메뉴 건너뛰기




Volumn 38, Issue 7, 2006, Pages 457-466

Nuclear magnetic resonance studies on Huwentoxin-XI from the Chinese bird spider Ornithoctonus huwena: 15N labeling and sequence-specific 1H, 15N nuclear magnetic resonance assignments

Author keywords

15N labeling; Huwentoxin XI; Nuclear magnetic resonance; Sequence specific assignment; Toxin

Indexed keywords

POTASSIUM CHANNEL BLOCKING AGENT; PROTEINASE INHIBITOR; RECOMBINANT PROTEIN; SPIDER VENOM;

EID: 33746237510     PISSN: 16729145     EISSN: 17457270     Source Type: Journal    
DOI: 10.1111/j.1745-7270.2006.00191.x     Document Type: Article
Times cited : (15)

References (12)
  • 1
    • 0026530977 scopus 로고
    • Natural protein proteinase inhibitors and their interaction with proteinases
    • Bode W, Huber R. Natural protein proteinase inhibitors and their interaction with proteinases. Eur J Biochem 1992, 204: 433-451
    • (1992) Eur J Biochem , vol.204 , pp. 433-451
    • Bode, W.1    Huber, R.2
  • 2
    • 0026795399 scopus 로고
    • Determination of a high-quality nuclear magnetic resonance solution structure of the bovine pancreatic trypsin inhibitor and comparison with three crystal structures
    • Berndt KD, Guntert P, Orbons LP, Wuthrich K. Determination of a high-quality nuclear magnetic resonance solution structure of the bovine pancreatic trypsin inhibitor and comparison with three crystal structures. J Mol Biol 1992, 227: 757-775
    • (1992) J Mol Biol , vol.227 , pp. 757-775
    • Berndt, K.D.1    Guntert, P.2    Orbons, L.P.3    Wuthrich, K.4
  • 3
    • 0014211618 scopus 로고
    • On the size of the active site in proteases. I. Papain
    • Schlechter I, Berger A. On the size of the active site in proteases. I. Papain. Biochem Biophys Res Commun 1967, 27: 157-162
    • (1967) Biochem Biophys Res Commun , vol.27 , pp. 157-162
    • Schlechter, I.1    Berger, A.2
  • 4
    • 0033574398 scopus 로고    scopus 로고
    • The crystal structures of the complexes between bovine beta-trypsin and ten P1 variants of BPTI
    • Helland R, Otlewski J, Sundheim O, Dadlez M, Smalas AO. The crystal structures of the complexes between bovine beta-trypsin and ten P1 variants of BPTI. J Mol Biol 1999, 287: 923-942
    • (1999) J Mol Biol , vol.287 , pp. 923-942
    • Helland, R.1    Otlewski, J.2    Sundheim, O.3    Dadlez, M.4    Smalas, A.O.5
  • 5
    • 0035239235 scopus 로고    scopus 로고
    • Twenty years of dendrotoxins
    • Harvey AL. Twenty years of dendrotoxins. Toxicon 2001, 39: 15-26
    • (2001) Toxicon , vol.39 , pp. 15-26
    • Harvey, A.L.1
  • 7
    • 0030849278 scopus 로고    scopus 로고
    • Changes to biological activity following acetylation of dendrotoxin I from Dendroaspis polylepis (black mamba)
    • Harvey AL, Rowan EG, Vatanpour H, Engstrom A, Westerlund B, Karlsson E. Changes to biological activity following acetylation of dendrotoxin I from Dendroaspis polylepis (black mamba). Toxicon 1997, 35: 1263-1273
    • (1997) Toxicon , vol.35 , pp. 1263-1273
    • Harvey, A.L.1    Rowan, E.G.2    Vatanpour, H.3    Engstrom, A.4    Westerlund, B.5    Karlsson, E.6
  • 8
    • 0028865859 scopus 로고
    • Kalicludines and kaliseptine. Two different classes of sea anemone toxins for voltage sensitive K+ channels
    • Schweitz H, Bruhn T, Guillemare E, Moinier D, Lancelin JM, Beress L, Lazdunski M. Kalicludines and kaliseptine. Two different classes of sea anemone toxins for voltage sensitive K+ channels. J Biol Chem 1995, 270: 25121-25126
    • (1995) J Biol Chem , vol.270 , pp. 25121-25126
    • Schweitz, H.1    Bruhn, T.2    Guillemare, E.3    Moinier, D.4    Lancelin, J.M.5    Beress, L.6    Lazdunski, M.7
  • 10
    • 34249765651 scopus 로고
    • NMRView: A computer program for the visualization and analysis of NMR data
    • Johnson BA, Blevins RA. NMRView: A computer program for the visualization and analysis of NMR data. J Biomol NMR 1994, 4: 603-614
    • (1994) J Biomol NMR , vol.4 , pp. 603-614
    • Johnson, B.A.1    Blevins, R.A.2
  • 12
    • 0036147845 scopus 로고    scopus 로고
    • The structure of spider toxin huwentoxin-II with unique disulfide linkage: Evidence for structural evolution
    • Shu Q, Lu SY, Gu XC, Liang SP. The structure of spider toxin huwentoxin-II with unique disulfide linkage: Evidence for structural evolution. Protein Sci 2002, 11: 245-252
    • (2002) Protein Sci , vol.11 , pp. 245-252
    • Shu, Q.1    Lu, S.Y.2    Gu, X.C.3    Liang, S.P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.