Yan, Nieng

Crystal structure of the human glucose transporter GLUT1

Deng, D., Xu, C., Sun, P., Wu, J., Yan, C., Hu, M., & Yan, N. (2014) · Nature

Enzyme Structure and FunctionMetabolism, Diabetes, and Cancer

Cited by 777

Structural basis for the recognition of Sonic Hedgehog by human Patched1

Gong, X., Qian, H., Cao, P., Zhao, X., Zhou, Q., Lei, J., & Yan, N. (2018) · Science

Hedgehog Signaling Pathway StudiesReceptor Mechanisms and Signaling

Cited by 216

Structure of the BRCT Repeats of BRCA1 Bound to a BACH1 Phosphopeptide

Shiozaki, E. N., Gu, L., Yan, N., & Shi, Y. (2004) · Molecular Cell

DNA Repair MechanismsBRCA gene mutations in cancer

Cited by 174

Structure and mechanism of human diacylglycerol O-acyltransferase 1

Wang, L., Qian, H., Nian, Y., Han, Y., Ren, Z., Zhang, H., Hu, L., Prasad, B. V. V., Laganowsky, A., Yan, N., et al. (2020) · Nature

Lipid metabolism and biosynthesisLipid metabolism and disorders

Cited by 123

Structural basis for catalysis and substrate specificity of human ACAT1

Qian, H., Zhao, X., Yan, R., Yao, X., Gao, S., Sun, X., Du, X., Yang, H., Wong, C. C. L., & Yan, N. (2020) · Nature

Cholesterol and Lipid MetabolismLipid Membrane Structure and Behavior

Cited by 108

A structure of human Scap bound to Insig-2 suggests how their interaction is regulated by sterols

Yan, R., Cao, P., Song, W., Qian, H., Du, X., Coates, H. W., Zhao, X., Li, Y., Gao, S., Gong, X., et al. (2021) · Science

Cholesterol and Lipid MetabolismLipid Membrane Structure and Behavior

Cited by 100

Structural basis of ion transport and inhibition in ferroportin

Pan, Y., Ren, Z., Gao, S., Shen, J., Wang, L., Xu, Z., Yu, Y., Bachina, P., Zhang, H., Fan, X., et al. (2020) · Nature Communications

Iron Metabolism and DisordersProtein Structure and Dynamics

Cited by 81

CryoPROS: Correcting misalignment caused by preferred orientation using AI-generated auxiliary particles

Zhang, H., Zheng, D., Wu, Q., Yan, N., Peng, H., Hu, Q., Peng, Y., Yan, Z., Shi, Z., Bao, C., et al. (2025) · Nature Communications

Advanced Electron Microscopy Techniques and ApplicationsEnzyme Structure and Function

Cited by 12

Cryo-EM structure of histidyl-tRNA synthetase-like domain reveals activating crossed helices at the core of GCN2

Solorio-Kirpichyan, K., Fan, X., Golovenko, D., Korostelev, A. A., Yan, N., & Korennykh, A. (2024) · PNAS Nexus

Endoplasmic Reticulum Stress and DiseaseRNA and protein synthesis mechanisms

Cited by 5

Cryo-EM Structure of HRSL Domain Reveals Activating Crossed Helices at the Core of GCN2

Solorio-Kirpichyan, K., Fan, X., Golovenko, D., Korostelev, A. A., Yan, N., & Korennykh, A. (2024) · PNAS Nexus

Endoplasmic Reticulum Stress and DiseaseRNA and protein synthesis mechanisms

Cited by 5

Absolute hand determination of glycofibrils from natural sources in cryo-EM

Zhang, Q., Qin, L., Wang, T., Li, Z., Zhang, Y., Chen, S., Yan, N., Wang, J., & Hu, M. (2025) · Proceedings of the National Academy of Sciences

Advanced Electron Microscopy Techniques and ApplicationsEnzyme Structure and Function

Cited by 3

Absolute hand determination of glycofibrils from natural sources in cryo-EM

Zhang, Q., Qin, L., Wang, T., Li, Z., Zhang, Y., Chen, S., Ge, Q., Wen, J., Yan, N., Wang, J., et al. (2026) · Proceedings of the National Academy of Sciences

Advanced Electron Microscopy Techniques and ApplicationsEnzyme Structure and Function

Cited by 3