메뉴 건너뛰기




Volumn 17, Issue 12, 2010, Pages 1325-1333

Photoreactive stapled BH3 peptides to dissect the BCL-2 family interactome

Author keywords

[No Author keywords available]

Indexed keywords

PEPTIDE; PROTEIN BCL 2;

EID: 78650437120     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chembiol.2010.09.015     Document Type: Article
Times cited : (43)

References (35)
  • 1
    • 1842450290 scopus 로고    scopus 로고
    • A docking approach to the study of copper trafficking proteins; Interaction between metallochaperones and soluble domains of copper ATPases
    • F. Arnesano, L. Banci, I. Bertini, and A.M. Bonvin A docking approach to the study of copper trafficking proteins; interaction between metallochaperones and soluble domains of copper ATPases Structure 12 2004 669 676
    • (2004) Structure , vol.12 , pp. 669-676
    • Arnesano, F.1    Banci, L.2    Bertini, I.3    Bonvin, A.M.4
  • 3
    • 50349097899 scopus 로고    scopus 로고
    • Chapter 22 synthesis and biophysical characterization of stabilized alpha-helices of BCL-2 domains
    • G.H. Bird, F. Bernal, K. Pitter, and L.D. Walensky Chapter 22 synthesis and biophysical characterization of stabilized alpha-helices of BCL-2 domains Methods Enzymol. 446 2008 369 386
    • (2008) Methods Enzymol. , vol.446 , pp. 369-386
    • Bird, G.H.1    Bernal, F.2    Pitter, K.3    Walensky, L.D.4
  • 5
    • 0027731091 scopus 로고
    • Role of the mu immunoglobulin heavy chain transmembrane and cytoplasmic domains in B cell antigen receptor expression and signal transduction
    • J.H. Blum, T.L. Stevens, and A.L. DeFranco Role of the mu immunoglobulin heavy chain transmembrane and cytoplasmic domains in B cell antigen receptor expression and signal transduction J. Biol. Chem. 268 1993 27236 27245
    • (1993) J. Biol. Chem. , vol.268 , pp. 27236-27245
    • Blum, J.H.1    Stevens, T.L.2    Defranco, A.L.3
  • 8
    • 33846674886 scopus 로고    scopus 로고
    • Mcl-1 down-regulation potentiates ABT-737 lethality by cooperatively inducing Bak activation and Bax translocation
    • S. Chen, Y. Dai, H. Harada, P. Dent, and S. Grant Mcl-1 down-regulation potentiates ABT-737 lethality by cooperatively inducing Bak activation and Bax translocation Cancer Res. 67 2007 782 791
    • (2007) Cancer Res. , vol.67 , pp. 782-791
    • Chen, S.1    Dai, Y.2    Harada, H.3    Dent, P.4    Grant, S.5
  • 11
    • 0037442962 scopus 로고    scopus 로고
    • HADDOCK: A protein-protein docking approach based on biochemical or biophysical information
    • C. Dominguez, R. Boelens, and A.M. Bonvin HADDOCK: a protein-protein docking approach based on biochemical or biophysical information J. Am. Chem. Soc. 125 2003 1731 1737
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 1731-1737
    • Dominguez, C.1    Boelens, R.2    Bonvin, A.M.3
  • 12
    • 0028235205 scopus 로고
    • Benzophenone photophores in biochemistry
    • G. Dorman, and G.D. Prestwich Benzophenone photophores in biochemistry Biochemistry 33 1994 5661 5673
    • (1994) Biochemistry , vol.33 , pp. 5661-5673
    • Dorman, G.1    Prestwich, G.D.2
  • 13
    • 77449146854 scopus 로고    scopus 로고
    • Target-decoy search strategy for mass spectrometry-based proteomics
    • J.E. Elias, and S.P. Gygi Target-decoy search strategy for mass spectrometry-based proteomics Methods Mol. Biol. 604 2010 55 71
    • (2010) Methods Mol. Biol. , vol.604 , pp. 55-71
    • Elias, J.E.1    Gygi, S.P.2
  • 14
    • 0000857494 scopus 로고
    • An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database
    • J.K. Eng, A.L. McCormack, and J.R. Yates An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database J. Am. Soc. Mass Spectrom. 5 1994 976 989
    • (1994) J. Am. Soc. Mass Spectrom. , vol.5 , pp. 976-989
    • Eng, J.K.1    McCormack, A.L.2    Yates, J.R.3
  • 19
    • 0030575937 scopus 로고    scopus 로고
    • Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain
    • DOI 10.1126/science.274.5289.948
    • P.H. Kussie, S. Gorina, V. Marechal, B. Elenbaas, J. Moreau, A.J. Levine, and N.P. Pavletich Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain Science 274 1996 948 953 (Pubitemid 26398409)
    • (1996) Science , vol.274 , Issue.5289 , pp. 948-953
    • Kussie, P.H.1    Gorina, S.2    Marechal, V.3    Elenbaas, B.4    Moreau, J.5    Levine, A.J.6    Pavletich, N.P.7
  • 20
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
    • R.A. Laskowski, J.A. Rullmannn, M.W. MacArthur, R. Kaptein, and J.M. Thornton AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR J. Biomol. NMR 8 1996 477 486
    • (1996) J. Biomol. NMR , vol.8 , pp. 477-486
    • Laskowski, R.A.1    Rullmannn, J.A.2    MacArthur, M.W.3    Kaptein, R.4    Thornton, J.M.5
  • 21
    • 0037316363 scopus 로고    scopus 로고
    • ARIA: Automated NOE assignment and NMR structure calculation
    • J.P. Linge, M. Habeck, W. Rieping, and M. Nilges ARIA: automated NOE assignment and NMR structure calculation Bioinformatics 19 2003 315 316
    • (2003) Bioinformatics , vol.19 , pp. 315-316
    • Linge, J.P.1    Habeck, M.2    Rieping, W.3    Nilges, M.4
  • 23
    • 34548183872 scopus 로고    scopus 로고
    • Protocol for micro-purification, enrichment, pre-fractionation and storage of peptides for proteomics using StageTips
    • J. Rappsilber, M. Mann, and Y. Ishihama Protocol for micro-purification, enrichment, pre-fractionation and storage of peptides for proteomics using StageTips Nat. Protoc. 2 2007 1896 1906
    • (2007) Nat. Protoc. , vol.2 , pp. 1896-1906
    • Rappsilber, J.1    Mann, M.2    Ishihama, Y.3
  • 26
    • 0034697649 scopus 로고    scopus 로고
    • An all-hydrocarbon cross-linking system for enhancing the helicity and metabolic stability of peptides
    • C. Schafmeister, J. Po, and G. Verdine An all-hydrocarbon cross-linking system for enhancing the helicity and metabolic stability of peptides J. Am. Chem. Soc. 122 2000 5891 5892
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 5891-5892
    • Schafmeister, C.1    Po, J.2    Verdine, G.3
  • 27
    • 77955891885 scopus 로고    scopus 로고
    • The MCL-1 BH3 helix is an exclusive MCL-1 inhibitor and apoptosis sensitizer
    • M.L. Stewart, E. Fire, A.E. Keating, and L.D. Walensky The MCL-1 BH3 helix is an exclusive MCL-1 inhibitor and apoptosis sensitizer Nat. Chem. Biol 6 2010 595 601
    • (2010) Nat. Chem. Biol , vol.6 , pp. 595-601
    • Stewart, M.L.1    Fire, E.2    Keating, A.E.3    Walensky, L.D.4
  • 29
    • 33846889729 scopus 로고    scopus 로고
    • Photoaffinity labeling and its application in structural biology
    • E.L. Vodovozova Photoaffinity labeling and its application in structural biology Biochemistry (Mosc.) 72 2007 1 20
    • (2007) Biochemistry (Mosc.) , vol.72 , pp. 1-20
    • Vodovozova, E.L.1
  • 34
    • 0028809209 scopus 로고
    • Bad, a heterodimeric partner for Bcl-XL and Bcl-2, displaces Bax and promotes cell death
    • E. Yang, J. Zha, J. Jockel, L.H. Boise, C.B. Thompson, and S.J. Korsmeyer Bad, a heterodimeric partner for Bcl-XL and Bcl-2, displaces Bax and promotes cell death Cell 80 1995 285 291
    • (1995) Cell , vol.80 , pp. 285-291
    • Yang, E.1    Zha, J.2    Jockel, J.3    Boise, L.H.4    Thompson, C.B.5    Korsmeyer, S.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.