Stephen Gerard Flynn
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Stephen Gerard Flynn has a total of 21 co-authors. Here are the top co-authors by number of shared publications:
James M Peyton
Department of Anesthesiology Critical Care and Pain Medicine, Boston Children’s Hospital, Boston, Massachusetts, USA
2 shared publicationsMary Lyn Stein
Department of Anesthesiology Critical Care and Pain Medicine, Boston Children’s Hospital, Boston, Massachusetts, USA
2 shared publicationsPete G Kovatsis
Department of Anesthesiology Critical Care and Pain Medicine, Boston Children’s Hospital, Boston, Massachusetts, USA
2 shared publicationsRaymond S Park
Department of Anesthesiology Critical Care and Pain Medicine, Boston Children’s Hospital, Boston, Massachusetts, USA
2 shared publications- Samuel Y. Kim
Department of Anesthesiology, Critical Care and Pain Medicine, Boston Children’s Hospital, Boston, Massachusetts
2 shared publications Anupam B Jena
Department of Health Care Policy, Harvard Medical School, Boston, MA, USA
1 shared publication
Latest Publications
- Open Access
- 9 October 2026
- Published by Wolters Kluwer Health in Anesthesia & Analgesia
Common Laryngoscopy Errors Among Novice Pediatric Anesthesia Trainees Intubating Neonates and Infants
Was not provided for this article.
- 9 October 2026
- Published by Wolters Kluwer Health in Anesthesia & Analgesia
Open AccessCommon Laryngoscopy Errors Among Novice Pediatric Anesthesia Trainees Intubating Neonates and Infants
Was not provided for this article.
- Open Access
- 23 June 2026
- Published by BMJ in BMJ Paediatrics Open
- Vol. 10 (1) , e004775
Complementary views: addressing blind spots in the direct versus video laryngoscopy debate
- 23 June 2026
- Published by BMJ in BMJ Paediatrics Open
- Vol. 10 (1) , e004775
Open AccessComplementary views: addressing blind spots in the direct versus video laryngoscopy debate
- Open Access
Coaching inexperienced clinicians before a high stakes medical procedure: randomized clinical trial
K-Ras mutations represent a most prevalent oncogenic alteration in human cancers. Despite of tremendous efforts, it remains a big challenge to develop inhibitors that can target the oncogenic K-Ras mutants, especially mutants without specific active or charged side chains such as K-RasG12V. Here, taking advantage of our previous finding that Nedd4-1 is a bona fide E3 ubiquitin ligase for wild-type Ras proteins, we developed a compound XMU-MP-9 that can promote ubiquitination and degradation of various K-Ras mutants including K-RasG12V, and significantly inhibit proliferation and tumor development of K-Ras mutant harboring cells. Mechanistically, XMU-MP-9 acts as a bifunctional compound to bind the C2 domain of Nedd4-1 and an allosteric site of K-Ras to enhance Nedd4-1 and K-Ras interaction, and to induce a conformational change of Nedd4-1/K-Ras complex to allow Nedd4-1 targeting K128 of K-Ras for ubiquitination. Hence, our study presents a robust strategy to develop small-molecule degrader of K-Ras mutants, and also sheds light on the development of small-molecule degraders for H-Ras and N-Ras mutants.
Open AccessCoaching inexperienced clinicians before a high stakes medical procedure: randomized clinical trial
K-Ras mutations represent a most prevalent oncogenic alteration in human cancers. Despite of tremendous efforts, it remains a big challenge to develop inhibitors that can target the oncogenic K-Ras mutants, especially mutants without specific active or charged side chains such as K-RasG12V. Here, taking advantage of our previous finding that Nedd4-1 is a bona fide E3 ubiquitin ligase for wild-type Ras proteins, we developed a compound XMU-MP-9 that can promote ubiquitination and degradation of various K-Ras mutants including K-RasG12V, and significantly inhibit proliferation and tumor development of K-Ras mutant harboring cells. Mechanistically, XMU-MP-9 acts as a bifunctional compound to bind the C2 domain of Nedd4-1 and an allosteric site of K-Ras to enhance Nedd4-1 and K-Ras interaction, and to induce a conformational change of Nedd4-1/K-Ras complex to allow Nedd4-1 targeting K128 of K-Ras for ubiquitination. Hence, our study presents a robust strategy to develop small-molecule degrader of K-Ras mutants, and also sheds light on the development of small-molecule degraders for H-Ras and N-Ras mutants.