scholarly journals Correction to Inhibition of Hypoxia Inducible Factor 1–Transcription Coactivator Interaction by a Hydrogen Bond Surrogate α-Helix

2012 ◽  
Vol 134 (18) ◽  
pp. 8000-8000 ◽  
Author(s):  
Laura K. Henchey ◽  
Swati Kushal ◽  
Ramin Dubey ◽  
Ross N. Chapman ◽  
Bogdan Z. Olenyuk ◽  
...  
Keyword(s):  
Hydrogen Bond ◽  
Hypoxia Inducible Factor ◽  
Hypoxia Inducible Factor 1 ◽  
Hydrogen Bond Surrogate ◽  
Α Helix ◽  
Transcription Coactivator

scholarly journals Inhibition of Hypoxia Inducible Factor 1—Transcription Coactivator Interaction by a Hydrogen Bond Surrogate α-Helix

2010 ◽  
Vol 132 (3) ◽  
pp. 941-943 ◽  
Author(s):  
Laura K. Henchey ◽  
Swati Kushal ◽  
Ramin Dubey ◽  
Ross N. Chapman ◽  
Bogdan Z. Olenyuk ◽  
...  
Keyword(s):  
Hydrogen Bond ◽  
Hypoxia Inducible Factor ◽  
Hypoxia Inducible Factor 1 ◽  
Hydrogen Bond Surrogate ◽  
Α Helix ◽  
Transcription Coactivator

scholarly journals Reversible α-helix formation controlled by a hydrogen bond surrogate

Tetrahedron ◽  
2012 ◽  
Vol 68 (23) ◽  
pp. 4434-4437 ◽  
Author(s):  
Stephen E. Miller ◽  
Neville R. Kallenbach ◽  
Paramjit S. Arora
Keyword(s):  
Hydrogen Bond ◽  
Hydrogen Bond Surrogate ◽  
Helix Formation ◽  
Α Helix

A Highly Stable Short α-Helix Constrained by a Main-Chain Hydrogen-Bond Surrogate

2004 ◽  
Vol 126 (39) ◽  
pp. 12252-12253 ◽  
Author(s):  
Ross N. Chapman ◽  
Gianluca Dimartino ◽  
Paramjit S. Arora
Keyword(s):  
Hydrogen Bond ◽  
Main Chain ◽  
Hydrogen Bond Surrogate ◽  
Α Helix

Atomic Structure of a Short α-Helix Stabilized by a Main Chain Hydrogen-Bond Surrogate

2008 ◽  
Vol 130 (13) ◽  
pp. 4334-4337 ◽  
Author(s):  
Jie Liu ◽  
Deyun Wang ◽  
Qi Zheng ◽  
Min Lu ◽  
Paramjit S. Arora
Keyword(s):  
Hydrogen Bond ◽  
Atomic Structure ◽  
Main Chain ◽  
Hydrogen Bond Surrogate ◽  
Α Helix

Vascular adaptations to hypoxia: molecular and cellular mechanisms regulating vascular tone

2007 ◽  
Vol 43 ◽  
pp. 105-120 ◽  
Author(s):  
Michael L. Paffett ◽  
Benjimen R. Walker
Keyword(s):  
Vascular Tone ◽  
Cellular Proliferation ◽  
Hypoxic Pulmonary Vasoconstriction ◽  
Hypoxia Inducible Factor ◽  
Systemic Circulation ◽  
Cellular Mechanisms ◽  
Hypoxia Inducible Factor 1 ◽  
Pulmonary Vasoconstriction ◽  
Adaptive Mechanisms ◽  
Adaptive Processes

Several molecular and cellular adaptive mechanisms to hypoxia exist within the vasculature. Many of these processes involve oxygen sensing which is transduced into mediators of vasoconstriction in the pulmonary circulation and vasodilation in the systemic circulation. A variety of oxygen-responsive pathways, such as HIF (hypoxia-inducible factor)-1 and HOs (haem oxygenases), contribute to the overall adaptive process during hypoxia and are currently an area of intense research. Generation of ROS (reactive oxygen species) may also differentially regulate vascular tone in these circulations. Potential candidates underlying the divergent responses between the systemic and pulmonary circulations may include Nox (NADPH oxidase)-derived ROS and mitochondrial-derived ROS. In addition to alterations in ROS production governing vascular tone in the hypoxic setting, other vascular adaptations are likely to be involved. HPV (hypoxic pulmonary vasoconstriction) and CH (chronic hypoxia)-induced alterations in cellular proliferation, ionic conductances and changes in the contractile apparatus sensitivity to calcium, all occur as adaptive processes within the vasculature.

TAp73 opposes tumor angiogenesis by promoting hypoxia-inducible factor 1α degradation

2020 ◽  
Author(s):  
Lungwani Muungo
Keyword(s):  
Cancer Progression ◽  
Hypoxia Inducible Factor ◽  
Tumor Hypoxia ◽  
Human Lung Cancer ◽  
Regulatory Subunit ◽  
Patients With Cancer ◽  
Hypoxia Inducible Factor 1 ◽  
Chemically Induced ◽  
Induced Tumors ◽  
Patient Prognosis

Tumor hypoxia and hypoxia-inducible factor 1 (HIF-1) activationare associated with cancer progression. Here, we demonstrate thatthe transcription factor TAp73 opposes HIF-1 activity through anontranscriptional mechanism, thus affecting tumor angiogenesis.TAp73-deficient mice have an increased incidence of spontaneousand chemically induced tumors that also display enhanced vascularization.Mechanistically, TAp73 interacts with the regulatory subunit(α) of HIF-1 and recruits mouse double minute 2 homolog intothe protein complex, thus promoting HIF-1α polyubiquitination andconsequent proteasomal degradation in an oxygen-independentmanner. In human lung cancer datasets, TAp73 strongly predictsgood patient prognosis, and its expression is associated with lowHIF-1 activation and angiogenesis. Our findings, supported by invivo and clinical evidence, demonstrate a mechanism for oxygenindependentHIF-1 regulation, which has important implicationsfor individualizing therapies in patients with cancer.

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