Publications

Selected Publications

Sui, L. and Guo, H.-C. (2021). ERAP1 binds peptide C-termini of different sequences and/or lengths by a common recognition mechanism. Immunobiology 226, 152112 (pp. 1-10).

Sui, L. and Guo, H.-C. (2021). Enhanced recombinant expression and purification of human IRAP for biochemical and crystallography studies. Biochem. Biophys. Rep. 27, 101042 (pp. 1-6).

Pande, S. and Guo, H.-C. (2019). The T99K variant of glycosylasparaginase shows a new structural mechanism of the genetic disease aspartylglucosaminuriaProtein Sci. 28, 1013-1023.

Pande, S., Bizilj, W., and Guo, H.-C. (2018). Biochemical and structural insights into an allelic variant causing the lysosomal storage disorder – aspartylglucosaminuria. FEBS Lett. 592, 2550-2561.

Pande, S., Lakshminarasimhan, D., and Guo, H.-C. (2017). Crystal structure of a mutant glycosylasparaginase shedding light on aspartylglycosaminurea-causing mechanism as well as on hydrolysis of non-chitobiose substrate. Mol. Genet. and Metab. 121, 150-156.

Sui, L., Gandhi, A., and Guo, H.-C. (2016). Crystal structure of a polypeptide’s C-terminus in complex with the regulatory domain of ER aminopeptidase 1. Mol. Immunol. 80, 41-49.

Sui, L., Gandhi, A., and Guo, H.-C. (2015). Single-chain expression and crystallization of an antigenic C-terminus in complex with the regulatory domain of ER aminopeptidase 1. Crystal Structure Theory and Applications 4, 47-52.

Sui, L., Lakshminarasimhan, D., Pande, S., and Guo, H.-C. (2014). Structural basis of a point mutation that causes the genetic disease Aspartylglucosaminuriainto. Structure 22, 1855-1861.

Gandhi, A., Lakshminarasimhan, D., Sun, Y., and Guo, H.-C. (2011). Structural insights into the molecular ruler mechanism of the endoplasmic reticulum aminopeptidase ERAP1. Sci. Rep. (Nature Publishing Group) 1, 186.

Wang, Y. and Guo, H.-C. (2010). Crystallographic snapshot of glycosylasparaginase precursor poised for autoprocessing. J. Mol. Biol. 403, 120-130.

Sun, Y. and Guo, H.-C. (2008). Structural constraints on autoprocessing of the human nucleoporin Nup98. Protein Sci. 17, 494-505.

Wang, Y. and Guo, H.-C. (2007). Crystallographic snapshot of a productive glycosylasparaginase-substrate complex. J. Mol. Biol. 366, 82-92.

Meyer, R.D., Qian, X., Guo, H.-C., and Rahimi, N. (2006). Leucine motif-dependent tyrosine autophosphorylation of type III receptor tyrosine kinases. J. Biol. Chem. 281, 8620-8627.

Xu, Q.S., Kucera, R.B., Roberts, R.J., and Guo, H.-C. (2004). An asymmetric complex of restriction endonuclease MspI on its palindromic DNA recognition site. Structure 12, 1741-1747.

Wang, Y. and Guo, H.-C. (2003). Two-step dimerization for autoproteolysis to activate glycosylasparaginase. J. Biol. Chem. 278, 3210-3219.

Xu, Q., Buckley, D., Guan, C., and Guo, H.-C. (1999). Structural insights into the mechanism of intramolecular proteolysis. Cell 98, 651-661.

Guo, H.-C., Xu, Q., Buckley, D., and Guan, C. (1998). Crystal structures of Flavobacterium glycosylasparaginase: an N-terminal nucleophile hydrolase activated by intramolecular proteolysis. J. Biol. Chem. 273, 20205-20212.

Guo, H.-C., Madden, D.R., Silver, M.L., Jardetzky, T.S., Gorga, J.C., Strominger, J.L., and Wiley, D.C. (1993). Comparison of the P2 specificity pocket in three human histocompatibility antigens: HLA-A*6801, HLA-A*0201 and HLA-B*2705. Proc. Natl. Acad. Sci. USA 90, 8053-8057.

Guo, H.-C., Jardetzky, T.S., Garrett, T.P.J., Lane, W.S., Strominger, J.L., and Wiley, D.C. (1992). Different length peptides bind to HLA-Aw68 similarly at their ends but bulge out in the middle. Nature 360, 364-366.

Silver, M.L., Guo, H.-C., Strominger, J.L., and Wiley, D.C. (1992). Atomic structure of a human MHC molecule presenting an influenza virus peptide. Nature 360, 367-369.

Guo, H.-C. and Roberts, J.W. (1990). Heterogeneous initiation due to slippage at the bacteriophage 82 late gene promoter in vitro. Biochemistry 29, 10702-10709.

 

Complete list of citations on PubMed