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{{Infobox_gene}}
{{PBB_Controls
'''Sentrin-specific protease 1''' is an [[enzyme]] that in humans is encoded by the ''SENP1'' [[gene]].<ref name="pmid10652325">{{cite journal | vauthors = Gong L, Millas S, Maul GG, Yeh ET | title = Differential regulation of sentrinized proteins by a novel sentrin-specific protease | journal = The Journal of Biological Chemistry | volume = 275 | issue = 5 | pages = 3355–9 | date = Feb 2000 | pmid = 10652325 | pmc =  | doi = 10.1074/jbc.275.5.3355 }}</ref><ref name="pmid14563852">{{cite journal | vauthors = Bailey D, O'Hare P | title = Characterization of the localization and proteolytic activity of the SUMO-specific protease, SENP1 | journal = The Journal of Biological Chemistry | volume = 279 | issue = 1 | pages = 692–703 | date = Jan 2004 | pmid = 14563852 | pmc = | doi = 10.1074/jbc.M306195200 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: SENP1 SUMO1/sentrin specific peptidase 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=29843| 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. -->
== General ==
{{GNF_Protein_box
| image = PBB_Protein_SENP1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2ckg.
| PDB = {{PDB2|2ckg}}, {{PDB2|2ckh}}, {{PDB2|2g4d}}, {{PDB2|2iy0}}, {{PDB2|2iy1}}, {{PDB2|2iyc}}, {{PDB2|2iyd}}
| Name = SUMO1/sentrin specific peptidase 1
| HGNCid = 17927
| Symbol = SENP1
| AltSymbols =; SuPr-2
| OMIM = 
| ECnumber = 
| Homologene = 8731
| MGIid = 2445054
| Function = {{GNF_GO|id=GO:0004175 |text = endopeptidase activity}} {{GNF_GO|id=GO:0008234 |text = cysteine-type peptidase activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0006512 |text = ubiquitin cycle}} {{GNF_GO|id=GO:0016926 |text = protein desumoylation}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 29843
    | Hs_Ensembl = ENSG00000079387
    | Hs_RefseqProtein = NP_055369
    | Hs_RefseqmRNA = NM_014554
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 12
    | Hs_GenLoc_start = 46723275
    | Hs_GenLoc_end = 46786042
    | Hs_Uniprot = Q9P0U3
    | Mm_EntrezGene = 223870
    | Mm_Ensembl = ENSMUSG00000033075
    | Mm_RefseqmRNA = NM_144851
    | Mm_RefseqProtein = NP_659100
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 15
    | Mm_GenLoc_start = 97870924
    | Mm_GenLoc_end = 97913138
    | Mm_Uniprot = Q8C187
  }}
}}
'''SUMO1/sentrin specific peptidase 1''', also known as '''SENP1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SENP1 SUMO1/sentrin specific peptidase 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=29843| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
So far there are seven SUMO [[proteases]] in humans that have been designated SENP1-7 (sentrin/SUMO-specific protease).1 The seven proteases possess a conserved [[C-terminal]] domain which are variable in size, and with a distinct [[N-terminal]] domain between them. The C-terminal domain shows [[catalytic activity]] and N-terminal domain regulates cell localization and substrate specificity.<ref name = "Xu_2006">{{cite journal | vauthors = Xu Z, Chau SF, Lam KH, Chan HY, Ng TB, Au SW | title = Crystal structure of the SENP1 mutant C603S-SUMO complex reveals the hydrolytic mechanism of SUMO-specific protease | journal = The Biochemical Journal | volume = 398 | issue = 3 | date = Sep 2006 | pmid = 16712526 | doi = 10.1042/BJ20060526 | pmc=1559472 | pages=345–52}}</ref>
{{PBB_Summary
| section_title =  
| summary_text =  
}}


==References==
== Features ==
{{reflist|2}}
 
==Further reading==
SENP1 (Sentrin-specific protease 1) is a human protease of 643 amino acids with a weight of 73 kDa, [[Enzyme Commission number|EC number]] in humans 3.4.22.B70, which adopts a conformation that identifies it as a member of the superfamily of cysteine proteases contain a catalytic triad with characterized three amino acids: a [[cysteine]] at position 602, a [[histidine]] at position 533 and [[aspartic acid]] at position 550.
{{refbegin | 2}}
The important nucleophile is cysteine located at the N-terminal [[alpha helix]] of the protein core, the other two amino acids, aspartate and histidine, are located in a [[beta sheet]] end.
{{PBB_Further_reading
<ref>{{cite journal | vauthors = Shen LN, Dong C, Liu H, Naismith JH, Hay RT | year = 2006 | title = The structure of SENP1-SUMO-2 complex suggests a structural basis for discrimination between SUMO paralogues during processing | url = | journal = The Biochemical Journal | volume = 397 | issue = 2| pages = 279–288 | doi = 10.1042/BJ20052030 | pmid=16553580 | pmc=1513277}}</ref>
| citations =  
[[File:SENP1.png|thumb|SENP1 The catalytic site consists of three amino acids: Cys 602, His 533 and Asp 550.]]
*{{cite journal | author=Cheng J, Bawa T, Lee P, ''et al.'' |title=Role of desumoylation in the development of prostate cancer. |journal=Neoplasia |volume=8 |issue= 8 |pages= 667-76 |year= 2006 |pmid= 16925949 |doi= 10.1593/neo.06445 }}
 
*{{cite journal | author=Gong L, Millas S, Maul GG, Yeh ET |title=Differential regulation of sentrinized proteins by a novel sentrin-specific protease. |journal=J. Biol. Chem. |volume=275 |issue= 5 |pages= 3355-9 |year= 2000 |pmid= 10652325 |doi= }}
== Location ==
*{{cite journal | author=Bailey D, O'Hare P |title=Herpes simplex virus 1 ICP0 co-localizes with a SUMO-specific protease. |journal=J. Gen. Virol. |volume=83 |issue= Pt 12 |pages= 2951-64 |year= 2003 |pmid= 12466471 |doi= }}
 
*{{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 }}
Both SENP1 are located in the [[Cell nucleus|nucleus]] and [[cytosol]] depending on the cell type, although it has been seen that is exported out from the nucleus to the cytosol through a sequence of nuclear export (NES) that is located at the C-terminus. The mammalian SENP1 is localized mainly in the nucleus.<ref>{{cite journal | vauthors = Kim YH, Sung KS, Lee SJ, Kim YO, Choi CY, Kim Y | year = 2005 | title = Desumoylation of homeodomain-interacting protein kinase 2 (HIPK2) through the cytoplasmic-nuclear shuttling of the SUMO-specific protease SENP1 | url = | journal = FEBS Letters | volume = 579 | issue = 27| pages = 6272–6278 | doi = 10.1016/j.febslet.2005.10.010 | pmid=16253240}}</ref>
*{{cite journal | author=Bailey D, O'Hare P |title=Characterization of the localization and proteolytic activity of the SUMO-specific protease, SENP1. |journal=J. Biol. Chem. |volume=279 |issue= 1 |pages= 692-703 |year= 2004 |pmid= 14563852 |doi= 10.1074/jbc.M306195200 }}
 
*{{cite journal | author=Cheng J, Wang D, Wang Z, Yeh ET |title=SENP1 enhances androgen receptor-dependent transcription through desumoylation of histone deacetylase 1. |journal=Mol. Cell. Biol. |volume=24 |issue= 13 |pages= 6021-8 |year= 2004 |pmid= 15199155 |doi= 10.1128/MCB.24.13.6021-6028.2004 }}
== Function ==
*{{cite journal | author=Xu Z, Au SW |title=Mapping residues of SUMO precursors essential in differential maturation by SUMO-specific protease, SENP1. |journal=Biochem. J. |volume=386 |issue= Pt 2 |pages= 325-30 |year= 2005 |pmid= 15487983 |doi= 10.1042/BJ20041210 }}
SENP1 catalyzes maturation [[SUMO protein]] (small ubiquitin-related modifier), which causes hydrolysis peptide bond of SUMO is in a conserved sequence Gly-Gly-|-Ala-Thr-Tyr at the C-terminal <ref>http://www.uniprot.org/uniprot/Q9P0U3#ptm_processing</ref> to be added to the conjugation of other proteins ([[sumoylation]]).<ref>{{cite journal | vauthors = Xu Z, Au SW | year = 2005 | title = Mapping residues of SUMO precursors essential in differential maturation by SUMO-specific protease, SENP1 | url = | journal = The Biochemical Journal | volume = 386 | issue = Pt 2| pages = 325–330 | doi = 10.1042/BJ20041210 | pmid=15487983 | pmc=1134797}}</ref>
*{{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 }}
In vertebrates there are three members of the family of SUMO: SUMO-1, -2 and -3. SENP1 can catalyze any of these three.
*{{cite journal  | author=Boggio R, Colombo R, Hay RT, ''et al.'' |title=A mechanism for inhibiting the SUMO pathway. |journal=Mol. Cell |volume=16 |issue= 4 |pages= 549-61 |year= 2005 |pmid= 15546615 |doi= 10.1016/j.molcel.2004.11.007 }}
This conjugation of SUMO toward other proteins is a lot like ubiquitination, however these modifications leads to different results depending on the type of protein been modified.<ref>{{cite journal | vauthors = Xu Z, Chau SF, Lam KH, Chan HY, Ng TB, Au SW | title = Crystal structure of the SENP1 mutant C603S-SUMO complex reveals the hydrolytic mechanism of SUMO-specific protease | journal = The Biochemical Journal | volume = 398 | issue = 3 | date = 2006 | pmid = 16712526 | doi = 10.1042/BJ20060526 | pmc=1559472 | pages=345–52}}</ref>
*{{cite journal | author=Cheng J, Perkins ND, Yeh ET |title=Differential regulation of c-Jun-dependent transcription by SUMO-specific proteases. |journal=J. Biol. Chem. |volume=280 |issue= 15 |pages= 14492-8 |year= 2005 |pmid= 15701643 |doi= 10.1074/jbc.M412185200 }}
 
*{{cite journal | author=Rajan S, Plant LD, Rabin ML, ''et al.'' |title=Sumoylation silences the plasma membrane leak K+ channel K2P1. |journal=Cell |volume=121 |issue= 1 |pages= 37-47 |year= 2005 |pmid= 15820677 |doi= 10.1016/j.cell.2005.01.019 }}
== References ==
*{{cite journal | author=Veltman IM, Vreede LA, Cheng J, ''et al.'' |title=Fusion of the SUMO/Sentrin-specific protease 1 gene SENP1 and the embryonic polarity-related mesoderm development gene MESDC2 in a patient with an infantile teratoma and a constitutional t(12;15)(q13;q25). |journal=Hum. Mol. Genet. |volume=14 |issue= 14 |pages= 1955-63 |year= 2005 |pmid= 15917269 |doi= 10.1093/hmg/ddi200 }}
{{reflist|33em}}
*{{cite journal | author=Kim YH, Sung KS, Lee SJ, ''et al.'' |title=Desumoylation of homeodomain-interacting protein kinase 2 (HIPK2) through the cytoplasmic-nuclear shuttling of the SUMO-specific protease SENP1. |journal=FEBS Lett. |volume=579 |issue= 27 |pages= 6272-8 |year= 2005 |pmid= 16253240 |doi= 10.1016/j.febslet.2005.10.010 }}
 
*{{cite journal | author=Shen LN, Dong C, Liu H, ''et al.'' |title=The structure of SENP1-SUMO-2 complex suggests a structural basis for discrimination between SUMO paralogues during processing. |journal=Biochem. J. |volume=397 |issue= 2 |pages= 279-88 |year= 2006 |pmid= 16553580 |doi= 10.1042/BJ20052030 }}
== Further reading ==
*{{cite journal | author=Xu Z, Chau SF, Lam KH, ''et al.'' |title=Crystal structure of the SENP1 mutant C603S-SUMO complex reveals the hydrolytic mechanism of SUMO-specific protease. |journal=Biochem. J. |volume=398 |issue= 3 |pages= 345-52 |year= 2006 |pmid= 16712526 |doi= 10.1042/BJ20060526 }}
{{refbegin|33em}}
*{{cite journal | author=Shen L, Tatham MH, Dong C, ''et al.'' |title=SUMO protease SENP1 induces isomerization of the scissile peptide bond. |journal=Nat. Struct. Mol. Biol. |volume=13 |issue= 12 |pages= 1069-77 |year= 2007 |pmid= 17099698 |doi= 10.1038/nsmb1172 }}
* {{cite journal | vauthors = Mikolajczyk J, Drag M, Békés M, Cao JT, Ronai Z, Salvesen GS | title = Small ubiquitin-related modifier (SUMO)-specific proteases: profiling the specificities and activities of human SENPs | journal = The Journal of Biological Chemistry | volume = 282 | issue = 36 | pages = 26217–24 | date = Sep 2007 | pmid = 17591783 | doi = 10.1074/jbc.M702444200 }}
}}
* {{cite journal | vauthors = Drag M, Mikolajczyk J, Krishnakumar IM, Huang Z, Salvesen GS | title = Activity profiling of human deSUMOylating enzymes (SENPs) with synthetic substrates suggests an unexpected specificity of two newly characterized members of the family | journal = The Biochemical Journal | volume = 409 | issue = 2 | pages = 461–9 | date = Jan 2008 | pmid = 17916063 | doi = 10.1042/BJ20070940 }}
* {{cite journal | vauthors = Cheng J, Bawa T, Lee P, Gong L, Yeh ET | title = Role of desumoylation in the development of prostate cancer | journal = Neoplasia | volume = 8 | issue = 8 | pages = 667–76 | date = Aug 2006 | pmid = 16925949 | pmc = 1601940 | doi = 10.1593/neo.06445 }}
* {{cite journal | vauthors = Bailey D, O'Hare P | title = Herpes simplex virus 1 ICP0 co-localizes with a SUMO-specific protease | journal = The Journal of General Virology | volume = 83 | issue = Pt 12 | pages = 2951–64 | date = Dec 2002 | pmid = 12466471 | doi = 10.1099/0022-1317-83-12-2951}}
* {{cite journal | vauthors = Cheng J, Wang D, Wang Z, Yeh ET | title = SENP1 enhances androgen receptor-dependent transcription through desumoylation of histone deacetylase 1 | journal = Molecular and Cellular Biology | volume = 24 | issue = 13 | pages = 6021–8 | date = Jul 2004 | pmid = 15199155 | pmc = 480885 | doi = 10.1128/MCB.24.13.6021-6028.2004 }}
* {{cite journal | vauthors = Xu Z, Au SW | title = Mapping residues of SUMO precursors essential in differential maturation by SUMO-specific protease, SENP1 | journal = The Biochemical Journal | volume = 386 | issue = Pt 2 | pages = 325–30 | date = Mar 2005 | pmid = 15487983 | pmc = 1134797 | doi = 10.1042/BJ20041210 }}
* {{cite journal | vauthors = Boggio R, Colombo R, Hay RT, Draetta GF, Chiocca S | title = A mechanism for inhibiting the SUMO pathway | journal = Molecular Cell | volume = 16 | issue = 4 | pages = 549–61 | date = Nov 2004 | pmid = 15546615 | doi = 10.1016/j.molcel.2004.11.007 }}
* {{cite journal | vauthors = Cheng J, Perkins ND, Yeh ET | title = Differential regulation of c-Jun-dependent transcription by SUMO-specific proteases | journal = The Journal of Biological Chemistry | volume = 280 | issue = 15 | pages = 14492–8 | date = Apr 2005 | pmid = 15701643 | doi = 10.1074/jbc.M412185200 }}
* {{cite journal | vauthors = Rajan S, Plant LD, Rabin ML, Butler MH, Goldstein SA | title = Sumoylation silences the plasma membrane leak K+ channel K2P1 | journal = Cell | volume = 121 | issue = 1 | pages = 37–47 | date = Apr 2005 | pmid = 15820677 | doi = 10.1016/j.cell.2005.01.019 }}
* {{cite journal | vauthors = Veltman IM, Vreede LA, Cheng J, Looijenga LH, Janssen B, Schoenmakers EF, Yeh ET, van Kessel AG | title = Fusion of the SUMO/Sentrin-specific protease 1 gene SENP1 and the embryonic polarity-related mesoderm development gene MESDC2 in a patient with an infantile teratoma and a constitutional t(12;15)(q13;q25) | journal = Human Molecular Genetics | volume = 14 | issue = 14 | pages = 1955–63 | date = Jul 2005 | pmid = 15917269 | doi = 10.1093/hmg/ddi200 }}
* {{cite journal | vauthors = Kim YH, Sung KS, Lee SJ, Kim YO, Choi CY, Kim Y | title = Desumoylation of homeodomain-interacting protein kinase 2 (HIPK2) through the cytoplasmic-nuclear shuttling of the SUMO-specific protease SENP1 | journal = FEBS Letters | volume = 579 | issue = 27 | pages = 6272–8 | date = Nov 2005 | pmid = 16253240 | doi = 10.1016/j.febslet.2005.10.010 }}
* {{cite journal | vauthors = Shen LN, Dong C, Liu H, Naismith JH, Hay RT | title = The structure of SENP1-SUMO-2 complex suggests a structural basis for discrimination between SUMO paralogues during processing | journal = The Biochemical Journal | volume = 397 | issue = 2 | pages = 279–88 | date = Jul 2006 | pmid = 16553580 | pmc = 1513277 | doi = 10.1042/BJ20052030 }}
* {{cite journal | vauthors = Xu Z, Chau SF, Lam KH, Chan HY, Ng TB, Au SW | title = Crystal structure of the SENP1 mutant C603S-SUMO complex reveals the hydrolytic mechanism of SUMO-specific protease | journal = The Biochemical Journal | volume = 398 | issue = 3 | pages = 345–52 | date = Sep 2006 | pmid = 16712526 | pmc = 1559472 | doi = 10.1042/BJ20060526 }}
* {{cite journal | vauthors = Shen L, Tatham MH, Dong C, Zagórska A, Naismith JH, Hay RT | title = SUMO protease SENP1 induces isomerization of the scissile peptide bond | journal = Nature Structural & Molecular Biology | volume = 13 | issue = 12 | pages = 1069–77 | date = Dec 2006 | pmid = 17099698 | pmc = 3326531 | doi = 10.1038/nsmb1172 }}
{{refend}}
{{refend}}
 
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Revision as of 06:06, 11 September 2017

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

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Ensembl

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UniProt

n/a

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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

Sentrin-specific protease 1 is an enzyme that in humans is encoded by the SENP1 gene.[1][2][3]

General

So far there are seven SUMO proteases in humans that have been designated SENP1-7 (sentrin/SUMO-specific protease).1 The seven proteases possess a conserved C-terminal domain which are variable in size, and with a distinct N-terminal domain between them. The C-terminal domain shows catalytic activity and N-terminal domain regulates cell localization and substrate specificity.[4]

Features

SENP1 (Sentrin-specific protease 1) is a human protease of 643 amino acids with a weight of 73 kDa, EC number in humans 3.4.22.B70, which adopts a conformation that identifies it as a member of the superfamily of cysteine proteases contain a catalytic triad with characterized three amino acids: a cysteine at position 602, a histidine at position 533 and aspartic acid at position 550. The important nucleophile is cysteine located at the N-terminal alpha helix of the protein core, the other two amino acids, aspartate and histidine, are located in a beta sheet end. [5]

File:SENP1.png
SENP1 The catalytic site consists of three amino acids: Cys 602, His 533 and Asp 550.

Location

Both SENP1 are located in the nucleus and cytosol depending on the cell type, although it has been seen that is exported out from the nucleus to the cytosol through a sequence of nuclear export (NES) that is located at the C-terminus. The mammalian SENP1 is localized mainly in the nucleus.[6]

Function

SENP1 catalyzes maturation SUMO protein (small ubiquitin-related modifier), which causes hydrolysis peptide bond of SUMO is in a conserved sequence Gly-Gly-|-Ala-Thr-Tyr at the C-terminal [7] to be added to the conjugation of other proteins (sumoylation).[8] In vertebrates there are three members of the family of SUMO: SUMO-1, -2 and -3. SENP1 can catalyze any of these three. This conjugation of SUMO toward other proteins is a lot like ubiquitination, however these modifications leads to different results depending on the type of protein been modified.[9]

References

  1. ↑ Gong L, Millas S, Maul GG, Yeh ET (Feb 2000). "Differential regulation of sentrinized proteins by a novel sentrin-specific protease". The Journal of Biological Chemistry. 275 (5): 3355–9. doi:10.1074/jbc.275.5.3355. PMID 10652325.
  2. ↑ Bailey D, O'Hare P (Jan 2004). "Characterization of the localization and proteolytic activity of the SUMO-specific protease, SENP1". The Journal of Biological Chemistry. 279 (1): 692–703. doi:10.1074/jbc.M306195200. PMID 14563852.
  3. ↑ "Entrez Gene: SENP1 SUMO1/sentrin specific peptidase 1".
  4. ↑ Xu Z, Chau SF, Lam KH, Chan HY, Ng TB, Au SW (Sep 2006). "Crystal structure of the SENP1 mutant C603S-SUMO complex reveals the hydrolytic mechanism of SUMO-specific protease". The Biochemical Journal. 398 (3): 345–52. doi:10.1042/BJ20060526. PMC 1559472. PMID 16712526.
  5. ↑ Shen LN, Dong C, Liu H, Naismith JH, Hay RT (2006). "The structure of SENP1-SUMO-2 complex suggests a structural basis for discrimination between SUMO paralogues during processing". The Biochemical Journal. 397 (2): 279–288. doi:10.1042/BJ20052030. PMC 1513277. PMID 16553580.
  6. ↑ Kim YH, Sung KS, Lee SJ, Kim YO, Choi CY, Kim Y (2005). "Desumoylation of homeodomain-interacting protein kinase 2 (HIPK2) through the cytoplasmic-nuclear shuttling of the SUMO-specific protease SENP1". FEBS Letters. 579 (27): 6272–6278. doi:10.1016/j.febslet.2005.10.010. PMID 16253240.
  7. ↑ http://www.uniprot.org/uniprot/Q9P0U3#ptm_processing
  8. ↑ Xu Z, Au SW (2005). "Mapping residues of SUMO precursors essential in differential maturation by SUMO-specific protease, SENP1". The Biochemical Journal. 386 (Pt 2): 325–330. doi:10.1042/BJ20041210. PMC 1134797. PMID 15487983.
  9. ↑ Xu Z, Chau SF, Lam KH, Chan HY, Ng TB, Au SW (2006). "Crystal structure of the SENP1 mutant C603S-SUMO complex reveals the hydrolytic mechanism of SUMO-specific protease". The Biochemical Journal. 398 (3): 345–52. doi:10.1042/BJ20060526. PMC 1559472. PMID 16712526.

Further reading

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