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Volumn 91, Issue 5, 2006, Pages 2009-2010

Fingerprinting DHFR in single-molecule AFM studies

Author keywords

[No Author keywords available]

Indexed keywords

8 DIHYDROFOLIC ACID; DIHYDROFOLATE REDUCTASE; FOLIC ACID DERIVATIVE; METHOTREXATE; UNCLASSIFIED DRUG;

EID: 33748447337     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.106.085126     Document Type: Letter
Times cited : (5)

References (12)
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    • Ligand binding modulates the mechanical stability of dihydrofolate reductase
    • Ainavarapu, S. R., L. Li, C. L. Badilla, and J. M. Fernandez. 2005. Ligand binding modulates the mechanical stability of dihydrofolate reductase. Biophys. J. 89:3337-3344.
    • (2005) Biophys. J. , vol.89 , pp. 3337-3344
    • Ainavarapu, S.R.1    Li, L.2    Badilla, C.L.3    Fernandez, J.M.4
  • 2
    • 27744453306 scopus 로고    scopus 로고
    • Influence of substrate binding on the mechanical stability of mouse dihydrofolate reductase
    • Junker, J. P., K. Hell, M. Schlierf, W. Neupert, and M. Rief. 2005. Influence of substrate binding on the mechanical stability of mouse dihydrofolate reductase. Biophys. J. 89:L46-L48.
    • (2005) Biophys. J. , vol.89
    • Junker, J.P.1    Hell, K.2    Schlierf, M.3    Neupert, W.4    Rief, M.5
  • 6
    • 0034804341 scopus 로고    scopus 로고
    • Can non-mechanical proteins withstand force? Stretching barnase by atomic force microscopy and molecular dynamics simulation
    • Best, R. B., B. Li, A. Steward, V. Daggett, and J. Clarke. 2001. Can non-mechanical proteins withstand force? Stretching barnase by atomic force microscopy and molecular dynamics simulation. Biophys. J. 81:2344-2356.
    • (2001) Biophys. J. , vol.81 , pp. 2344-2356
    • Best, R.B.1    Li, B.2    Steward, A.3    Daggett, V.4    Clarke, J.5
  • 7
    • 10044247452 scopus 로고    scopus 로고
    • Mechanical unfolding intermediates observed by single-molecule force spectroscopy in a fibronectin type III module
    • Li, L., H. H. Huang, C. L. Badilla, and J. M. Fernandez. 2005. Mechanical unfolding intermediates observed by single-molecule force spectroscopy in a fibronectin type III module. J. Mol. Biol. 345:817-826.
    • (2005) J. Mol. Biol. , vol.345 , pp. 817-826
    • Li, L.1    Huang, H.H.2    Badilla, C.L.3    Fernandez, J.M.4
  • 8
    • 0022515029 scopus 로고
    • Binding of a specific ligand inhibits import of a purified precursor protein into mitochondria
    • Eilers, M., and G. Schatz. 1986. Binding of a specific ligand inhibits import of a purified precursor protein into mitochondria. Nature. 322:228-232.
    • (1986) Nature , vol.322 , pp. 228-232
    • Eilers, M.1    Schatz, G.2
  • 9
    • 0034328890 scopus 로고    scopus 로고
    • Protein unfolding by mitochondria. The Hsp70 import motor
    • Matouschek, A., N. Pfanner, and W. Voos. 2000. Protein unfolding by mitochondria. The Hsp70 import motor. EMBO J. 1:404-410.
    • (2000) EMBO J. , vol.1 , pp. 404-410
    • Matouschek, A.1    Pfanner, N.2    Voos, W.3
  • 10
    • 0028951190 scopus 로고
    • Methotrexate inhibits proteolysis of dihydrofolate reductase by the N-end rule pathway
    • Johnston, J. A., E. S. Johnson, P. R. Waller, and A. Varshavsky. 1995. Methotrexate inhibits proteolysis of dihydrofolate reductase by the N-end rule pathway. J. Biol. Chem. 270:8172-8178.
    • (1995) J. Biol. Chem. , vol.270 , pp. 8172-8178
    • Johnston, J.A.1    Johnson, E.S.2    Waller, P.R.3    Varshavsky, A.4
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    • ATP-dependent proteases degrade their substrates by processively unraveling them from the degradation signal
    • Lee, C., M. P. Schwartz, S. Prakash, M. Iwakura, and A. Matouschek. 2001. ATP-dependent proteases degrade their substrates by processively unraveling them from the degradation signal. Mol. Cell. 7:627-637.
    • (2001) Mol. Cell. , vol.7 , pp. 627-637
    • Lee, C.1    Schwartz, M.P.2    Prakash, S.3    Iwakura, M.4    Matouschek, A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.