MFSD2 (English Wikipedia)

Analysis of information sources in references of the Wikipedia article "MFSD2" in English language version.

Last modified: 02:08:17, 3 October 2026 (UTC)

Ref.Un. Ref.Website

Global rank English rank

1412nih.gov

5^th place

65doi.org

2^nd place

62ensembl.org

630^th place

326^th place

31uniprot.org

2,402^nd place

2,501^st place

22adsabs.harvard.edu

14^th place

9^th place

11web.archive.org

1^st place

11hms.harvard.edu

low place

7,550^th place

adsabs.harvard.edu (Global: 14^th place; English: 9^th place)

ui.adsabs.harvard.edu

Ben-Zvi A, Lacoste B, Kur E, Andreone BJ, Mayshar Y, Yan H, et al. (May 2014). "Mfsd2a is critical for the formation and function of the blood-brain barrier". Nature. 509 (7501): 507–511. Bibcode:2014Natur.509..507B. doi:10.1038/nature13324. PMC 4134871. PMID 24828040.
- Stephanie Dutchen (14 May 2014). "Breaking Through the Barrier". Harvard Medical School. Archived from the original on 15 May 2014.
- Reiling JH, Clish CB, Carette JE, Varadarajan M, Brummelkamp TR, Sabatini DM (July 2011). "A haploid genetic screen identifies the major facilitator domain containing 2A (MFSD2A) transporter as a key mediator in the response to tunicamycin". Proceedings of the National Academy of Sciences of the United States of America. 108 (29): 11756–11765. Bibcode:2011PNAS..10811756R. doi:10.1073/pnas.1018098108. PMC 3141996. PMID 21677192.

doi.org (Global: 2^nd place; English: 2^nd place)

Ben-Zvi A, Lacoste B, Kur E, Andreone BJ, Mayshar Y, Yan H, et al. (May 2014). "Mfsd2a is critical for the formation and function of the blood-brain barrier". Nature. 509 (7501): 507–511. Bibcode:2014Natur.509..507B. doi:10.1038/nature13324. PMC 4134871. PMID 24828040.
- Stephanie Dutchen (14 May 2014). "Breaking Through the Barrier". Harvard Medical School. Archived from the original on 15 May 2014.
- Perland E, Fredriksson R (March 2017). "Classification Systems of Secondary Active Transporters". Trends in Pharmacological Sciences. 38 (3): 305–315. doi:10.1016/j.tips.2016.11.008. PMID 27939446.
- Perland E, Bagchi S, Klaesson A, Fredriksson R (September 2017). "Characteristics of 29 novel atypical solute carriers of major facilitator superfamily type: evolutionary conservation, predicted structure and neuronal co-expression". Open Biology. 7 (9) 170142. doi:10.1098/rsob.170142. PMC 5627054. PMID 28878041.
- Angers M, Uldry M, Kong D, Gimble JM, Jetten AM (November 2008). "Mfsd2a encodes a novel major facilitator superfamily domain-containing protein highly induced in brown adipose tissue during fasting and adaptive thermogenesis". The Biochemical Journal. 416 (3): 347–355. doi:10.1042/BJ20080165. PMC 2587516. PMID 18694395.
- Reiling JH, Clish CB, Carette JE, Varadarajan M, Brummelkamp TR, Sabatini DM (July 2011). "A haploid genetic screen identifies the major facilitator domain containing 2A (MFSD2A) transporter as a key mediator in the response to tunicamycin". Proceedings of the National Academy of Sciences of the United States of America. 108 (29): 11756–11765. Bibcode:2011PNAS..10811756R. doi:10.1073/pnas.1018098108. PMC 3141996. PMID 21677192.

ensembl.org (Global: 630^th place; English: 326^th place)

may2017.archive.ensembl.org

GRCh38: Ensembl release 89: ENSG00000168389 – Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000028655 – Ensembl, May 2017

hms.harvard.edu (Global: low place; English: 7,550^th place)

Ben-Zvi A, Lacoste B, Kur E, Andreone BJ, Mayshar Y, Yan H, et al. (May 2014). "Mfsd2a is critical for the formation and function of the blood-brain barrier". Nature. 509 (7501): 507–511. Bibcode:2014Natur.509..507B. doi:10.1038/nature13324. PMC 4134871. PMID 24828040.
- Stephanie Dutchen (14 May 2014). "Breaking Through the Barrier". Harvard Medical School. Archived from the original on 15 May 2014.

nih.gov (Global: 5^th place; English: 5^th place)

ncbi.nlm.nih.gov

"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
Ben-Zvi A, Lacoste B, Kur E, Andreone BJ, Mayshar Y, Yan H, et al. (May 2014). "Mfsd2a is critical for the formation and function of the blood-brain barrier". Nature. 509 (7501): 507–511. Bibcode:2014Natur.509..507B. doi:10.1038/nature13324. PMC 4134871. PMID 24828040.
- Stephanie Dutchen (14 May 2014). "Breaking Through the Barrier". Harvard Medical School. Archived from the original on 15 May 2014.
- Perland E, Bagchi S, Klaesson A, Fredriksson R (September 2017). "Characteristics of 29 novel atypical solute carriers of major facilitator superfamily type: evolutionary conservation, predicted structure and neuronal co-expression". Open Biology. 7 (9) 170142. doi:10.1098/rsob.170142. PMC 5627054. PMID 28878041.
- Angers M, Uldry M, Kong D, Gimble JM, Jetten AM (November 2008). "Mfsd2a encodes a novel major facilitator superfamily domain-containing protein highly induced in brown adipose tissue during fasting and adaptive thermogenesis". The Biochemical Journal. 416 (3): 347–355. doi:10.1042/BJ20080165. PMC 2587516. PMID 18694395.
- "Entrez Gene: MFSD2 major facilitator superfamily domain containing 2".
- Reiling JH, Clish CB, Carette JE, Varadarajan M, Brummelkamp TR, Sabatini DM (July 2011). "A haploid genetic screen identifies the major facilitator domain containing 2A (MFSD2A) transporter as a key mediator in the response to tunicamycin". Proceedings of the National Academy of Sciences of the United States of America. 108 (29): 11756–11765. Bibcode:2011PNAS..10811756R. doi:10.1073/pnas.1018098108. PMC 3141996. PMID 21677192.
pubmed.ncbi.nlm.nih.gov
- Ben-Zvi A, Lacoste B, Kur E, Andreone BJ, Mayshar Y, Yan H, et al. (May 2014). "Mfsd2a is critical for the formation and function of the blood-brain barrier". Nature. 509 (7501): 507–511. Bibcode:2014Natur.509..507B. doi:10.1038/nature13324. PMC 4134871. PMID 24828040.
  - Stephanie Dutchen (14 May 2014). "Breaking Through the Barrier". Harvard Medical School. Archived from the original on 15 May 2014.
  - Perland E, Fredriksson R (March 2017). "Classification Systems of Secondary Active Transporters". Trends in Pharmacological Sciences. 38 (3): 305–315. doi:10.1016/j.tips.2016.11.008. PMID 27939446.
  - Perland E, Bagchi S, Klaesson A, Fredriksson R (September 2017). "Characteristics of 29 novel atypical solute carriers of major facilitator superfamily type: evolutionary conservation, predicted structure and neuronal co-expression". Open Biology. 7 (9) 170142. doi:10.1098/rsob.170142. PMC 5627054. PMID 28878041.
  - Angers M, Uldry M, Kong D, Gimble JM, Jetten AM (November 2008). "Mfsd2a encodes a novel major facilitator superfamily domain-containing protein highly induced in brown adipose tissue during fasting and adaptive thermogenesis". The Biochemical Journal. 416 (3): 347–355. doi:10.1042/BJ20080165. PMC 2587516. PMID 18694395.
  - Reiling JH, Clish CB, Carette JE, Varadarajan M, Brummelkamp TR, Sabatini DM (July 2011). "A haploid genetic screen identifies the major facilitator domain containing 2A (MFSD2A) transporter as a key mediator in the response to tunicamycin". Proceedings of the National Academy of Sciences of the United States of America. 108 (29): 11756–11765. Bibcode:2011PNAS..10811756R. doi:10.1073/pnas.1018098108. PMC 3141996. PMID 21677192.

uniprot.org (Global: 2,402^nd place; English: 2,501^st place)

"Sodium-dependent lysophosphatidylcholine symporter 1". UniProt. Retrieved 2 April 2016.

web.archive.org (Global: 1^st place; English: 1^st place)

Ben-Zvi A, Lacoste B, Kur E, Andreone BJ, Mayshar Y, Yan H, et al. (May 2014). "Mfsd2a is critical for the formation and function of the blood-brain barrier". Nature. 509 (7501): 507–511. Bibcode:2014Natur.509..507B. doi:10.1038/nature13324. PMC 4134871. PMID 24828040.
- Stephanie Dutchen (14 May 2014). "Breaking Through the Barrier". Harvard Medical School. Archived from the original on 15 May 2014.

MFSD2 (English Wikipedia)

adsabs.harvard.edu (Global: 14th place; English: 9th place)

ui.adsabs.harvard.edu

doi.org (Global: 2nd place; English: 2nd place)

ensembl.org (Global: 630th place; English: 326th place)

may2017.archive.ensembl.org

hms.harvard.edu (Global: low place; English: 7,550th place)

nih.gov (Global: 5th place; English: 5th place)