Gong Y - Search Results

1

Changing the inhibitory specificity and function of Cucurbita maxima trypsin inhibitor-V by site-directed mutagenesis.

Wen L, Lee I, Chen G, Huang JK, Gong Y, Krishnamoorthi R. Wen L, et al. Among authors: gong y. Biochem Biophys Res Commun. 1995 Feb 27;207(3):897-902. doi: 10.1006/bbrc.1995.1270. Biochem Biophys Res Commun. 1995. PMID: 7864895

2

Chemical synthesis, molecular cloning, overexpression, and site-directed mutagenesis of the gene coding for pumpkin (Curcubita maxima) trypsin inhibitor CMTI-V.

Wen L, Kim SS, Tinn TT, Huang JK, Krishnamoorthi R, Gong YX, Lwin YN, Kyin S. Wen L, et al. Among authors: gong yx. Protein Expr Purif. 1993 Jun;4(3):215-22. doi: 10.1006/prep.1993.1028. Protein Expr Purif. 1993. PMID: 8518561

3

Correlation of binding-loop internal dynamics with stability and function in potato I inhibitor family: relative contributions of Arg(50) and Arg(52) in Cucurbita maxima trypsin inhibitor-V as studied by site-directed mutagenesis and NMR spectroscopy.

Cai M, Gong YX, Wen L, Krishnamoorthi R. Cai M, et al. Biochemistry. 2002 Jul 30;41(30):9572-9. doi: 10.1021/bi0258952. Biochemistry. 2002. PMID: 12135379

4

Reactive-site hydrolyzed Cucurbita maxima trypsin inhibitor-V: function, thermodynamic stability, and NMR solution structure.

Cai M, Gong Y, Prakash O, Krishnamoorthi R. Cai M, et al. Among authors: gong y. Biochemistry. 1995 Sep 26;34(38):12087-94. doi: 10.1021/bi00038a001. Biochemistry. 1995. PMID: 7547948

5

Three-dimensional solution structure of Cucurbita maxima trypsin inhibitor-V determined by NMR spectroscopy.

Cai M, Gong Y, Kao JL, Krishnamoorthi R. Cai M, et al. Among authors: gong y. Biochemistry. 1995 Apr 18;34(15):5201-11. doi: 10.1021/bi00015a034. Biochemistry. 1995. PMID: 7711040

6

Solution structure and backbone dynamics of recombinant Cucurbita maxima trypsin inhibitor-V determined by NMR spectroscopy.

Liu J, Prakash O, Cai M, Gong Y, Huang Y, Wen L, Wen JJ, Huang JK, Krishnamoorthi R. Liu J, et al. Among authors: gong y. Biochemistry. 1996 Feb 6;35(5):1516-24. doi: 10.1021/bi952466d. Biochemistry. 1996. PMID: 8634282

The average structure of rCMTI-V is found to be almost the same as that of the native protein [Cai, M., Gong, Y., Kao, J.-L., & Krishnamoorthi, R. (1995) Biochemistry 34, 5201-5211]. The backbone dynamics of uniformly 15N-labeled rCMTI-V were characterized by 2D …

The average structure of rCMTI-V is found to be almost the same as that of the native protein [Cai, M., Gong, Y., Kao, J.-L., …

7

NMR studies of internal dynamics of serine proteinase protein inhibitors: Binding region mobilities of intact and reactive-site hydrolyzed Cucurbita maxima trypsin inhibitor (CMTI)-III of the squash family and comparison with those of counterparts of CMTI-V of the potato I family.

Liu J, Gong Y, Prakash O, Wen L, Lee I, Huang JK, Krishnamoorthi R. Liu J, et al. Among authors: gong y. Protein Sci. 1998 Jan;7(1):132-41. doi: 10.1002/pro.5560070114. Protein Sci. 1998. PMID: 9514268 Free PMC article.

8

Two-dimensional NMR studies of squash family inhibitors. Sequence-specific proton assignments and secondary structure of reactive-site hydrolyzed Cucurbita maxima trypsin inhibitor III.

Krishnamoorthi R, Gong YX, Lin CL, VanderVelde D. Krishnamoorthi R, et al. Among authors: gong yx. Biochemistry. 1992 Jan 28;31(3):898-904. doi: 10.1021/bi00118a036. Biochemistry. 1992. PMID: 1731946

9

A new protein inhibitor of trypsin and activated Hageman factor from pumpkin (Cucurbita maxima) seeds.

Krishnamoorthi R, Gong YX, Richardson M. Krishnamoorthi R, et al. Among authors: gong yx. FEBS Lett. 1990 Oct 29;273(1-2):163-7. doi: 10.1016/0014-5793(90)81075-y. FEBS Lett. 1990. PMID: 2226848 Free article.

10

Proton NMR studies of Cucurbita maxima trypsin inhibitors: evidence for pH-dependent conformational change and His25-Tyr27 interaction.

Krishnamoorthi R, Lin CL, Gong YX, VanderVelde D, Hahn K. Krishnamoorthi R, et al. Among authors: gong yx. Biochemistry. 1992 Jan 28;31(3):905-10. doi: 10.1021/bi00118a037. Biochemistry. 1992. PMID: 1731947

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