CPM (gene): Difference between revisions

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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
'''Carboxypeptidase M''' is an [[enzyme]] that in humans is encoded by the ''CPM'' [[gene]].<ref name="pmid8586455">{{cite journal | vauthors = Kas K, Schoenmakers EF, Van de Ven WJ | title = Physical map location of the human carboxypeptidase M gene (CPM) distal to D12S375 and proximal to D12S8 at chromosome 12q15 | journal = Genomics | volume = 30 | issue = 2 | pages = 403–5 | date = November 1995 | pmid = 8586455 | pmc = | doi =  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: CPM carboxypeptidase M| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1368| 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
| image = PBB_Protein_CPM_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1uwy.
| PDB = {{PDB2|1uwy}}
| Name = Carboxypeptidase M
| HGNCid = 2311
| Symbol = CPM
| AltSymbols =;
| OMIM = 114860
| ECnumber = 
| Homologene = 35367
| MGIid = 1917824
| GeneAtlas_image1 = PBB_GE_CPM_206100_at_tn.png
| Function = {{GNF_GO|id=GO:0004182 |text = carboxypeptidase A activity}} {{GNF_GO|id=GO:0008199 |text = ferric iron binding}} {{GNF_GO|id=GO:0008237 |text = metallopeptidase activity}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}} {{GNF_GO|id=GO:0048503 |text = GPI anchor binding}}
| Component = {{GNF_GO|id=GO:0005886 |text = plasma membrane}}
| Process = {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0006725 |text = aromatic compound metabolic process}} {{GNF_GO|id=GO:0009653 |text = anatomical structure morphogenesis}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 1368
    | Hs_Ensembl = ENSG00000135678
    | Hs_RefseqProtein = NP_001005502
    | Hs_RefseqmRNA = NM_001005502
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 12
    | Hs_GenLoc_start = 67531227
    | Hs_GenLoc_end = 67612891
    | Hs_Uniprot = P14384
    | Mm_EntrezGene = 70574
    | Mm_Ensembl = ENSMUSG00000020183
    | Mm_RefseqmRNA = XM_917914
    | Mm_RefseqProtein = XP_923007
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 10
    | Mm_GenLoc_start = 117032498
    | Mm_GenLoc_end = 117088295
    | Mm_Uniprot = Q80V42
  }}
}}
'''Carboxypeptidase M''', also known as '''CPM''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CPM carboxypeptidase M| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1368| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
The protein encoded by this gene is a membrane-bound arginine/lysine [[carboxypeptidase]]. Its [[gene expression|expression]] is associated with [[monocyte]] to [[macrophage]] differentiation. This encoded protein contains [[hydrophobic]] regions at the amino and carboxy termini and has 6 potential [[asparagine]]-linked [[glycosylation]] sites. The active site residues of carboxypeptidases A and B are conserved in this protein. Three alternatively spliced [[transcript variants]] encoding the same protein have been described for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: CPM carboxypeptidase M| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1368| accessdate = }}</ref>
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is a membrane-bound arginine/lysine carboxypeptidase. Its expression is associated with monocyte to macrophage differentiation. This encoded protein contains hydrophobic regions at the amino and carboxy termini and has 6 potential asparagine-linked glycosylation sites. The active site residues of carboxypeptidases A and B are conserved in this protein. Three alternatively spliced transcript variants encoding the same protein have been described for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: CPM carboxypeptidase M| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1368| accessdate = }}</ref>
}}


==References==
== References ==
{{reflist|2}}
{{reflist}}
==Further reading==
 
== External links ==
* {{UCSC gene info|CPM}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Fujiwara H, Imai K, Inoue T, Maeda M, Fujii S | title = Membrane-bound cell surface peptidases in reproductive organs | journal = Endocrine Journal | volume = 46 | issue = 1 | pages = 11–25 | date = February 1999 | pmid = 10426564 | doi = 10.1507/endocrj.46.11 }}
| citations =
* {{cite journal | vauthors = Rehli M, Krause SW, Andreesen R | title = The membrane-bound ectopeptidase CPM as a marker of macrophage maturation in vitro and in vivo | journal = Advances in Experimental Medicine and Biology | volume = 477 | issue =  | pages = 205–16 | year = 2000 | pmid = 10849748 | doi = 10.1007/0-306-46826-3_23 }}
*{{cite journal | author=Fujiwara H, Imai K, Inoue T, ''et al.'' |title=Membrane-bound cell surface peptidases in reproductive organs. |journal=Endocr. J. |volume=46 |issue= 1 |pages= 11-25 |year= 1999 |pmid= 10426564 |doi= }}
* {{cite journal | vauthors = Nagae A, Deddish PA, Becker RP, Anderson CH, Abe M, Tan F, Skidgel RA, Erdös EG | title = Carboxypeptidase M in brain and peripheral nerves | journal = Journal of Neurochemistry | volume = 59 | issue = 6 | pages = 2201–12 | date = December 1992 | pmid = 1431901 | doi = 10.1111/j.1471-4159.1992.tb10112.x }}
*{{cite journal | author=Rehli M, Krause SW, Andreesen R |title=The membrane-bound ectopeptidase CPM as a marker of macrophage maturation in vitro and in vivo. |journal=Adv. Exp. Med. Biol. |volume=477 |issue=  |pages= 205-16 |year= 2000 |pmid= 10849748 |doi= }}
* {{cite journal | vauthors = Tan F, Chan SJ, Steiner DF, Schilling JW, Skidgel RA | title = Molecular cloning and sequencing of the cDNA for human membrane-bound carboxypeptidase M. Comparison with carboxypeptidases A, B, H, and N | journal = The Journal of Biological Chemistry | volume = 264 | issue = 22 | pages = 13165–70 | date = August 1989 | pmid = 2753907 | doi =  }}
*{{cite journal | author=Nagae A, Deddish PA, Becker RP, ''et al.'' |title=Carboxypeptidase M in brain and peripheral nerves. |journal=J. Neurochem. |volume=59 |issue= 6 |pages= 2201-12 |year= 1992 |pmid= 1431901 |doi= }}
* {{cite journal | vauthors = Skidgel RA, Davis RM, Tan F | title = Human carboxypeptidase M. Purification and characterization of a membrane-bound carboxypeptidase that cleaves peptide hormones | journal = The Journal of Biological Chemistry | volume = 264 | issue = 4 | pages = 2236–41 | date = February 1989 | pmid = 2914904 | doi =  }}
*{{cite journal | author=Tan F, Chan SJ, Steiner DF, ''et al.'' |title=Molecular cloning and sequencing of the cDNA for human membrane-bound carboxypeptidase M. Comparison with carboxypeptidases A, B, H, and N. |journal=J. Biol. Chem. |volume=264 |issue= 22 |pages= 13165-70 |year= 1989 |pmid= 2753907 |doi=  }}
* {{cite journal | vauthors = McGwire GB, Skidgel RA | title = Extracellular conversion of epidermal growth factor (EGF) to des-Arg53-EGF by carboxypeptidase M | journal = The Journal of Biological Chemistry | volume = 270 | issue = 29 | pages = 17154–8 | date = July 1995 | pmid = 7615511 | doi = 10.1074/jbc.270.29.17154 }}
*{{cite journal | author=Skidgel RA, Davis RM, Tan F |title=Human carboxypeptidase M. Purification and characterization of a membrane-bound carboxypeptidase that cleaves peptide hormones. |journal=J. Biol. Chem. |volume=264 |issue= 4 |pages= 2236-41 |year= 1989 |pmid= 2914904 |doi=  }}
* {{cite journal | vauthors = de Saint-Vis B, Cupillard L, Pandrau-Garcia D, Ho S, Renard N, Grouard G, Duvert V, Thomas X, Galizzi JP, Banchereau J | title = Distribution of carboxypeptidase M on lymphoid and myeloid cells parallels the other zinc-dependent proteases CD10 and CD13|authorlink10=Jacques Banchereau | journal = Blood | volume = 86 | issue = 3 | pages = 1098–105 | date = August 1995 | pmid = 7620164 | doi =  }}
*{{cite journal | author=McGwire GB, Skidgel RA |title=Extracellular conversion of epidermal growth factor (EGF) to des-Arg53-EGF by carboxypeptidase M. |journal=J. Biol. Chem. |volume=270 |issue= 29 |pages= 17154-8 |year= 1995 |pmid= 7615511 |doi= }}
* {{cite journal | vauthors = Rehli M, Krause SW, Kreutz M, Andreesen R | title = Carboxypeptidase M is identical to the MAX.1 antigen and its expression is associated with monocyte to macrophage differentiation | journal = The Journal of Biological Chemistry | volume = 270 | issue = 26 | pages = 15644–9 | date = June 1995 | pmid = 7797563 | doi = 10.1074/jbc.270.26.15644 }}
*{{cite journal | author=de Saint-Vis B, Cupillard L, Pandrau-Garcia D, ''et al.'' |title=Distribution of carboxypeptidase M on lymphoid and myeloid cells parallels the other zinc-dependent proteases CD10 and CD13. |journal=Blood |volume=86 |issue= 3 |pages= 1098-105 |year= 1995 |pmid= 7620164 |doi=  }}
* {{cite journal | vauthors = Nagae A, Abe M, Becker RP, Deddish PA, Skidgel RA, Erdös EG | title = High concentration of carboxypeptidase M in lungs: presence of the enzyme in alveolar type I cells | journal = American Journal of Respiratory Cell and Molecular Biology | volume = 9 | issue = 2 | pages = 221–9 | date = August 1993 | pmid = 8338689 | doi = 10.1165/ajrcmb/9.2.221 }}
*{{cite journal | author=Rehli M, Krause SW, Kreutz M, Andreesen R |title=Carboxypeptidase M is identical to the MAX.1 antigen and its expression is associated with monocyte to macrophage differentiation. |journal=J. Biol. Chem. |volume=270 |issue= 26 |pages= 15644-9 |year= 1995 |pmid= 7797563 |doi= }}
* {{cite journal | vauthors = Michel B, Igić R, Leray V, Deddish PA, Erdös EG | title = Removal of Arg141 from the alpha chain of human hemoglobin by carboxypeptidases N and M | journal = Circulation Research | volume = 78 | issue = 4 | pages = 635–42 | date = April 1996 | pmid = 8635221 | doi = 10.1161/01.res.78.4.635 }}
*{{cite journal | author=Nagae A, Abe M, Becker RP, ''et al.'' |title=High concentration of carboxypeptidase M in lungs: presence of the enzyme in alveolar type I cells. |journal=Am. J. Respir. Cell Mol. Biol. |volume=9 |issue= 2 |pages= 221-9 |year= 1993 |pmid= 8338689 |doi= }}
* {{cite journal | vauthors = Skidgel RA, McGwire GB, Li XY | title = Membrane anchoring and release of carboxypeptidase M: implications for extracellular hydrolysis of peptide hormones | journal = Immunopharmacology | volume = 32 | issue = 1–3 | pages = 48–52 | date = May 1996 | pmid = 8796265 | doi = 10.1016/0162-3109(96)00008-2 }}
*{{cite journal  | author=Kas K, Schoenmakers EF, Van de Ven WJ |title=Physical map location of the human carboxypeptidase M gene (CPM) distal to D12S375 and proximal to D12S8 at chromosome 12q15. |journal=Genomics |volume=30 |issue= 2 |pages= 403-5 |year= 1996 |pmid= 8586455 |doi=  }}
* {{cite journal | vauthors = Bonaldo MF, Lennon G, Soares MB | title = Normalization and subtraction: two approaches to facilitate gene discovery | journal = Genome Research | volume = 6 | issue = 9 | pages = 791–806 | date = September 1996 | pmid = 8889548 | doi = 10.1101/gr.6.9.791 }}
*{{cite journal | author=Michel B, Igić R, Leray V, ''et al.'' |title=Removal of Arg141 from the alpha chain of human hemoglobin by carboxypeptidases N and M. |journal=Circ. Res. |volume=78 |issue= 4 |pages= 635-42 |year= 1996 |pmid= 8635221 |doi= }}
* {{cite journal | vauthors = Yoshioka S, Fujiwara H, Yamada S, Nakayama T, Higuchi T, Inoue T, Mori T, Maeda M | title = Membrane-bound carboxypeptidase-M is expressed on human ovarian follicles and corpora lutea of menstrual cycle and early pregnancy | journal = Molecular Human Reproduction | volume = 4 | issue = 7 | pages = 709–17 | date = July 1998 | pmid = 9701794 | doi = 10.1093/molehr/4.7.709 }}
*{{cite journal | author=Skidgel RA, McGwire GB, Li XY |title=Membrane anchoring and release of carboxypeptidase M: implications for extracellular hydrolysis of peptide hormones. |journal=Immunopharmacology |volume=32 |issue= 1-3 |pages= 48-52 |year= 1997 |pmid= 8796265 |doi= }}
* {{cite journal | vauthors = Li XY, Skidgel RA | title = Release of glycosylphosphatidylinositol-anchored carboxypeptidase M by phosphatidylinositol-specific phospholipase C upregulates enzyme synthesis | journal = Biochemical and Biophysical Research Communications | volume = 258 | issue = 1 | pages = 204–10 | date = April 1999 | pmid = 10222261 | doi = 10.1006/bbrc.1999.0619 }}
*{{cite journal | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791-806 |year= 1997 |pmid= 8889548 |doi= }}
* {{cite journal | vauthors = Bektas A, Hughes JN, Warram JH, Krolewski AS, Doria A | title = Type 2 diabetes locus on 12q15. Further mapping and mutation screening of two candidate genes | journal = Diabetes | volume = 50 | issue = 1 | pages = 204–8 | date = January 2001 | pmid = 11147789 | doi = 10.2337/diabetes.50.1.204 }}
*{{cite journal | author=Yoshioka S, Fujiwara H, Yamada S, ''et al.'' |title=Membrane-bound carboxypeptidase-M is expressed on human ovarian follicles and corpora lutea of menstrual cycle and early pregnancy. |journal=Mol. Hum. Reprod. |volume=4 |issue= 7 |pages= 709-17 |year= 1998 |pmid= 9701794 |doi= }}
* {{cite journal | vauthors = Suzuki Y, Taira H, Tsunoda T, Mizushima-Sugano J, Sese J, Hata H, Ota T, Isogai T, Tanaka T, Morishita S, Okubo K, Sakaki Y, Nakamura Y, Suyama A, Sugano S | title = Diverse transcriptional initiation revealed by fine, large-scale mapping of mRNA start sites | journal = EMBO Reports | volume = 2 | issue = 5 | pages = 388–93 | date = May 2001 | pmid = 11375929 | pmc = 1083880 | doi = 10.1093/embo-reports/kve085 }}
*{{cite journal | author=Li XY, Skidgel RA |title=Release of glycosylphosphatidylinositol-anchored carboxypeptidase M by phosphatidylinositol-specific phospholipase C upregulates enzyme synthesis. |journal=Biochem. Biophys. Res. Commun. |volume=258 |issue= 1 |pages= 204-10 |year= 1999 |pmid= 10222261 |doi= 10.1006/bbrc.1999.0619 }}
* {{cite journal | vauthors = Lendeckel U, Arndt M, Wrenger S, Nepple K, Huth C, Ansorge S, Klein HU, Goette A | title = Expression and activity of ectopeptidases in fibrillating human atria | journal = Journal of Molecular and Cellular Cardiology | volume = 33 | issue = 6 | pages = 1273–81 | date = June 2001 | pmid = 11444929 | doi = 10.1006/jmcc.2001.1389 }}
*{{cite journal | author=Bektas A, Hughes JN, Warram JH, ''et al.'' |title=Type 2 diabetes locus on 12q15. Further mapping and mutation screening of two candidate genes. |journal=Diabetes |volume=50 |issue= 1 |pages= 204-8 |year= 2001 |pmid= 11147789 |doi= }}
*{{cite journal | author=Suzuki Y, Taira H, Tsunoda T, ''et al.'' |title=Diverse transcriptional initiation revealed by fine, large-scale mapping of mRNA start sites. |journal=EMBO Rep. |volume=2 |issue= 5 |pages= 388-93 |year= 2001 |pmid= 11375929 |doi= 10.1093/embo-reports/kve085 }}
*{{cite journal | author=Lendeckel U, Arndt M, Wrenger S, ''et al.'' |title=Expression and activity of ectopeptidases in fibrillating human atria. |journal=J. Mol. Cell. Cardiol. |volume=33 |issue= 6 |pages= 1273-81 |year= 2001 |pmid= 11444929 |doi= 10.1006/jmcc.2001.1389 }}
}}
{{refend}}
{{refend}}
{{PDB Gallery|geneid=1368}}


{{protein-stub}}
{{gene-12-stub}}
{{WikiDoc Sources}}

Latest revision as of 21:38, 14 December 2018

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

Carboxypeptidase M is an enzyme that in humans is encoded by the CPM gene.[1][2]

Function

The protein encoded by this gene is a membrane-bound arginine/lysine carboxypeptidase. Its expression is associated with monocyte to macrophage differentiation. This encoded protein contains hydrophobic regions at the amino and carboxy termini and has 6 potential asparagine-linked glycosylation sites. The active site residues of carboxypeptidases A and B are conserved in this protein. Three alternatively spliced transcript variants encoding the same protein have been described for this gene.[2]

References

  1. ↑ Kas K, Schoenmakers EF, Van de Ven WJ (November 1995). "Physical map location of the human carboxypeptidase M gene (CPM) distal to D12S375 and proximal to D12S8 at chromosome 12q15". Genomics. 30 (2): 403–5. PMID 8586455.
  2. ↑ 2.0 2.1 "Entrez Gene: CPM carboxypeptidase M".

External links

Further reading

  • Fujiwara H, Imai K, Inoue T, Maeda M, Fujii S (February 1999). "Membrane-bound cell surface peptidases in reproductive organs". Endocrine Journal. 46 (1): 11–25. doi:10.1507/endocrj.46.11. PMID 10426564.
  • Rehli M, Krause SW, Andreesen R (2000). "The membrane-bound ectopeptidase CPM as a marker of macrophage maturation in vitro and in vivo". Advances in Experimental Medicine and Biology. 477: 205–16. doi:10.1007/0-306-46826-3_23. PMID 10849748.
  • Nagae A, Deddish PA, Becker RP, Anderson CH, Abe M, Tan F, Skidgel RA, Erdös EG (December 1992). "Carboxypeptidase M in brain and peripheral nerves". Journal of Neurochemistry. 59 (6): 2201–12. doi:10.1111/j.1471-4159.1992.tb10112.x. PMID 1431901.
  • Tan F, Chan SJ, Steiner DF, Schilling JW, Skidgel RA (August 1989). "Molecular cloning and sequencing of the cDNA for human membrane-bound carboxypeptidase M. Comparison with carboxypeptidases A, B, H, and N". The Journal of Biological Chemistry. 264 (22): 13165–70. PMID 2753907.
  • Skidgel RA, Davis RM, Tan F (February 1989). "Human carboxypeptidase M. Purification and characterization of a membrane-bound carboxypeptidase that cleaves peptide hormones". The Journal of Biological Chemistry. 264 (4): 2236–41. PMID 2914904.
  • McGwire GB, Skidgel RA (July 1995). "Extracellular conversion of epidermal growth factor (EGF) to des-Arg53-EGF by carboxypeptidase M". The Journal of Biological Chemistry. 270 (29): 17154–8. doi:10.1074/jbc.270.29.17154. PMID 7615511.
  • de Saint-Vis B, Cupillard L, Pandrau-Garcia D, Ho S, Renard N, Grouard G, Duvert V, Thomas X, Galizzi JP, Banchereau J (August 1995). "Distribution of carboxypeptidase M on lymphoid and myeloid cells parallels the other zinc-dependent proteases CD10 and CD13". Blood. 86 (3): 1098–105. PMID 7620164.
  • Rehli M, Krause SW, Kreutz M, Andreesen R (June 1995). "Carboxypeptidase M is identical to the MAX.1 antigen and its expression is associated with monocyte to macrophage differentiation". The Journal of Biological Chemistry. 270 (26): 15644–9. doi:10.1074/jbc.270.26.15644. PMID 7797563.
  • Nagae A, Abe M, Becker RP, Deddish PA, Skidgel RA, Erdös EG (August 1993). "High concentration of carboxypeptidase M in lungs: presence of the enzyme in alveolar type I cells". American Journal of Respiratory Cell and Molecular Biology. 9 (2): 221–9. doi:10.1165/ajrcmb/9.2.221. PMID 8338689.
  • Michel B, Igić R, Leray V, Deddish PA, Erdös EG (April 1996). "Removal of Arg141 from the alpha chain of human hemoglobin by carboxypeptidases N and M". Circulation Research. 78 (4): 635–42. doi:10.1161/01.res.78.4.635. PMID 8635221.
  • Skidgel RA, McGwire GB, Li XY (May 1996). "Membrane anchoring and release of carboxypeptidase M: implications for extracellular hydrolysis of peptide hormones". Immunopharmacology. 32 (1–3): 48–52. doi:10.1016/0162-3109(96)00008-2. PMID 8796265.
  • Bonaldo MF, Lennon G, Soares MB (September 1996). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Research. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
  • Yoshioka S, Fujiwara H, Yamada S, Nakayama T, Higuchi T, Inoue T, Mori T, Maeda M (July 1998). "Membrane-bound carboxypeptidase-M is expressed on human ovarian follicles and corpora lutea of menstrual cycle and early pregnancy". Molecular Human Reproduction. 4 (7): 709–17. doi:10.1093/molehr/4.7.709. PMID 9701794.
  • Li XY, Skidgel RA (April 1999). "Release of glycosylphosphatidylinositol-anchored carboxypeptidase M by phosphatidylinositol-specific phospholipase C upregulates enzyme synthesis". Biochemical and Biophysical Research Communications. 258 (1): 204–10. doi:10.1006/bbrc.1999.0619. PMID 10222261.
  • Bektas A, Hughes JN, Warram JH, Krolewski AS, Doria A (January 2001). "Type 2 diabetes locus on 12q15. Further mapping and mutation screening of two candidate genes". Diabetes. 50 (1): 204–8. doi:10.2337/diabetes.50.1.204. PMID 11147789.
  • Suzuki Y, Taira H, Tsunoda T, Mizushima-Sugano J, Sese J, Hata H, Ota T, Isogai T, Tanaka T, Morishita S, Okubo K, Sakaki Y, Nakamura Y, Suyama A, Sugano S (May 2001). "Diverse transcriptional initiation revealed by fine, large-scale mapping of mRNA start sites". EMBO Reports. 2 (5): 388–93. doi:10.1093/embo-reports/kve085. PMC 1083880. PMID 11375929.
  • Lendeckel U, Arndt M, Wrenger S, Nepple K, Huth C, Ansorge S, Klein HU, Goette A (June 2001). "Expression and activity of ectopeptidases in fibrillating human atria". Journal of Molecular and Cellular Cardiology. 33 (6): 1273–81. doi:10.1006/jmcc.2001.1389. PMID 11444929.


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