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Volumn 277, Issue 37, 2002, Pages 34443-34450

Solution structure of peptide toxins that block mechanosensitive ion channels

(5) Oswald, Robert E a,b,c Suchyna, Thomas M a,b,c McFeeters, Robert a,b,c Gottlieb, Philip a,b,c Sachs, Frederick a,b,c

a Department of Obstetrics Gynecology (United States)

b UNIVERSITY AT BUFFALO (United States)

c Animal Health Diagnostic Center (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CELLS; HYDROPHOBICITY; NITROGEN COMPOUNDS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY;

ION CHANNELS;

BIOCHEMISTRY;

AROMATIC COMPOUND; CYSTEINE; ION CHANNEL; PEPTIDE; PEPTIDE GSMTX 2; PEPTIDE GSMTX 4; SPIDER VENOM; TOXIN; UNCLASSIFIED DRUG;

ANIMAL CELL; ANIMAL TISSUE; ARTICLE; ASTROCYTE; BINDING AFFINITY; CALCULATION; CELL SIZE; CONTROLLED STUDY; GENE EXPRESSION; HEART ARRHYTHMIA; HEART HYPERTROPHY; HYDROPHOBICITY; INFORMATION PROCESSING; ION CURRENT; MECHANORECEPTOR; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; OSMORECEPTION; PRIORITY JOURNAL; PROTEIN STRUCTURE; RAT; SPIDER; STRETCHING; SURFACE CHARGE;

AMINO ACID SEQUENCE; ANIMALS; DIFFUSION; DISULFIDES; ION CHANNELS; MOLECULAR SEQUENCE DATA; PEPTIDES; RATS; RATS, SPRAGUE-DAWLEY; SEQUENCE HOMOLOGY; SOLUTIONS; SPIDER VENOMS; STRUCTURE-ACTIVITY RELATIONSHIP;

ANIMALIA; ARANEAE; GRAMMOSTOLA SPATULATA;

EID: 0037072815 PISSN: 00219258 EISSN: None Source Type: Journal
DOI: 10.1074/jbc.M202715200 Document Type: Article

Times cited : (87)

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