Induction of HIF–1α in response to hypoxia is instantaneous

By U. R. Jewell, I. Kvietikova, A. Scheid, C. Bauer, Roland H. Wenger, M. Gassmann. The FASEB Journal, 2001

598 citations recorded by the source corpus.

Subfields: Cancer Research, Genetics, Physiology

View Paper: https://www.semanticscholar.org/paper/6f1c0cf1c3ddd0f05af43232031f35a0c32ab3ea

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Cancer Research

1. Roland H. Wenger
2. D. Stiehl
3. G. Camenisch
4. G. Semenza
5. M. C. Simon
6. C. V. Dang
7. P. Vaupel
8. Navdeep S. Chandel

In Genetics

1. G. Semenza
2. C. V. Dang
3. Navdeep S. Chandel
4. J. Espinosa
5. V. L. Dengler
6. M. Galbraith

In Physiology

1. Roland H. Wenger
2. G. Semenza
3. M. C. Simon
4. P. Trayhurn

Citations in the corpus

• Integration of Oxygen Signaling at the Consensus HRE (2005, background): “Thus, the high turnover rate of HIFα subunits enables the very rapid accumulation of HIFα under hypoxic conditions (14).”
• HIF‐1 is expressed in normoxic tissue and displays an organ‐specific regulation under systemic hypoxia (2001, background): “Oxygen concentrations in normal tissue range from 2 to 5%, in vitro, these concentrations produce a dramatic response with respect to HIF-1 activation (34, 35 ).”
• HIF-1, O(2), and the 3 PHDs: how animal cells signal hypoxia to the nucleus. (2001, background): “…factors in response to indicating that the induction of HIF-1 in response tochanges in the environmental O2 concentration have hypoxia is virtually instantaneous (Jewell et al., 2001)been delineated (for review, see Gilles-Gonzalez, 2001; argued against a complex signal-transduction pathway.”
• Cellular adaptation to hypoxia: O2‐sensing protein hydroxylases, hypoxia‐inducible transcription factors, and O2‐regulated gene expression (2002, background): “Hydroxylation of the HIF-1 ODD domain confers rapid degradation to the constitutively translated protein (58, 61).”