iEts/i in the Kidney—Unraveling the Molecular Mechanism Underlying Renal Damage in Salt-Sensitive Hypertension

Joseph C. Gigliotti; Thu H Lee

iEts/i in the Kidney—Unraveling the Molecular Mechanism Underlying Renal Damage in Salt-Sensitive Hypertension

College of Osteopathic Medicine

Research output: Contribution to journal › Article › peer-review

Abstract

Originally identified as a homolog of a viral oncogene (v-ets), the ETS family of transcription factors consists of over 25 proteins involved in regulating several biologic processes at the transcriptional level. The ETS DNA binding domain consists of a winged helix conformation and binds the DNA sequences 5′-GGA(A/T)-3′ with varying affinity depending on ETS phosphorylation status, epigenetic modifications, and various protein-protein interactions.

Original language	American English
Journal	Default journal
State	Published - Nov 1 2017

Keywords

hypertension
kidney injury
salt-sensitivity
inflammation

Disciplines

Medicine and Health Sciences

Access to Document

https://doi.org/10.1681/ASN.2017080917

Cite this

@article{b8b9eaf9a36445419aac82820acb5a96,

title = "iEts/i in the Kidney—Unraveling the Molecular Mechanism Underlying Renal Damage in Salt-Sensitive Hypertension",

abstract = " Originally identified as a homolog of a viral oncogene (v-ets), the ETS family of transcription factors consists of over 25 proteins involved in regulating several biologic processes at the transcriptional level. The ETS DNA binding domain consists of a winged helix conformation and binds the DNA sequences 5′-GGA(A/T)-3′ with varying affinity depending on ETS phosphorylation status, epigenetic modifications, and various protein-protein interactions.",

keywords = "hypertension, kidney injury, salt-sensitivity, inflammation",

author = "Gigliotti, {Joseph C.} and Lee, {Thu H}",

note = "Joseph C Gigliotti and Thu H. Lee, iEts/i in the Kidney—Unraveling the Molecular Mechanism Underlying Renal Damage in Salt-Sensitive Hypertension, Journal of the American Society of Nephrology, Volume 28, Issue 11, November 2017, Pages 3131-3133, https://doi.org/10.1681/ASN.2017080917",

year = "2017",

month = nov,

day = "1",

language = "American English",

journal = "Default journal",

}

TY - JOUR

T1 - iEts/i in the Kidney—Unraveling the Molecular Mechanism Underlying Renal Damage in Salt-Sensitive Hypertension

AU - Gigliotti, Joseph C.

AU - Lee, Thu H

N1 - Joseph C Gigliotti and Thu H. Lee, iEts/i in the Kidney—Unraveling the Molecular Mechanism Underlying Renal Damage in Salt-Sensitive Hypertension, Journal of the American Society of Nephrology, Volume 28, Issue 11, November 2017, Pages 3131-3133, https://doi.org/10.1681/ASN.2017080917

PY - 2017/11/1

Y1 - 2017/11/1

N2 - Originally identified as a homolog of a viral oncogene (v-ets), the ETS family of transcription factors consists of over 25 proteins involved in regulating several biologic processes at the transcriptional level. The ETS DNA binding domain consists of a winged helix conformation and binds the DNA sequences 5′-GGA(A/T)-3′ with varying affinity depending on ETS phosphorylation status, epigenetic modifications, and various protein-protein interactions.

AB - Originally identified as a homolog of a viral oncogene (v-ets), the ETS family of transcription factors consists of over 25 proteins involved in regulating several biologic processes at the transcriptional level. The ETS DNA binding domain consists of a winged helix conformation and binds the DNA sequences 5′-GGA(A/T)-3′ with varying affinity depending on ETS phosphorylation status, epigenetic modifications, and various protein-protein interactions.

KW - hypertension

KW - kidney injury

KW - salt-sensitivity

KW - inflammation

UR - https://digitalcommons.liberty.edu/lucom_fac_pubs/25

UR - https://doi.org/10.1681/ASN.2017080917

M3 - Article

JO - Default journal

JF - Default journal

ER -

iEts/i in the Kidney—Unraveling the Molecular Mechanism Underlying Renal Damage in Salt-Sensitive Hypertension

Abstract

Keywords

Disciplines

Access to Document

Other files and links

Cite this