034859
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 9
    | Mm_GenLoc_start = 58085868
    | Mm_GenLoc_end = 58111334
    | Mm_Uniprot = Q4QQJ7
  }}
}}
'''Lysyl oxidase-like 1''', also known as '''LOXL1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: LOXL1 lysyl oxidase-like 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4016| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
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">{{cite web | title = Entrez Gene: LOXL1 lysyl oxidase-like 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4016| accessdate = }}</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: LOXL1 lysyl oxidase-like 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4016| accessdate = }}</ref>
}}


==References==
== Clinical significance ==
{{reflist|2}}
 
==Further reading==
Polymorphisms of the LOXL1 gene are associated with [[pseudoexfoliation syndrome]], a disease where the [[extracellular matrix]] contains abnormal amounts of cross-linked, [[amyloid]]-like fibrillar material and [[glycoprotein]]s. When this happens in the [[eye]], [[exfoliation glaucoma]] results.<ref>{{cite journal | vauthors = Schlötzer-Schrehardt U, Naumann GO | title = Ocular and systemic pseudoexfoliation syndrome | journal = Am. J. Ophthalmol. | volume = 141 | issue = 5 | pages = 921–937 | year = 2006 | pmid = 16678509 | doi = 10.1016/j.ajo.2006.01.047 }}</ref><ref>{{cite journal | vauthors = Thorleifsson G, Magnusson KP, Sulem P, Walters GB, Gudbjartsson DF, Stefansson H, Jonsson T, Jonasdottir A, Jonasdottir A, Stefansdottir G, Masson G, Hardarson GA, Petursson H, Arnarsson A, Motallebipour M, Wallerman O, Wadelius C, Gulcher JR, Thorsteinsdottir U, Kong A, Jonasson F, Stefansson K | title = Common sequence variants in the LOXL1 gene confer susceptibility to exfoliation glaucoma | journal = Science | volume = 317 | issue = 5843 | pages = 1397–400 | year = 2007 | pmid = 17690259 | doi = 10.1126/science.1146554 | bibcode = 2007Sci...317.1397T }}</ref>
 
== Interactions ==
LOXL1 has been shown to [[Protein-protein interaction|interact]] with [[FBLN5]].<ref name=pmid14745449>{{cite journal | vauthors = Liu X, Zhao Y, Gao J, Pawlyk B, Starcher B, Spencer JA, Yanagisawa H, Zuo J, Li T | title = Elastic fiber homeostasis requires lysyl oxidase-like 1 protein  | journal = Nat. Genet. | volume = 36 | issue = 2 | pages = 178–82 | date = Feb 2004 | pmid = 14745449 | doi = 10.1038/ng1297 | url =  | authorlink =  | laysummary =  | oclc =  | id =  | bibcode =  | accessdate =  | location = United States | laydate =  | format =  | quote =  | publisher =  | issn = 1061-4036 | laysource =  }}</ref>
 
== See also ==
* [[LOXL2]]
* [[LOXL3]]
* [[LOXL4]]
 
== References ==
{{reflist |2}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = 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 = 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 = Kagan HM, Li W | title = Lysyl oxidase: properties, specificity, and biological roles inside and outside of the cell | journal = J. Cell. Biochem. | volume = 88 | issue = 4 | pages = 660–72 | year = 2003 | pmid = 12577300 | doi = 10.1002/jcb.10413 }}
*{{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 = 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 = Biochim. Biophys. Acta | volume = 1647 | issue = 1–2 | pages = 220–4 | year = 2003 | pmid = 12686136 | doi = 10.1016/s1570-9639(03)00053-0 }}
*{{cite journal | author=Kagan HM, Li W |title=Lysyl oxidase: properties, specificity, and biological roles inside and outside of the cell. |journal=J. Cell. Biochem. |volume=88 |issue= 4 |pages= 660-72 |year= 2003 |pmid= 12577300 |doi= 10.1002/jcb.10413 }}
* {{cite journal | vauthors = Kenyon K, Modi WS, Contente S, Friedman RM | title = A novel human cDNA with a predicted protein similar to lysyl oxidase maps to chromosome 15q24-q25 | journal = J. Biol. Chem. | volume = 268 | issue = 25 | pages = 18435–7 | year = 1993 | pmid = 7689553 | doi =  }}
*{{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 = Kim Y, Boyd CD, Csiszar K | title = A new gene with sequence and structural similarity to the gene encoding human lysyl oxidase | journal = J. Biol. Chem. | volume = 270 | issue = 13 | pages = 7176–82 | year = 1995 | pmid = 7706256 | doi = 10.1074/jbc.270.13.7176 }}
*{{cite journal | author=Kenyon K, Modi WS, Contente S, Friedman RM |title=A novel human cDNA with a predicted protein similar to lysyl oxidase maps to chromosome 15q24-q25. |journal=J. Biol. Chem. |volume=268 |issue= 25 |pages= 18435-7 |year= 1993 |pmid= 7689553 |doi=  }}
* {{cite journal | vauthors = Goy A, Gilles F, Remache Y, Zelenetz AD | title = Physical linkage of the lysyl oxidase-like (LOXL1) gene to the PML gene on human chromosome 15q22 | journal = Cytogenet. Cell Genet. | volume = 88 | issue = 1–2 | pages = 22–4 | year = 2000 | pmid = 10773658 | doi = 10.1159/000015477 }}
*{{cite journal | author=Kim Y, Boyd CD, Csiszar K |title=A new gene with sequence and structural similarity to the gene encoding human lysyl oxidase. |journal=J. Biol. Chem. |volume=270 |issue= 13 |pages= 7176-82 |year= 1995 |pmid= 7706256 |doi= }}
* {{cite journal | vauthors = Jung ST, Kim MS, Seo JY, Kim HC, Kim Y | title = Purification of enzymatically active human lysyl oxidase and lysyl oxidase-like protein from Escherichia coli inclusion bodies | journal = Protein Expr. Purif. | volume = 31 | issue = 2 | pages = 240–6 | year = 2004 | pmid = 14550642 | doi = 10.1016/S1046-5928(03)00217-1 }}
*{{cite journal | author=Goy A, Gilles F, Remache Y, Zelenetz AD |title=Physical linkage of the lysyl oxidase-like (LOXL1) gene to the PML gene on human chromosome 15q22. |journal=Cytogenet. Cell Genet. |volume=88 |issue= 1-2 |pages= 22-4 |year= 2000 |pmid= 10773658 |doi=  }}
* {{cite journal | vauthors = Liu X, Zhao Y, Gao J, Pawlyk B, Starcher B, Spencer JA, Yanagisawa H, Zuo J, Li T | title = Elastic fiber homeostasis requires lysyl oxidase-like 1 protein | journal = Nat. Genet. | volume = 36 | issue = 2 | pages = 178–82 | year = 2004 | pmid = 14745449 | doi = 10.1038/ng1297 }}
*{{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 = Noblesse E, Cenizo V, Bouez C, Borel A, Gleyzal C, Peyrol S, Jacob MP, Sommer P, Damour O | title = Lysyl oxidase-like and lysyl oxidase are present in the dermis and epidermis of a skin equivalent and in human skin and are associated to elastic fibers | journal = J. Invest. Dermatol. | volume = 122 | issue = 3 | pages = 621–30 | year = 2004 | pmid = 15086544 | doi = 10.1111/j.0022-202X.2004.22330.x }}
*{{cite journal | author=Jung ST, Kim MS, Seo JY, ''et al.'' |title=Purification of enzymatically active human lysyl oxidase and lysyl oxidase-like protein from Escherichia coli inclusion bodies. |journal=Protein Expr. Purif. |volume=31 |issue= 2 |pages= 240-6 |year= 2004 |pmid= 14550642 |doi= }}
* {{cite journal | vauthors = Thomassin L, Werneck CC, Broekelmann TJ, Gleyzal C, Hornstra IK, Mecham RP, Sommer P | title = The Pro-regions of lysyl oxidase and lysyl oxidase-like 1 are required for deposition onto elastic fibers | journal = J. Biol. Chem. | volume = 280 | issue = 52 | pages = 42848–55 | year = 2006 | pmid = 16251195 | doi = 10.1074/jbc.M506832200 }}
*{{cite journal | author=Liu X, Zhao Y, Gao J, ''et al.'' |title=Elastic fiber homeostasis requires lysyl oxidase-like 1 protein. |journal=Nat. Genet. |volume=36 |issue= 2 |pages= 178-82 |year= 2004 |pmid= 14745449 |doi= 10.1038/ng1297 }}
* {{cite journal | vauthors = Cenizo V, André V, Reymermier C, Sommer P, Damour O, Perrier E | title = LOXL as a target to increase the elastin content in adult skin: a dill extract induces the LOXL gene expression | journal = Exp. Dermatol. | volume = 15 | issue = 8 | pages = 574–81 | year = 2007 | pmid = 16842595 | doi = 10.1111/j.1600-0625.2006.00442.x }}
*{{cite journal | author=Noblesse E, Cenizo V, Bouez C, ''et al.'' |title=Lysyl oxidase-like and lysyl oxidase are present in the dermis and epidermis of a skin equivalent and in human skin and are associated to elastic fibers. |journal=J. Invest. Dermatol. |volume=122 |issue= 3 |pages= 621-30 |year= 2004 |pmid= 15086544 |doi= 10.1111/j.0022-202X.2004.22330.x }}
* {{cite journal | vauthors = Thorleifsson G, Magnusson KP, Sulem P, Walters GB, Gudbjartsson DF, Stefansson H, Jonsson T, Jonasdottir A, Jonasdottir A, Stefansdottir G, Masson G, Hardarson GA, Petursson H, Arnarsson A, Motallebipour M, Wallerman O, Wadelius C, Gulcher JR, Thorsteinsdottir U, Kong A, Jonasson F, Stefansson K | title = Common sequence variants in the LOXL1 gene confer susceptibility to exfoliation glaucoma | journal = Science | volume = 317 | issue = 5843 | pages = 1397–400 | year = 2007 | pmid = 17690259 | doi = 10.1126/science.1146554 | bibcode = 2007Sci...317.1397T }}
*{{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 | vauthors = Damji KF | title = Progress in understanding pseudoexfoliation syndrome and pseudoexfoliation-associated glaucoma | journal = Can. J. Ophthalmol. | volume = 42 | issue = 5 | pages = 657–8 | year = 2007 | pmid = 17891191 | doi = 10.3129/I07-158 }}
*{{cite journal  | author=Thomassin L, Werneck CC, Broekelmann TJ, ''et al.'' |title=The Pro-regions of lysyl oxidase and lysyl oxidase-like 1 are required for deposition onto elastic fibers. |journal=J. Biol. Chem. |volume=280 |issue= 52 |pages= 42848-55 |year= 2006 |pmid= 16251195 |doi= 10.1074/jbc.M506832200 }}
*{{cite journal | author=Cenizo V, André V, Reymermier C, ''et al.'' |title=LOXL as a target to increase the elastin content in adult skin: a dill extract induces the LOXL gene expression. |journal=Exp. Dermatol. |volume=15 |issue= 8 |pages= 574-81 |year= 2007 |pmid= 16842595 |doi= 10.1111/j.1600-0625.2006.00442.x }}
*{{cite journal | author=Thorleifsson G, Magnusson KP, Sulem P, ''et al.'' |title=Common sequence variants in the LOXL1 gene confer susceptibility to exfoliation glaucoma. |journal=Science |volume=317 |issue= 5843 |pages= 1397-400 |year= 2007 |pmid= 17690259 |doi= 10.1126/science.1146554 }}
*{{cite journal | author=Damji KF |title=Progress in understanding pseudoexfoliation syndrome and pseudoexfoliation-associated glaucoma. |journal=Can. J. Ophthalmol. |volume=42 |issue= 5 |pages= 657-8 |year= 2007 |pmid= 17891191 |doi= 10.1139/i07-158 }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
 
{{WikiDoc Sources}}
{{gene-15-stub}}
 
[[Category:Lysyl oxidases]]

Latest revision as of 12:44, 9 January 2019

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 1, also known as LOXL1, is an enzyme which in humans is encoded by the LOXL1 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.[1]

Clinical significance

Polymorphisms of the LOXL1 gene are associated with pseudoexfoliation syndrome, a disease where the extracellular matrix contains abnormal amounts of cross-linked, amyloid-like fibrillar material and glycoproteins. When this happens in the eye, exfoliation glaucoma results.[3][4]

Interactions

LOXL1 has been shown to interact with FBLN5.[5]

See also

References

  1. ↑ 1.0 1.1 "Entrez Gene: LOXL1 lysyl oxidase-like 1".
  2. ↑ Kenyon K, Modi WS, Contente S, Friedman RM (September 1993). "A novel human cDNA with a predicted protein similar to lysyl oxidase maps to chromosome 15q24-q25". The Journal of Biological Chemistry. 268 (25): 18435–7. PMID 7689553.
  3. ↑ Schlötzer-Schrehardt U, Naumann GO (2006). "Ocular and systemic pseudoexfoliation syndrome". Am. J. Ophthalmol. 141 (5): 921–937. doi:10.1016/j.ajo.2006.01.047. PMID 16678509.
  4. ↑ Thorleifsson G, Magnusson KP, Sulem P, Walters GB, Gudbjartsson DF, Stefansson H, Jonsson T, Jonasdottir A, Jonasdottir A, Stefansdottir G, Masson G, Hardarson GA, Petursson H, Arnarsson A, Motallebipour M, Wallerman O, Wadelius C, Gulcher JR, Thorsteinsdottir U, Kong A, Jonasson F, Stefansson K (2007). "Common sequence variants in the LOXL1 gene confer susceptibility to exfoliation glaucoma". Science. 317 (5843): 1397–400. Bibcode:2007Sci...317.1397T. doi:10.1126/science.1146554. PMID 17690259.
  5. ↑ Liu X, Zhao Y, Gao J, Pawlyk B, Starcher B, Spencer JA, Yanagisawa H, Zuo J, Li T (Feb 2004). "Elastic fiber homeostasis requires lysyl oxidase-like 1 protein". Nat. Genet. United States. 36 (2): 178–82. doi:10.1038/ng1297. ISSN 1061-4036. PMID 14745449.

Further reading

  • Csiszar K (2001). "Lysyl oxidases: a novel multifunctional amine oxidase family". Prog. Nucleic Acid Res. Mol. Biol. 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.
  • Kagan HM, Li W (2003). "Lysyl oxidase: properties, specificity, and biological roles inside and outside of the cell". J. Cell. Biochem. 88 (4): 660–72. doi:10.1002/jcb.10413. PMID 12577300.
  • Molnar J, Fong KS, He QP, Hayashi K, Kim Y, Fong SF, Fogelgren B, Szauter KM, Mink M, Csiszar K (2003). "Structural and functional diversity of lysyl oxidase and the LOX-like proteins". Biochim. Biophys. Acta. 1647 (1–2): 220–4. doi:10.1016/s1570-9639(03)00053-0. PMID 12686136.
  • Kenyon K, Modi WS, Contente S, Friedman RM (1993). "A novel human cDNA with a predicted protein similar to lysyl oxidase maps to chromosome 15q24-q25". J. Biol. Chem. 268 (25): 18435–7. PMID 7689553.
  • Kim Y, Boyd CD, Csiszar K (1995). "A new gene with sequence and structural similarity to the gene encoding human lysyl oxidase". J. Biol. Chem. 270 (13): 7176–82. doi:10.1074/jbc.270.13.7176. PMID 7706256.
  • Goy A, Gilles F, Remache Y, Zelenetz AD (2000). "Physical linkage of the lysyl oxidase-like (LOXL1) gene to the PML gene on human chromosome 15q22". Cytogenet. Cell Genet. 88 (1–2): 22–4. doi:10.1159/000015477. PMID 10773658.
  • Jung ST, Kim MS, Seo JY, Kim HC, Kim Y (2004). "Purification of enzymatically active human lysyl oxidase and lysyl oxidase-like protein from Escherichia coli inclusion bodies". Protein Expr. Purif. 31 (2): 240–6. doi:10.1016/S1046-5928(03)00217-1. PMID 14550642.
  • Liu X, Zhao Y, Gao J, Pawlyk B, Starcher B, Spencer JA, Yanagisawa H, Zuo J, Li T (2004). "Elastic fiber homeostasis requires lysyl oxidase-like 1 protein". Nat. Genet. 36 (2): 178–82. doi:10.1038/ng1297. PMID 14745449.
  • Noblesse E, Cenizo V, Bouez C, Borel A, Gleyzal C, Peyrol S, Jacob MP, Sommer P, Damour O (2004). "Lysyl oxidase-like and lysyl oxidase are present in the dermis and epidermis of a skin equivalent and in human skin and are associated to elastic fibers". J. Invest. Dermatol. 122 (3): 621–30. doi:10.1111/j.0022-202X.2004.22330.x. PMID 15086544.
  • Thomassin L, Werneck CC, Broekelmann TJ, Gleyzal C, Hornstra IK, Mecham RP, Sommer P (2006). "The Pro-regions of lysyl oxidase and lysyl oxidase-like 1 are required for deposition onto elastic fibers". J. Biol. Chem. 280 (52): 42848–55. doi:10.1074/jbc.M506832200. PMID 16251195.
  • Cenizo V, André V, Reymermier C, Sommer P, Damour O, Perrier E (2007). "LOXL as a target to increase the elastin content in adult skin: a dill extract induces the LOXL gene expression". Exp. Dermatol. 15 (8): 574–81. doi:10.1111/j.1600-0625.2006.00442.x. PMID 16842595.
  • Thorleifsson G, Magnusson KP, Sulem P, Walters GB, Gudbjartsson DF, Stefansson H, Jonsson T, Jonasdottir A, Jonasdottir A, Stefansdottir G, Masson G, Hardarson GA, Petursson H, Arnarsson A, Motallebipour M, Wallerman O, Wadelius C, Gulcher JR, Thorsteinsdottir U, Kong A, Jonasson F, Stefansson K (2007). "Common sequence variants in the LOXL1 gene confer susceptibility to exfoliation glaucoma". Science. 317 (5843): 1397–400. Bibcode:2007Sci...317.1397T. doi:10.1126/science.1146554. PMID 17690259.
  • Damji KF (2007). "Progress in understanding pseudoexfoliation syndrome and pseudoexfoliation-associated glaucoma". Can. J. Ophthalmol. 42 (5): 657–8. doi:10.3129/I07-158. PMID 17891191.


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