These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


BIOMARKERS

Molecular Biopsy of Human Tumors

- a resource for Precision Medicine *

208 related articles for article (PubMed ID: 1731946)

  • 1. 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
    Biochemistry; 1992 Jan; 31(3):898-904. PubMed ID: 1731946
    [TBL] [Abstract][Full Text] [Related]  

  • 2. Structural consequences of the natural substitution, E9K, on reactive-site-hydrolyzed squash (Cucurbita maxima) trypsin inhibitor (CMTI), as studied by two-dimensional NMR.
    Krishnamoorthi R; Lin CL; VanderVelde D
    Biochemistry; 1992 Jun; 31(21):4965-9. PubMed ID: 1599921
    [TBL] [Abstract][Full Text] [Related]  

  • 3. 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
    Biochemistry; 1992 Jan; 31(3):905-10. PubMed ID: 1731947
    [TBL] [Abstract][Full Text] [Related]  

  • 4. An 1H NMR determination of the three-dimensional structures of mirror-image forms of a Leu-5 variant of the trypsin inhibitor from Ecballium elaterium (EETI-II).
    Nielsen KJ; Alewood D; Andrews J; Kent SB; Craik DJ
    Protein Sci; 1994 Feb; 3(2):291-302. PubMed ID: 8003965
    [TBL] [Abstract][Full Text] [Related]  

  • 5. 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
    Protein Sci; 1998 Jan; 7(1):132-41. PubMed ID: 9514268
    [TBL] [Abstract][Full Text] [Related]  

  • 6. Natural abundance 15N NMR assignments delineate structural differences between intact and reactive-site hydrolyzed Cucurbita maxima trypsin inhibitor III.
    Krishnamoorthi R; Nemmers S; Tobias B
    FEBS Lett; 1992 Jun; 304(2-3):149-52. PubMed ID: 1618315
    [TBL] [Abstract][Full Text] [Related]  

  • 7. Reactive-site hydrolyzed Cucurbita maxima trypsin inhibitor-V: function, thermodynamic stability, and NMR solution structure.
    Cai M; Gong Y; Prakash O; Krishnamoorthi R
    Biochemistry; 1995 Sep; 34(38):12087-94. PubMed ID: 7547948
    [TBL] [Abstract][Full Text] [Related]  

  • 8. Differential modulation of binding loop flexibility and stability by Arg50 and Arg52 in Cucurbita maxima trypsin inhibitor-V deduced by trypsin-catalyzed hydrolysis and NMR spectroscopy.
    Cai M; Huang Y; Prakash O; Wen L; Dunkelbarger SP; Huang JK; Liu J; Krishnamoorthi R
    Biochemistry; 1996 Apr; 35(15):4784-94. PubMed ID: 8664268
    [TBL] [Abstract][Full Text] [Related]  

  • 9. Internal mobility of reactive-site-hydrolyzed recombinant Cucurbita maxima trypsin inhibitor-V characterized by NMR spectroscopy: evidence for differential stabilization of newly formed C- and N-termini.
    Liu J; Prakash O; Huang Y; Wen L; Wen JJ; Huang JK; Krishnamoorthi R
    Biochemistry; 1996 Sep; 35(38):12503-10. PubMed ID: 8823186
    [TBL] [Abstract][Full Text] [Related]  

  • 10. 1H-n.m.r. studies of squash seed trypsin inhibitor.
    Likos JJ
    Int J Pept Protein Res; 1989 Nov; 34(5):381-6. PubMed ID: 2613440
    [TBL] [Abstract][Full Text] [Related]  

  • 11. Single peptide bond hydrolysis/resynthesis in squash inhibitors of serine proteinases. 1. Kinetics and thermodynamics of the interaction between squash inhibitors and bovine beta-trypsin.
    Otlewski J; Zbyryt T
    Biochemistry; 1994 Jan; 33(1):200-7. PubMed ID: 8286341
    [TBL] [Abstract][Full Text] [Related]  

  • 12. Three-dimensional solution structure of Cucurbita maxima trypsin inhibitor-V determined by NMR spectroscopy.
    Cai M; Gong Y; Kao JL; Krishnamoorthi R
    Biochemistry; 1995 Apr; 34(15):5201-11. PubMed ID: 7711040
    [TBL] [Abstract][Full Text] [Related]  

  • 13. 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
    Biochemistry; 2002 Jul; 41(30):9572-9. PubMed ID: 12135379
    [TBL] [Abstract][Full Text] [Related]  

  • 14. New active analogues of Cucurbita maxima trypsin inhibitor III (CMTI-III) modified in the non-contact region.
    Rózycki J; Kupryszewski G; Rolka K; Ragnarsson U; Zbyryt T; Krokoszyńska I; Wilusz T
    Biol Chem Hoppe Seyler; 1994 Jan; 375(1):21-3. PubMed ID: 8003251
    [TBL] [Abstract][Full Text] [Related]  

  • 15. Design, chemical synthesis and kinetic studies of trypsin chromogenic substrates based on the proteinase binding loop of Cucurbita maxima trypsin inhibitor (CMTI-III).
    Lesner A; Brzozowski K; Kupryszewski G; Rolka K
    Biochem Biophys Res Commun; 2000 Mar; 269(1):81-4. PubMed ID: 10694481
    [TBL] [Abstract][Full Text] [Related]  

  • 16. The refined 2.0 A X-ray crystal structure of the complex formed between bovine beta-trypsin and CMTI-I, a trypsin inhibitor from squash seeds (Cucurbita maxima). Topological similarity of the squash seed inhibitors with the carboxypeptidase A inhibitor from potatoes.
    Bode W; Greyling HJ; Huber R; Otlewski J; Wilusz T
    FEBS Lett; 1989 Jan; 242(2):285-92. PubMed ID: 2914611
    [TBL] [Abstract][Full Text] [Related]  

  • 17. Synthesis of a squash-type protease inhibitor by gene engineering and effects of replacements of conserved hydrophobic amino acid residues on its inhibitory activity.
    Kojima S; Miyoshi K; Miura K
    Protein Eng; 1996 Dec; 9(12):1241-6. PubMed ID: 9010939
    [TBL] [Abstract][Full Text] [Related]  

  • 18. Distance between the basic group of the amino acid residue's side chain in position P1 of trypsin inhibitor CMTI-III and Asp189 in the substrate pocket of trypsin has an essential influence on the inhibitory activity.
    Jaśkiewicz A; Lesner A; Rózycki J; Rodziewicz S; Rolka K; Ragnarsson U; Kupryszewski G
    Biochem Biophys Res Commun; 1997 Nov; 240(3):869-71. PubMed ID: 9398660
    [TBL] [Abstract][Full Text] [Related]  

  • 19. Modifications outside the proteinase binding loop in Cucurbita maxima trypsin inhibitor III (CMTI-III) analogues change the binding energy with bovine beta-trypsin.
    Jaśkiewicz A; Lis K; Rózycki J; Kupryszewski G; Rolka K; Ragnarsson U; Zbyryt T; Wilusz T
    FEBS Lett; 1998 Oct; 436(2):174-8. PubMed ID: 9781673
    [TBL] [Abstract][Full Text] [Related]  

  • 20. High-resolution structures of three new trypsin-squash-inhibitor complexes: a detailed comparison with other trypsins and their complexes.
    Helland R; Berglund GI; Otlewski J; Apostoluk W; Andersen OA; Willassen NP; Smalås AO
    Acta Crystallogr D Biol Crystallogr; 1999 Jan; 55(Pt 1):139-48. PubMed ID: 10089404
    [TBL] [Abstract][Full Text] [Related]  

    [Next]    [New Search]
    of 11.