Sangwon Lee

Scopus Author ID Scopus Author ID ORCID

Publication Activity (10 Years)

Years Active: 2020-2023
Publications (10 Years): 4

Top Topics

Electron Microscopy

Allogeneic Hematopoietic Stem Cell Transplantation

Tyrosine Kinase

Binding Protein

Top Venues

Proceedings of the National Academy of Sciences of the United States of America

Yale School of Medicine

University of California, San Diego (PHD)

This page only lists publications with an associated author ORCID identifier.

Affiliation History

Yale School of Medicine Jul 01 2018

United States

Assistant Professor :: Pharmacology

Education History

University of California, San Diego

United States

PHD :: Chemistry and Biochemistry

Konkuk University

South Korea

MSC :: Chemistry

Publications

Stefan G Krimmer, Nicole Bertoletti, Yoshihisa Suzuki, Luka Katic, Jyotidarsini Mohanty, Sheng Shu, Sangwon Lee, Irit Lax, Wei Mi, Joseph Schlessinger
Cryo-EM analyses of KIT and oncogenic mutants reveal structural oncogenic plasticity and a target for therapeutic intervention. Proceedings of the National Academy of Sciences of the United States of America 120 (13) (2023)
Stefan G Krimmer, Nicole Bertoletti, Yoshihisa Suzuki, Luka Katic, Jyotidarsini Mohanty, Sheng Shu, Sangwon Lee, Irit Lax, Wei Mi, Joseph Schlessinger
Cryo-EM analyses of KIT and oncogenic mutants reveal structural oncogenic plasticity and a target for therapeutic intervention. Proceedings of the National Academy of Sciences of the United States of America 120 (13) (2023)
Stefan G Krimmer, Nicole Bertoletti, Yoshihisa Suzuki, Luka Katic, Jyotidarsini Mohanty, Sheng Shu, Sangwon Lee, Irit Lax, Wei Mi, Joseph Schlessinger
Cryo-EM analyses of KIT and oncogenic mutants reveal structural oncogenic plasticity and a target for therapeutic intervention. Proceedings of the National Academy of Sciences of the United States of America 120 (13) (2023)
Yoshihisa Suzuki, Ekaterina Kuzina, Seong J An, Francisco Tome, Jyotidarsini Mohanty, Wenxue Li, Sangwon Lee, Yansheng Liu, Irit Lax, Joseph Schlessinger
FGF23 contains two distinct high-affinity binding sites enabling bivalent interactions with α-Klotho. Proceedings of the National Academy of Sciences of the United States of America 117 (50) (2020)