Structural and functional aspects of PR-10 proteins

FEBS Journal

Volumn 280, Issue 5, 2013, Pages 1169-1199

  Fernandes, Humberto ^a,c   Michalska, Karolina ^b,d   Sikorski, Michal ^a   Jaskolski, Mariusz ^a,b  

^a INSTITUTE OF BIOORGANIC CHEMISTRY   (Poland)

^b ADAM MICKIEWICZ UNIVERSITY   (Poland)

^c IMPERIAL COLLEGE LONDON   (United Kingdom)

^d ARGONNE NATIONAL LABORATORY   (United States)

Author keywords

cytokinin; pathogenesis; phytohormones; plant allergen; PR 10; protein ligand binding

Indexed keywords

ABA RECEPTOR; ALLERGEN; ANTIFREEZE PROTEIN; AROMATASE; CELL PROTEIN; CELL RECEPTOR; CYTOKININ; DEOXYCHOLIC ACID; HYP 1 PROTEIN; NORCOCLAURINE SYNTHASE; PAPAIN; PATHOGENESIS RELATED PROTEIN 10; POLYMER; PROTEIN BET V 1ALPHA; PROTEIN CSBP; PROTEIN LLPR 10.2B; PROTEIN TCMN; RIBONUCLEASE; SPOROPOLLENIN; STEROIDOGENIC ACUTE REGULATORY PROTEIN; SYNTHETASE; UNCLASSIFIED DRUG; VEGETABLE PROTEIN; ZEATIN;

ALLERGIC REACTION; ALPHA HELIX; AMINO TERMINAL SEQUENCE; ANTIBACTERIAL ACTIVITY; ANTIFUNGAL ACTIVITY; ANTIPROTOZOAL ACTIVITY; ANTIVIRAL ACTIVITY; BETA SHEET; CARBOXY TERMINAL SEQUENCE; CHEMICAL STRESS; COMPLEX FORMATION; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; CRYSTALLIZATION; ENZYME ACTIVITY; HUMAN; HYDROPHOBICITY; IMMUNOCYTOCHEMISTRY; INFECTION; LIGAND BINDING; MEMBRANE BINDING; METAL BINDING; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; OLIGOMERIZATION; OXIDATIVE COUPLING; PARTICLE SIZE; PHYSICAL STRESS; PHYSIOLOGICAL STRESS; PLANT GENE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN EXPRESSION; PROTEIN FAMILY; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; PROTEIN STRUCTURE; REVIEW; SEQUENCE ALIGNMENT; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY; STRUCTURAL HOMOLOGY; THERMOSTABILITY; THREE DIMENSIONAL IMAGING; TRANSCRIPTION REGULATION; X RAY DIFFRACTION;

AMINO ACID SEQUENCE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PLANT PROTEINS; PLANTS; PROTEIN CONFORMATION; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 84874494513     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/febs.12114     Document Type: Review

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