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 *

176 related articles for article (PubMed ID: 12215410)

  • 1. A cis-prolyl peptide bond isomerization dominates the folding of the alpha subunit of Trp synthase, a TIM barrel protein.
    Wu Y; Matthews CR
    J Mol Biol; 2002 Sep; 322(1):7-13. PubMed ID: 12215410
    [TBL] [Abstract][Full Text] [Related]  

  • 2. Parallel channels and rate-limiting steps in complex protein folding reactions: prolyl isomerization and the alpha subunit of Trp synthase, a TIM barrel protein.
    Wu Y; Matthews CR
    J Mol Biol; 2002 Oct; 323(2):309-25. PubMed ID: 12381323
    [TBL] [Abstract][Full Text] [Related]  

  • 3. Proline replacements and the simplification of the complex, parallel channel folding mechanism for the alpha subunit of Trp synthase, a TIM barrel protein.
    Wu Y; Matthews CR
    J Mol Biol; 2003 Jul; 330(5):1131-44. PubMed ID: 12860133
    [TBL] [Abstract][Full Text] [Related]  

  • 4. Molecular dissection of the folding mechanism of the alpha subunit of tryptophan synthase: an amino-terminal autonomous folding unit controls several rate-limiting steps in the folding of a single domain protein.
    Zitzewitz JA; Matthews CR
    Biochemistry; 1999 Aug; 38(31):10205-14. PubMed ID: 10433729
    [TBL] [Abstract][Full Text] [Related]  

  • 5. An obligatory intermediate controls the folding of the alpha-subunit of tryptophan synthase, a TIM barrel protein.
    Wintrode PL; Rojsajjakul T; Vadrevu R; Matthews CR; Smith DL
    J Mol Biol; 2005 Apr; 347(5):911-9. PubMed ID: 15784252
    [TBL] [Abstract][Full Text] [Related]  

  • 6. The coordination of the isomerization of a conserved non-prolyl cis peptide bond with the rate-limiting steps in the folding of dihydrofolate reductase.
    Svensson AK; O'Neill JC; Matthews CR
    J Mol Biol; 2003 Feb; 326(2):569-83. PubMed ID: 12559923
    [TBL] [Abstract][Full Text] [Related]  

  • 7. A tightly packed hydrophobic cluster directs the formation of an off-pathway sub-millisecond folding intermediate in the alpha subunit of tryptophan synthase, a TIM barrel protein.
    Wu Y; Vadrevu R; Kathuria S; Yang X; Matthews CR
    J Mol Biol; 2007 Mar; 366(5):1624-38. PubMed ID: 17222865
    [TBL] [Abstract][Full Text] [Related]  

  • 8. Equilibrium and kinetic analyses of unfolding and refolding for the conserved proline mutants of tryptophan synthase alpha subunit.
    Ogasahara K; Yutani K
    Biochemistry; 1997 Jan; 36(4):932-40. PubMed ID: 9020793
    [TBL] [Abstract][Full Text] [Related]  

  • 9. Equilibrium and kinetic folding pathways of a TIM barrel with a funneled energy landscape.
    Finke JM; Onuchic JN
    Biophys J; 2005 Jul; 89(1):488-505. PubMed ID: 15833999
    [TBL] [Abstract][Full Text] [Related]  

  • 10. Folding mechanism of the alpha-subunit of tryptophan synthase, an alpha/beta barrel protein: global analysis highlights the interconversion of multiple native, intermediate, and unfolded forms through parallel channels.
    Bilsel O; Zitzewitz JA; Bowers KE; Matthews CR
    Biochemistry; 1999 Jan; 38(3):1018-29. PubMed ID: 9893998
    [TBL] [Abstract][Full Text] [Related]  

  • 11. Mutagenic analysis of the interior packing of an alpha/beta barrel protein. Effects on the stabilities and rates of interconversion of the native and partially folded forms of the alpha subunit of tryptophan synthase.
    Tsuji T; Chrunyk BA; Chen X; Matthews CR
    Biochemistry; 1993 Jun; 32(21):5566-75. PubMed ID: 8504078
    [TBL] [Abstract][Full Text] [Related]  

  • 12. Multi-state unfolding of the alpha subunit of tryptophan synthase, a TIM barrel protein: insights into the secondary structure of the stable equilibrium intermediates by hydrogen exchange mass spectrometry.
    Rojsajjakul T; Wintrode P; Vadrevu R; Robert Matthews C; Smith DL
    J Mol Biol; 2004 Jul; 341(1):241-53. PubMed ID: 15312776
    [TBL] [Abstract][Full Text] [Related]  

  • 13. Long-range side-chain-main-chain interactions play crucial roles in stabilizing the (betaalpha)8 barrel motif of the alpha subunit of tryptophan synthase.
    Yang X; Vadrevu R; Wu Y; Matthews CR
    Protein Sci; 2007 Jul; 16(7):1398-409. PubMed ID: 17586773
    [TBL] [Abstract][Full Text] [Related]  

  • 14. Kinetic folding and cis/trans prolyl isomerization of staphylococcal nuclease. A study by stopped-flow absorption, stopped-flow circular dichroism, and molecular dynamics simulations.
    Ikura T; Tsurupa GP; Kuwajima K
    Biochemistry; 1997 May; 36(21):6529-38. PubMed ID: 9174370
    [TBL] [Abstract][Full Text] [Related]  

  • 15. Kinetic models for unfolding and refolding of ribonuclease T1 with substitution of cis-proline 39 by alanine.
    Mayr LM; Schmid FX
    J Mol Biol; 1993 Jun; 231(3):913-26. PubMed ID: 8515460
    [TBL] [Abstract][Full Text] [Related]  

  • 16. The slow folding reaction of barstar: the core tryptophan region attains tight packing before substantial secondary and tertiary structure formation and final compaction of the polypeptide chain.
    Sridevi K; Juneja J; Bhuyan AK; Krishnamoorthy G; Udgaonkar JB
    J Mol Biol; 2000 Sep; 302(2):479-95. PubMed ID: 10970747
    [TBL] [Abstract][Full Text] [Related]  

  • 17. Folding pathway of Escherichia coli ribonuclease HI: a circular dichroism, fluorescence, and NMR study.
    Yamasaki K; Ogasahara K; Yutani K; Oobatake M; Kanaya S
    Biochemistry; 1995 Dec; 34(51):16552-62. PubMed ID: 8527428
    [TBL] [Abstract][Full Text] [Related]  

  • 18. Non-prolyl cis-trans peptide bond isomerization as a rate-determining step in protein unfolding and refolding.
    Odefey C; Mayr LM; Schmid FX
    J Mol Biol; 1995 Jan; 245(1):69-78. PubMed ID: 7823321
    [TBL] [Abstract][Full Text] [Related]  

  • 19. Fast folding of Escherichia coli cyclophilin A: a hypothesis of a unique hydrophobic core with a phenylalanine cluster.
    Ikura T; Hayano T; Takahashi N; Kuwajima K
    J Mol Biol; 2000 Mar; 297(3):791-802. PubMed ID: 10731429
    [TBL] [Abstract][Full Text] [Related]  

  • 20. Role of conserved proline residues in stabilizing tryptophan synthase alpha subunit: analysis by mutants with alanine or glycine.
    Yutani K; Hayashi S; Sugisaki Y; Ogasahara K
    Proteins; 1991; 9(2):90-8. PubMed ID: 2008436
    [TBL] [Abstract][Full Text] [Related]  

    [Next]    [New Search]
    of 9.