BIOMARKERS

Molecular Biopsy of Human Tumors

- a resource for Precision Medicine *

228 related articles for article (PubMed ID: 15792862)

  • 1. Solvent accessibility in native and isolated domain environments: general features and implications to interface predictability.
    Raih MF; Ahmad S; Zheng R; Mohamed R
    Biophys Chem; 2005 Apr; 114(1):63-9. PubMed ID: 15792862
    [TBL] [Abstract][Full Text] [Related]  

  • 2. Analysis of accessible surface of residues in proteins.
    Lins L; Thomas A; Brasseur R
    Protein Sci; 2003 Jul; 12(7):1406-17. PubMed ID: 12824487
    [TBL] [Abstract][Full Text] [Related]  

  • 3. Characteristic features of amino acid residues in coiled-coil protein structures.
    Gromiha MM; Parry DA
    Biophys Chem; 2004 Oct; 111(2):95-103. PubMed ID: 15381307
    [TBL] [Abstract][Full Text] [Related]  

  • 4. Solvent accessible surface area of amino acid residues in globular proteins: correlation of apparent transfer free energies with experimental hydrophobicity scales.
    Shaytan AK; Shaitan KV; Khokhlov AR
    Biomacromolecules; 2009 May; 10(5):1224-37. PubMed ID: 19334678
    [TBL] [Abstract][Full Text] [Related]  

  • 5. On residues in the disallowed region of the Ramachandran map.
    Pal D; Chakrabarti P
    Biopolymers; 2002 Mar; 63(3):195-206. PubMed ID: 11787007
    [TBL] [Abstract][Full Text] [Related]  

  • 6. Sequence-dependence and prediction of nucleotide solvent accessibility in double stranded DNA.
    Ahmad S
    Gene; 2009 Jan; 428(1-2):25-30. PubMed ID: 18955120
    [TBL] [Abstract][Full Text] [Related]  

  • 7. Prediction of the interaction site on the surface of an isolated protein structure by analysis of side chain energy scores.
    Liang S; Zhang J; Zhang S; Guo H
    Proteins; 2004 Nov; 57(3):548-57. PubMed ID: 15382230
    [TBL] [Abstract][Full Text] [Related]  

  • 8. Use of amino acid environment-dependent substitution tables and conformational propensities in structure prediction from aligned sequences of homologous proteins. I. Solvent accessibility classes.
    Wako H; Blundell TL
    J Mol Biol; 1994 May; 238(5):682-92. PubMed ID: 8182743
    [TBL] [Abstract][Full Text] [Related]  

  • 9. Statistical characterization of salt bridges in proteins.
    Sarakatsannis JN; Duan Y
    Proteins; 2005 Sep; 60(4):732-9. PubMed ID: 16021620
    [TBL] [Abstract][Full Text] [Related]  

  • 10. Sequence and structural analysis of binding site residues in protein-protein complexes.
    Gromiha MM; Yokota K; Fukui K
    Int J Biol Macromol; 2010 Mar; 46(2):187-92. PubMed ID: 20026105
    [TBL] [Abstract][Full Text] [Related]  

  • 11. Inter-residue and solvent-residue interactions in proteins: a statistical study on experimental structures.
    Chelli R; Gervasio FL; Procacci P; Schettino V
    Proteins; 2004 Apr; 55(1):139-51. PubMed ID: 14997548
    [TBL] [Abstract][Full Text] [Related]  

  • 12. Quantitative expression of protein heterogeneity: Response of amino acid side chains to their local environment.
    Bandyopadhyay D; Mehler EL
    Proteins; 2008 Aug; 72(2):646-59. PubMed ID: 18247345
    [TBL] [Abstract][Full Text] [Related]  

  • 13. Look-up tables for protein solvent accessibility prediction and nearest neighbor effect analysis.
    Wang JY; Ahmad S; Gromiha MM; Sarai A
    Biopolymers; 2004 Oct; 75(3):209-16. PubMed ID: 15378480
    [TBL] [Abstract][Full Text] [Related]  

  • 14. Amino acid propensities for secondary structures are influenced by the protein structural class.
    Costantini S; Colonna G; Facchiano AM
    Biochem Biophys Res Commun; 2006 Apr; 342(2):441-51. PubMed ID: 16487481
    [TBL] [Abstract][Full Text] [Related]  

  • 15. Atom-wise statistics and prediction of solvent accessibility in proteins.
    Singh YH; Gromiha MM; Sarai A; Ahmad S
    Biophys Chem; 2006 Nov; 124(2):145-54. PubMed ID: 16860924
    [TBL] [Abstract][Full Text] [Related]  

  • 16. Discarding functional residues from the substitution table improves predictions of active sites within three-dimensional structures.
    Gong S; Blundell TL
    PLoS Comput Biol; 2008 Oct; 4(10):e1000179. PubMed ID: 18833291
    [TBL] [Abstract][Full Text] [Related]  

  • 17. Inference of the solvation energy parameters of amino acids using maximum entropy approach.
    Hoang TX; Seno F; Trovato A; Banavar JR; Maritan A
    J Chem Phys; 2008 Jul; 129(3):035102. PubMed ID: 18647046
    [TBL] [Abstract][Full Text] [Related]  

  • 18. Average assignment method for predicting the stability of protein mutants.
    Saraboji K; Gromiha MM; Ponnuswamy MN
    Biopolymers; 2006 May; 82(1):80-92. PubMed ID: 16453276
    [TBL] [Abstract][Full Text] [Related]  

  • 19. A molecular dynamics approach to study the importance of solvent in protein interactions.
    Samsonov S; Teyra J; Pisabarro MT
    Proteins; 2008 Nov; 73(2):515-25. PubMed ID: 18452208
    [TBL] [Abstract][Full Text] [Related]  

  • 20. Protein structural change upon ligand binding correlates with enzymatic reaction mechanism.
    Koike R; Amemiya T; Ota M; Kidera A
    J Mol Biol; 2008 Jun; 379(3):397-401. PubMed ID: 18455184
    [TBL] [Abstract][Full Text] [Related]  

    [Next]    [New Search]
    of 12.