AAMP (gene): Difference between revisions

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{{Infobox_gene}}
{{Infobox_gene}}
'''Angio-associated, migratory cell protein''', also known as '''AAMP''', is a [[protein]] which in humans is encoded by the ''AAMP'' [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: AAMP angio-associated, migratory cell protein| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=14| accessdate = }}</ref>. This protein has been conserved in evolution and is so common to lots of mammalian cells<ref name="Beckner AAMP">{{cite journal|last1=Beckner|first1=Marie E. | name-list-format = vanc |title=AAMP (angio-associated, migratory cell protein)|journal=Atlas of Genetics and Cytogenetics in Oncology and Haematology|date=March 2012|volume=16|issue=2|page=111-114|doi=10.4267/2042/46939}}</ref> and it also has a yeast homolog which is the protein YCR072c <ref name="Beckner 2">{{cite journal|last1=Beckner|first1=Marie E.|last2=Peterson|first2=Virginia A.|last3=Moul|first3=Douglas E.|title=Angio-associated migratory cell protein is expressed as an extracellular protein by blood-vessel-associated mesenchymal cells|journal=Microvascular research|date=18 May 1998|volume=57|page=347-352}}</ref><ref>{{cite journal|last1=Beckner|first1=ME|last2=Liotta|first2=LA|title=AAMP, a conserved protein with immunoglobulin and WD40 domains, regulates endothelial tube formation in vitro.|journal=Laboratory Investigation |date=July 1996|volume=75|issue=1|page=97-107|pmid=8683944}}</ref>.
'''Angio-associated, migratory cell protein''', also known as '''AAMP''', is a [[protein]] which in humans is encoded by the ''AAMP'' [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: AAMP angio-associated, migratory cell protein| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=14| accessdate = }}</ref> This protein has been conserved in evolution and is so common to many mammals. <ref name="Beckner AAMP">{{cite journal|last1=Beckner|first1=Marie E. | name-list-format = vanc |title = AAMP (angio-associated, migratory cell protein)|journal=Atlas of Genetics and Cytogenetics in Oncology and Haematology|date=March 2012|volume=16|issue=2|pages=111–114|doi=10.4267/2042/46939}}</ref> and it also has a yeast homolog which is the protein YCR072c.<ref name="Beckner 2">{{cite journal | vauthors = Beckner ME, Peterson VA, Moul DE | title = Angio-associated migratory cell protein is expressed as an extracellular protein by blood-vessel-associated mesenchymal cells | journal = Microvascular Research | volume = 57 | issue = 3 | pages = 347–52 | year = 1999 | pmid = 10329261 | doi = 10.1006/mvre.1999.2144 | url = }}</ref><ref>{{cite journal | vauthors = Beckner ME, Liotta LA | title = AAMP, a conserved protein with immunoglobulin and WD40 domains, regulates endothelial tube formation in vitro | journal = Laboratory Investigation; A Journal of Technical Methods and Pathology | volume = 75 | issue = 1 | pages = 97–107 | date = July 1996 | pmid = 8683944 }}</ref>


== Localisation ==
== Localisation ==


The gene is located on the second human chromosome, near the end of the chromosome's arm (2q35), between the codons 85-87 and 1387-1389. It contains 6042 bp and 11 [[exon|exons]]<ref name="Beckner AAMP" /> When transcripted, it gives a 1859 bp mRNA.
The gene is located on the second human chromosome, near the end of the chromosome's arm (2q35), between the codons 85-87 and 1387-1389. It contains 6042 bp and 11 [[exon]]s<ref name="Beckner AAMP" /> When transcribed, it gives a 1859 bp mRNA.
<ref name="Beckner AAMP" />. The [[vascular endothelial growth factor]] is a promoting factor of the protein synthesis and localisation in the different parts of the cells.<ref name = "Hu_2016" />.
.<ref name="Beckner AAMP" /> The [[vascular endothelial growth factor]] is a promoting factor of the protein synthesis and localisation in the different parts of the cells.<ref name = "Hu_2016" />
The protein's expression is higher in the intracellular than in the extracellularspace <ref name="Beckner 2">{{cite journal|last1=Beckner|first1=Marie E.|last2=Peterson|first2=Virginia A.|last3=Moul|first3=Douglas E.|title=Angio-associated migratory cell protein is expressed as an extracellular protein by blood-vessel-associated mesenchymal cells|journal=Microvascular research|date=18 May 1998|volume=57|page=347-352}}</ref>.
The protein's expression is higher in the intracellular than in the extracellular space.<ref name="Beckner 2"/>


== Function ==
== Function ==
Line 12: Line 12:
The gene product is an [[immunoglobulin]]-type protein of 434 amino acids and 49 kDa.<ref name="Beckner AAMP" /> It is found to be expressed strongly in the cytosol of [[endothelium|endothelial]] cells, [[cytotrophoblast]]s, and poorly differentiated colon [[adenocarcinoma]] cells found in lymphatics and has been observed at the luminal edges of [[endometrium|endometrial cells]] and in the extracellular environment of vascular-associated [[mesenchyme|mesenchymal]] cells.<ref name="Beckner AAMP" />
The gene product is an [[immunoglobulin]]-type protein of 434 amino acids and 49 kDa.<ref name="Beckner AAMP" /> It is found to be expressed strongly in the cytosol of [[endothelium|endothelial]] cells, [[cytotrophoblast]]s, and poorly differentiated colon [[adenocarcinoma]] cells found in lymphatics and has been observed at the luminal edges of [[endometrium|endometrial cells]] and in the extracellular environment of vascular-associated [[mesenchyme|mesenchymal]] cells.<ref name="Beckner AAMP" />


The protein contains a [[WD40 repeat|WD40 domain]] which permits multi-proteins complexes formation <ref name="Beckner AAMP"/> and a [[heparin]]-binding domain which mediates heparin-sensitive [[cell adhesion]]<ref name="entrez"/>.
The protein contains a [[WD40 repeat|WD40 domain]] which permits multi-proteins complexes formation <ref name="Beckner AAMP"/> and a [[heparin]]-binding domain which mediates heparin-sensitive [[cell adhesion]].<ref name="entrez"/>
AAMP helps to regulate vascular endothelial cell migration regulation and angiogenesis, with other signaling pathway like [[RhoA]]/[[Rho-associated protein kinase|Rho-kinase]] signaling.<ref name = "Hu_2016">{{cite journal | vauthors = Hu J, Qiu J, Zheng Y, Zhang T, Yin T, Xie X, Wang G | title = AAMP Regulates Endothelial Cell Migration and Angiogenesis Through RhoA/Rho Kinase Signaling | journal = Annals of Biomedical Engineering | volume = 44 | issue = 5 | pages = 1462–74 | date = May 2016 | pmid = 26350504 | doi = 10.1007/s10439-015-1442-0 }}</ref>.
AAMP helps to regulate vascular endothelial cell migration regulation and angiogenesis, with other signaling pathway like [[RhoA]]/[[Rho-associated protein kinase|Rho-kinase]] signaling.<ref name = "Hu_2016">{{cite journal | vauthors = Hu J, Qiu J, Zheng Y, Zhang T, Yin T, Xie X, Wang G | title = AAMP Regulates Endothelial Cell Migration and Angiogenesis Through RhoA/Rho Kinase Signaling | journal = Annals of Biomedical Engineering | volume = 44 | issue = 5 | pages = 1462–74 | date = May 2016 | pmid = 26350504 | doi = 10.1007/s10439-015-1442-0 }}</ref>  
A malfunction can therefore lead to different diseases (see Associated diseases). For example, in the smooth muscle cells, if AAMP is overexpressed, it activates RhoA, which activates Rho-kinase (this one generates GTP) and it finally leads to increased smooth muscle cell migration and division, causing [[atherosclerosis]] and [[restenosis]] <ref>{{cite journal|last1=Holvoet|first1=Paul|last2=Sinnaeve|first2=Peter|title=Angio-Associated Migratory Cell Protein and Smooth Muscle Cell Migration in Development of Restenosis and Atherosclerosis⁎⁎Editorials published in the Journal of the American College of Cardiology reflect the views of the authors and do not necessarily represent the views of JACC or the American College of Cardiology.|journal=Journal of the American College of Cardiology|date=July 2008|volume=52|issue=4|pages=312–314|doi=10.1016/j.jacc.2008.04.024}}</ref>.
A malfunction can therefore lead to different diseases (see Associated diseases). For example, in the smooth muscle cells, if AAMP is overexpressed, it activates RhoA, which activates Rho-kinase (this one generates GTP) and it finally leads to increased smooth muscle cell migration and division, causing [[atherosclerosis]] and [[restenosis]].<ref>{{cite journal | vauthors = Holvoet P, Sinnaeve P | title = Angio-associated migratory cell protein and smooth muscle cell migration in development of restenosis and atherosclerosis | journal = Journal of the American College of Cardiology | volume = 52 | issue = 4 | pages = 312–4 | date = July 2008 | pmid = 18634988 | doi = 10.1016/j.jacc.2008.04.024 }}</ref>


== Associated diseases ==  
== Associated diseases ==


Note : In all these diseases<ref name="Beckner AAMP">{{cite journal|last1=Beckner|first1=Marie E. | name-list-format = vanc |title=AAMP (angio-associated, migratory cell protein)|journal=Atlas of Genetics and Cytogenetics in Oncology and Haematology|date=March 2012|volume=16|issue=2|page=111-114|doi=10.4267/2042/46939}}</ref> we can observe the expression of the AAMP gene. This one can either remain stable, increase or decrease depending on the disease.  
Note : In all these diseases<ref name="Beckner AAMP"/> we can observe the expression of the AAMP gene. This one can either remain stable, increase or decrease depending on the disease.


List of the diseases : [[gastrointestinal stromal tumor]] (GIST) (for this disease and the ductal carcinomas, the expression levels are to correlate with necrosis in situ<ref>{{cite journal | vauthors = Bielig H, Zurek B, Kutsch A, Menning M, Philpott DJ, Sansonetti PJ, Kufer TA | title = A function for AAMP in Nod2-mediated NF-kappaB activation | journal = Molecular Immunology | volume = 46 | issue = 13 | pages = 2647–54 | date = August 2009 | pmid = 19535145 | doi = 10.1016/j.molimm.2009.04.022 }}</ref>), myeloid leukemia (chronic (CML) and [[Acute myeloid leukemia|acute]] (AML) forms), [[lymphoma]], [[breast cancer]], glial [[brain tumor|brain tumors]], colon neoplasia, epidermoid [[carcinoma]], [[cervical cancer]], [[ovarian cancer]], [[papillary thyroid cancer]], [[lung cancer|pulmonary cancer]], atherosclerosis, restenosis.
List of the diseases : [[gastrointestinal stromal tumor]] (GIST) (for this disease and the ductal carcinomas, the expression levels are to correlate with necrosis in situ<ref>{{cite journal | vauthors = Bielig H, Zurek B, Kutsch A, Menning M, Philpott DJ, Sansonetti PJ, Kufer TA | title = A function for AAMP in Nod2-mediated NF-kappaB activation | journal = Molecular Immunology | volume = 46 | issue = 13 | pages = 2647–54 | date = August 2009 | pmid = 19535145 | doi = 10.1016/j.molimm.2009.04.022 }}</ref>), myeloid leukemia (chronic (CML) and [[Acute myeloid leukemia|acute]] (AML) forms), [[lymphoma]], [[breast cancer]], glial [[brain tumor]]s, colon neoplasia, epidermoid [[carcinoma]], [[cervical cancer]], [[ovarian cancer]], [[papillary thyroid cancer]], [[lung cancer|pulmonary cancer]], atherosclerosis, restenosis.


== References ==
== References ==
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{{refbegin | 2}}
{{refbegin | 2}}
* {{cite journal | vauthors = Beckner ME, Krutzsch HC, Stracke ML, Williams ST, Gallardo JA, Liotta LA | title = Identification of a new immunoglobulin superfamily protein expressed in blood vessels with a heparin-binding consensus sequence | journal = Cancer Research | volume = 55 | issue = 10 | pages = 2140–9 | date = May 1995 | pmid = 7743515 | doi =  }}
* {{cite journal | vauthors = Beckner ME, Krutzsch HC, Stracke ML, Williams ST, Gallardo JA, Liotta LA | title = Identification of a new immunoglobulin superfamily protein expressed in blood vessels with a heparin-binding consensus sequence | journal = Cancer Research | volume = 55 | issue = 10 | pages = 2140–9 | date = May 1995 | pmid = 7743515 | 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 = January 1994 | pmid = 8125298 | doi = 10.1016/0378-1119(94)90802-8 }}
* {{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 = January 1994 | pmid = 8125298 | doi = 10.1016/0378-1119(94)90802-8 }}
* {{cite journal | vauthors = Beckner ME, Krutzsch HC, Klipstein S, Williams ST, Maguire JE, Doval M, Liotta LA | title = AAMP, a newly identified protein, shares a common epitope with alpha-actinin and a fast skeletal muscle fiber protein | journal = Experimental Cell Research | volume = 225 | issue = 2 | pages = 306–14 | date = June 1996 | pmid = 8660919 | doi = 10.1006/excr.1996.0181 }}
* {{cite journal | vauthors = Beckner ME, Krutzsch HC, Klipstein S, Williams ST, Maguire JE, Doval M, Liotta LA | title = AAMP, a newly identified protein, shares a common epitope with alpha-actinin and a fast skeletal muscle fiber protein | journal = Experimental Cell Research | volume = 225 | issue = 2 | pages = 306–14 | date = June 1996 | pmid = 8660919 | doi = 10.1006/excr.1996.0181 }}
* {{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 | 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 | vauthors = Beckner ME, Peterson VA, Moul DE | title = Angio-associated migratory cell protein is expressed as an extracellular protein by blood-vessel-associated mesenchymal cells | journal = Microvascular Research | volume = 57 | issue = 3 | pages = 347–52 | date = May 1999 | pmid = 10329261 | doi = 10.1006/mvre.1999.2144 }}
* {{cite journal | vauthors = Beckner ME, Jagannathan S, Peterson VA | title = Extracellular angio-associated migratory cell protein plays a positive role in angiogenesis and is regulated by astrocytes in coculture | journal = Microvascular Research | volume = 63 | issue = 3 | pages = 259–69 | date = May 2002 | pmid = 11969303 | doi = 10.1006/mvre.2001.2384 }}
* {{cite journal | vauthors = Beckner ME, Jagannathan S, Peterson VA | title = Extracellular angio-associated migratory cell protein plays a positive role in angiogenesis and is regulated by astrocytes in coculture | journal = Microvascular Research | volume = 63 | issue = 3 | pages = 259–69 | date = May 2002 | pmid = 11969303 | doi = 10.1006/mvre.2001.2384 }}
* {{cite journal | vauthors = Brandenberger R, Wei H, Zhang S, Lei S, Murage J, Fisk GJ, Li Y, Xu C, Fang R, Guegler K, Rao MS, Mandalam R, Lebkowski J, Stanton LW | title = Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation | journal = Nature Biotechnology | volume = 22 | issue = 6 | pages = 707–16 | date = June 2004 | pmid = 15146197 | doi = 10.1038/nbt971 }}
* {{cite journal | vauthors = Brandenberger R, Wei H, Zhang S, Lei S, Murage J, Fisk GJ, Li Y, Xu C, Fang R, Guegler K, Rao MS, Mandalam R, Lebkowski J, Stanton LW | title = Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation | journal = Nature Biotechnology | volume = 22 | issue = 6 | pages = 707–16 | date = June 2004 | pmid = 15146197 | doi = 10.1038/nbt971 }}
* {{cite journal | vauthors = Kimura K, Wakamatsu A, Suzuki Y, Ota T, Nishikawa T, Yamashita R, Yamamoto J, Sekine M, Tsuritani K, Wakaguri H, Ishii S, Sugiyama T, Saito K, Isono Y, Irie R, Kushida N, Yoneyama T, Otsuka R, Kanda K, Yokoi T, Kondo H, Wagatsuma M, Murakawa K, Ishida S, Ishibashi T, Takahashi-Fujii A, Tanase T, Nagai K, Kikuchi H, Nakai K, Isogai T, Sugano S | title = Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes | journal = Genome Research | volume = 16 | issue = 1 | pages = 55–65 | date = January 2006 | pmid = 16344560 | pmc = 1356129 | doi = 10.1101/gr.4039406 }}
* {{cite journal | vauthors = Kimura K, Wakamatsu A, Suzuki Y, Ota T, Nishikawa T, Yamashita R, Yamamoto J, Sekine M, Tsuritani K, Wakaguri H, Ishii S, Sugiyama T, Saito K, Isono Y, Irie R, Kushida N, Yoneyama T, Otsuka R, Kanda K, Yokoi T, Kondo H, Wagatsuma M, Murakawa K, Ishida S, Ishibashi T, Takahashi-Fujii A, Tanase T, Nagai K, Kikuchi H, Nakai K, Isogai T, Sugano S | title = Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes | journal = Genome Research | volume = 16 | issue = 1 | pages = 55–65 | date = January 2006 | pmid = 16344560 | pmc = 1356129 | doi = 10.1101/gr.4039406 }}
{{refend}}
{{refend}}


{{DEFAULTSORT:Aamp}}
{{DEFAULTSORT:Aamp}}


{{gene-2-stub}}
{{gene-2-stub}}

Latest revision as of 20:35, 20 July 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

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Angio-associated, migratory cell protein, also known as AAMP, is a protein which in humans is encoded by the AAMP gene.[1] This protein has been conserved in evolution and is so common to many mammals. [2] and it also has a yeast homolog which is the protein YCR072c.[3][4]

Localisation

The gene is located on the second human chromosome, near the end of the chromosome's arm (2q35), between the codons 85-87 and 1387-1389. It contains 6042 bp and 11 exons[2] When transcribed, it gives a 1859 bp mRNA. .[2] The vascular endothelial growth factor is a promoting factor of the protein synthesis and localisation in the different parts of the cells.[5] The protein's expression is higher in the intracellular than in the extracellular space.[3]

Function

The gene product is an immunoglobulin-type protein of 434 amino acids and 49 kDa.[2] It is found to be expressed strongly in the cytosol of endothelial cells, cytotrophoblasts, and poorly differentiated colon adenocarcinoma cells found in lymphatics and has been observed at the luminal edges of endometrial cells and in the extracellular environment of vascular-associated mesenchymal cells.[2]

The protein contains a WD40 domain which permits multi-proteins complexes formation [2] and a heparin-binding domain which mediates heparin-sensitive cell adhesion.[1] AAMP helps to regulate vascular endothelial cell migration regulation and angiogenesis, with other signaling pathway like RhoA/Rho-kinase signaling.[5] A malfunction can therefore lead to different diseases (see Associated diseases). For example, in the smooth muscle cells, if AAMP is overexpressed, it activates RhoA, which activates Rho-kinase (this one generates GTP) and it finally leads to increased smooth muscle cell migration and division, causing atherosclerosis and restenosis.[6]

Associated diseases

Note : In all these diseases[2] we can observe the expression of the AAMP gene. This one can either remain stable, increase or decrease depending on the disease.

List of the diseases : gastrointestinal stromal tumor (GIST) (for this disease and the ductal carcinomas, the expression levels are to correlate with necrosis in situ[7]), myeloid leukemia (chronic (CML) and acute (AML) forms), lymphoma, breast cancer, glial brain tumors, colon neoplasia, epidermoid carcinoma, cervical cancer, ovarian cancer, papillary thyroid cancer, pulmonary cancer, atherosclerosis, restenosis.

References

  1. ↑ 1.0 1.1 "Entrez Gene: AAMP angio-associated, migratory cell protein".
  2. ↑ 2.0 2.1 2.2 2.3 2.4 2.5 2.6 Beckner ME (March 2012). "AAMP (angio-associated, migratory cell protein)". Atlas of Genetics and Cytogenetics in Oncology and Haematology. 16 (2): 111–114. doi:10.4267/2042/46939.
  3. ↑ 3.0 3.1 Beckner ME, Peterson VA, Moul DE (1999). "Angio-associated migratory cell protein is expressed as an extracellular protein by blood-vessel-associated mesenchymal cells". Microvascular Research. 57 (3): 347–52. doi:10.1006/mvre.1999.2144. PMID 10329261.
  4. ↑ Beckner ME, Liotta LA (July 1996). "AAMP, a conserved protein with immunoglobulin and WD40 domains, regulates endothelial tube formation in vitro". Laboratory Investigation; A Journal of Technical Methods and Pathology. 75 (1): 97–107. PMID 8683944.
  5. ↑ 5.0 5.1 Hu J, Qiu J, Zheng Y, Zhang T, Yin T, Xie X, Wang G (May 2016). "AAMP Regulates Endothelial Cell Migration and Angiogenesis Through RhoA/Rho Kinase Signaling". Annals of Biomedical Engineering. 44 (5): 1462–74. doi:10.1007/s10439-015-1442-0. PMID 26350504.
  6. ↑ Holvoet P, Sinnaeve P (July 2008). "Angio-associated migratory cell protein and smooth muscle cell migration in development of restenosis and atherosclerosis". Journal of the American College of Cardiology. 52 (4): 312–4. doi:10.1016/j.jacc.2008.04.024. PMID 18634988.
  7. ↑ Bielig H, Zurek B, Kutsch A, Menning M, Philpott DJ, Sansonetti PJ, Kufer TA (August 2009). "A function for AAMP in Nod2-mediated NF-kappaB activation". Molecular Immunology. 46 (13): 2647–54. doi:10.1016/j.molimm.2009.04.022. PMID 19535145.

External links

Further reading

  • Beckner ME, Krutzsch HC, Stracke ML, Williams ST, Gallardo JA, Liotta LA (May 1995). "Identification of a new immunoglobulin superfamily protein expressed in blood vessels with a heparin-binding consensus sequence". Cancer Research. 55 (10): 2140–9. PMID 7743515.
  • Maruyama K, Sugano S (January 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.
  • Beckner ME, Krutzsch HC, Klipstein S, Williams ST, Maguire JE, Doval M, Liotta LA (June 1996). "AAMP, a newly identified protein, shares a common epitope with alpha-actinin and a fast skeletal muscle fiber protein". Experimental Cell Research. 225 (2): 306–14. doi:10.1006/excr.1996.0181. PMID 8660919.
  • 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.
  • Beckner ME, Jagannathan S, Peterson VA (May 2002). "Extracellular angio-associated migratory cell protein plays a positive role in angiogenesis and is regulated by astrocytes in coculture". Microvascular Research. 63 (3): 259–69. doi:10.1006/mvre.2001.2384. PMID 11969303.
  • Brandenberger R, Wei H, Zhang S, Lei S, Murage J, Fisk GJ, Li Y, Xu C, Fang R, Guegler K, Rao MS, Mandalam R, Lebkowski J, Stanton LW (June 2004). "Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation". Nature Biotechnology. 22 (6): 707–16. doi:10.1038/nbt971. PMID 15146197.
  • Kimura K, Wakamatsu A, Suzuki Y, Ota T, Nishikawa T, Yamashita R, Yamamoto J, Sekine M, Tsuritani K, Wakaguri H, Ishii S, Sugiyama T, Saito K, Isono Y, Irie R, Kushida N, Yoneyama T, Otsuka R, Kanda K, Yokoi T, Kondo H, Wagatsuma M, Murakawa K, Ishida S, Ishibashi T, Takahashi-Fujii A, Tanase T, Nagai K, Kikuchi H, Nakai K, Isogai T, Sugano S (January 2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Research. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.


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