메뉴 건너뛰기




Volumn 4, Issue 1, 2006, Pages 155-168

High torsional energy disulfides: Relationship between cross-strand disulfides and right-handed staples

Author keywords

Cross strand disulfide; Disulfide; Redox signaling; Right handed staple

Indexed keywords

DISULFIDE;

EID: 33645288239     PISSN: 02197200     EISSN: None     Source Type: Journal    
DOI: 10.1142/S0219720006001734     Document Type: Article
Times cited : (15)

References (23)
  • 1
    • 0037018912 scopus 로고    scopus 로고
    • Thiol-disulfide exchange in an immunoglobulin-like fold: Structure of the N-terminal domain of DsbD
    • Goulding CW, Sawaya MR, Parseghian A et al., Thiol-disulfide exchange in an immunoglobulin-like fold: Structure of the N-terminal domain of DsbD, Biochemistry 41:6920-7, 2002.
    • (2002) Biochemistry , vol.41 , pp. 6920-6927
    • Goulding, C.W.1    Sawaya, M.R.2    Parseghian, A.3
  • 2
    • 0027481123 scopus 로고
    • Redox properties of protein disulfide isomerase (DsbA) from Escherichia coli
    • Wunderlich M, Glockshuber R, Redox properties of protein disulfide isomerase (DsbA) from Escherichia coli, Protein Sci 2:717-26, 1993.
    • (1993) Protein Sci , vol.2 , pp. 717-726
    • Wunderlich, M.1    Glockshuber, R.2
  • 3
    • 0031776171 scopus 로고    scopus 로고
    • A single dipeptide sequence modulates the redox properties of a whole enzyme family
    • Huber-Wunderlich M, Glockshuber R, A single dipeptide sequence modulates the redox properties of a whole enzyme family, Fold Des 3:161-71, 1998.
    • (1998) Fold Des , vol.3 , pp. 161-171
    • Huber-Wunderlich, M.1    Glockshuber, R.2
  • 4
    • 0024324626 scopus 로고
    • Urea dependence of thiol-disulfide equilibria in thioredoxin: Confirmation of the linkage relationship and a sensitive assay for structure
    • Lin TY, Kim PS, Urea dependence of thiol-disulfide equilibria in thioredoxin: Confirmation of the linkage relationship and a sensitive assay for structure, Biochemistry 28:5282-7, 1989.
    • (1989) Biochemistry , vol.28 , pp. 5282-5287
    • Lin, T.Y.1    Kim, P.S.2
  • 5
    • 0025118967 scopus 로고
    • Molecular and cellular aspects of thiol-disulfide exchange
    • Gilbert HF, Molecular and cellular aspects of thiol-disulfide exchange, Adv Enzymol Relat Areas Mol Biol 63:69-172, 1990.
    • (1990) Adv Enzymol Relat Areas Mol Biol , vol.63 , pp. 69-172
    • Gilbert, H.F.1
  • 6
    • 0029058159 scopus 로고
    • An analysis of side chain interactions and pair correlations within antiparallel β-sheets: The differences between backbone hydrogen-bonded and non-hydrogen-bonded residue pairs
    • Wouters MA, Curmi PM, An analysis of side chain interactions and pair correlations within antiparallel β-sheets: The differences between backbone hydrogen-bonded and non-hydrogen-bonded residue pairs, Proteins 22:119-31, 1995.
    • (1995) Proteins , vol.22 , pp. 119-131
    • Wouters, M.A.1    Curmi, P.M.2
  • 7
    • 0019443447 scopus 로고
    • The anatomy and taxonomy of protein structure
    • Richardson JS, The anatomy and taxonomy of protein structure, Adv Protein Chem 34:167-339, 1981.
    • (1981) Adv Protein Chem , vol.34 , pp. 167-339
    • Richardson, J.S.1
  • 8
    • 0036341983 scopus 로고    scopus 로고
    • Disulphide exchange in domain 2 of CD4 is required for entry of the Human Immunodeficiency Virus Type 1
    • Matthias LJ, Yam PTW, Jiang X-M et al., Disulphide exchange in domain 2 of CD4 is required for entry of the Human Immunodeficiency Virus Type 1, Nature Immunol 3:727-732, 2002.
    • (2002) Nature Immunol , vol.3 , pp. 727-732
    • Matthias, L.J.1    Yam, P.T.W.2    Jiang, X.-M.3
  • 9
    • 0842344106 scopus 로고    scopus 로고
    • Investigating mitochondrial redox potential with redox-sensitive green fluorescent protein indicators
    • Hanson GT, Aggeler R, Oglesbe D et al., Investigating mitochondrial redox potential with redox-sensitive green fluorescent protein indicators, J Biol Chem 279(13): 13044-53, 2004.
    • (2004) J Biol Chem , vol.279 , Issue.13 , pp. 13044-13053
    • Hanson, G.T.1    Aggeler, R.2    Oglesbe, D.3
  • 10
    • 0842325793 scopus 로고    scopus 로고
    • Energy substrate modulates mitochondrial structure and oxidative capacity in cancer cells
    • Rossignol R, Gilkerson R, Aggeler R et al., Energy substrate modulates mitochondrial structure and oxidative capacity in cancer cells, Cancer Res 64:985-93, 2004.
    • (2004) Cancer Res , vol.64 , pp. 985-993
    • Rossignol, R.1    Gilkerson, R.2    Aggeler, R.3
  • 11
    • 0346374729 scopus 로고    scopus 로고
    • Cross-strand disulphides in cell entry proteins: Poised to act
    • Wouters MA, Lau KK, Hogg PJ, Cross-strand disulphides in cell entry proteins: Poised to act, Bioessays 26:73-9, 2004.
    • (2004) Bioessays , vol.26 , pp. 73-79
    • Wouters, M.A.1    Lau, K.K.2    Hogg, P.J.3
  • 12
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W, Sander C, Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features, Biopolymers 22:2577-637, 1983.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 13
    • 0028961335 scopus 로고
    • SCOP: A structural classification of proteins database for the investigation of sequences and structures
    • Murzin AG, Brenner SE, Hubbard T, Chothia C, SCOP: A structural classification of proteins database for the investigation of sequences and structures, J Mol Biol 247:536-40, 1995.
    • (1995) J Mol Biol , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 14
    • 0029633186 scopus 로고
    • AMBER, a computer program for applying molecular mechanics, normal mode analysis, molecular dynamics and free energy calculations to elucidate the structures and energies of molecules
    • Pearlman DA, Case DA, Caldwell JW et al., AMBER, a computer program for applying molecular mechanics, normal mode analysis, molecular dynamics and free energy calculations to elucidate the structures and energies of molecules, Comp Phys Commun 91:1-41, 1995.
    • (1995) Comp Phys Commun , vol.91 , pp. 1-41
    • Pearlman, D.A.1    Case, D.A.2    Caldwell, J.W.3
  • 15
    • 0030573025 scopus 로고    scopus 로고
    • The disulphide β-cross: From cystine geometry and clustering to classification of small disulphide-rich protein folds
    • Harrison PM, Sternberg MJ, The disulphide β-cross: From cystine geometry and clustering to classification of small disulphide-rich protein folds, J Mol Biol 264: 603-23, 1996.
    • (1996) J Mol Biol , vol.264 , pp. 603-623
    • Harrison, P.M.1    Sternberg, M.J.2
  • 16
    • 84985436412 scopus 로고
    • Conformational properties of disulphide bridges. 2. Rotational potentials of diethyl disulphide
    • Görbitz CH, Conformational properties of disulphide bridges. 2. Rotational potentials of diethyl disulphide, J Phys Org Chem 7:259-267, 1994.
    • (1994) J Phys Org Chem , vol.7 , pp. 259-267
    • Görbitz, C.H.1
  • 17
    • 0035909839 scopus 로고    scopus 로고
    • Role of the disulfide cleavage induced molten globule state of type a botulinum neurotoxin in its endopeptidase activity
    • Cai S, Singh BR, Role of the disulfide cleavage induced molten globule state of type a botulinum neurotoxin in its endopeptidase activity, Biochemistry 40:15327-33, 2001.
    • (2001) Biochemistry , vol.40 , pp. 15327-15333
    • Cai, S.1    Singh, B.R.2
  • 18
    • 0028104784 scopus 로고
    • PapD chaperone function in pilus biogenesis depends on oxidant and chaperone-like activities of DsbA
    • Jacob-Dubuisson F, Pinkner J, Xu Z et al., PapD chaperone function in pilus biogenesis depends on oxidant and chaperone-like activities of DsbA, Proc Natl Acad Sci USA 91:11552-6, 1994.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 11552-11556
    • Jacob-Dubuisson, F.1    Pinkner, J.2    Xu, Z.3
  • 19
    • 0020991935 scopus 로고
    • Structural properties of protein beta-sheets
    • Salemme FR, Structural properties of protein beta-sheets, Prog Biophys Mol Biol 42(2-3):95-133, 1983.
    • (1983) Prog Biophys Mol Biol , vol.42 , Issue.2-3 , pp. 95-133
    • Salemme, F.R.1
  • 21
    • 0142057021 scopus 로고    scopus 로고
    • Plant peroxiredoxins
    • Dietz KJ, Plant peroxiredoxins, Annu Rev Plant Biol 54:93-107, 2003.
    • (2003) Annu Rev Plant Biol , vol.54 , pp. 93-107
    • Dietz, K.J.1
  • 22
    • 2342593248 scopus 로고    scopus 로고
    • Structure-activity relationships for the β-hairpin cationic antimicrobial peptide polyphemusin I
    • Powers JP, Rozek A, Hancock RE, Structure-activity relationships for the β-hairpin cationic antimicrobial peptide polyphemusin I, Biochim Biophys Acta 1698:239-50, 2004.
    • (2004) Biochim Biophys Acta , vol.1698 , pp. 239-250
    • Powers, J.P.1    Rozek, A.2    Hancock, R.E.3
  • 23
    • 16844367916 scopus 로고    scopus 로고
    • Structural mechanism of oxidative regulation of the phosphatase Cdc25B via an intramolecular disulfide bond
    • Buhrman G, Parker B, Sohn J et al., Structural mechanism of oxidative regulation of the phosphatase Cdc25B via an intramolecular disulfide bond, Biochemistry 44:7602, 2005.
    • (2005) Biochemistry , vol.44 , pp. 7602
    • Buhrman, G.1    Parker, B.2    Sohn, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.