Protease inhibitors from plants with antimicrobial activity

scientific article published on 23 June 2009

Protease inhibitors from plants with antimicrobial activity is …
instance of (P31):
scholarly articleQ13442814
review articleQ7318358

External links are
P356DOI10.3390/IJMS10062860
P932PMC publication ID2705521
P698PubMed publication ID19582234
P5875ResearchGate publication ID26652007

P2093author name stringJin-Young Kim
Kyung-Soo Hahm
Seong-Cheol Park
Yoonkyung Park
Jae-Woon Nah
Indeok Hwang
Hyeonsook Cheong
P2860cites workDefensins: antimicrobial and cytotoxic peptides of mammalian cellsQ28268268
PR-1 protein inhibits the differentiation of rust infection hyphae in leaves of acquired resistant broad beanQ30321164
The disulfide bond pattern of catrocollastatin C, a disintegrin-like/cysteine-rich protein isolated from Crotalus atrox venomQ30444013
A novel antimicrobial protein isolated from potato (Solanum tuberosum) shares homology with an acid phosphataseQ31154259
Antimicrobial activity studies on a trypsin-chymotrypsin protease inhibitor obtained from potatoQ33213679
Purification and characterization of a heat-stable serine protease inhibitor from the tubers of new potato variety "Golden Valley".Q33246865
Identification and rational design of novel antimicrobial peptides for plant protectionQ33330976
The molecular characterization of two barley proteins establishes the novel PR-17 family of pathogenesis-related proteins.Q33612843
Plant defense peptidesQ33638733
Genes controlling expression of defense responses in ArabidopsisQ33718418
Diversity of antimicrobial peptides and their mechanisms of actionQ33789705
Differential scanning calorimetry and X-ray diffraction studies of the specificity of the interaction of antimicrobial peptides with membrane-mimetic systemsQ33789733
Potato carboxypeptidase inhibitor, a T-knot protein, is an epidermal growth factor antagonist that inhibits tumor cell growthQ34066456
From "carpet" mechanism to de-novo designed diastereomeric cell-selective antimicrobial peptidesQ34392413
Plant alpha-amylase inhibitors and their interaction with insect alpha-amylasesQ34539363
Antibacterial peptides: basic facts and emerging conceptsQ35203810
An unusual structural motif of antimicrobial peptides containing end-to-end macrocycle and cystine-knot disulfidesQ35588664
Anti-microbial peptides: from invertebrates to vertebrates.Q35806874
Antifungal proteins and peptides of leguminous and non-leguminous originsQ35832195
Proteinase inhibitors I and II from potatoes specifically block UV-induced activator protein-1 activation through a pathway that is independent of extracellular signal-regulated kinases, c-Jun N-terminal kinases, and P38 kinaseQ36631000
Purification, characterization, and molecular cloning of basic PR-1-type pathogenesis-related proteins from barleyQ36732117
Antimicrobial peptides and plant disease control.Q36764133
Polypeptide signaling for plant defensive genes exhibits analogies to defense signaling in animalsQ37223454
Amphibian skin: a promising resource for antimicrobial peptidesQ40437137
Plant Defensins: Novel Antimicrobial Peptides as Components of the Host Defense SystemQ40473953
The defensive role of nonspecific lipid-transfer proteins in plantsQ40512808
Innate immunity of insectsQ40540051
Susceptibility of Phytopathogenic Bacteria to Wheat Purothionins In VitroQ40731497
Protein proteinase inhibitors in legume seeds--overviewQ41460201
Cationic peptides: a new source of antibioticsQ41714967
Novel bifunctional alkaline protease inhibitor: protease inhibitory activity as the biochemical basis of antifungal activityQ43684386
Snakin-2, an antimicrobial peptide from potato whose gene is locally induced by wounding and responds to pathogen infectionQ43916190
Patatin, the tuber storage protein of potato (Solanum tuberosum L.), exhibits antioxidant activity in vitroQ44504988
The extracellular proteases of the phytopathogenic bacterium Xanthomonas campestrisQ44606911
Role of proteinase inhibitors in potato protectionQ44644728
Wound-induced proteinase inhibitors from tomato leaves. II. The cDNA-deduced primary structure of pre-inhibitor II.Q45000586
Kunitz-type serine protease inhibitor from potato (Solanum tuberosum L. cv. Jopung).Q46631520
Chemopreventive agents: protease inhibitorsQ47739935
Potato tuber proteins efficiently inhibit human faecal proteolytic activity: implications for treatment of peri-anal dermatitisQ47759659
Characterization and cDNA cloning of two glycine- and histidine-rich antimicrobial peptides from the roots of shepherd's purse, Capsella bursa-pastorisQ47807545
A napin-like polypeptide from dwarf Chinese white cabbage seeds with translation-inhibitory, trypsin-inhibitory, and antibacterial activities.Q47825690
Wheat genes encoding two types of PR-1 proteins are pathogen inducible, but do not respond to activators of systemic acquired resistanceQ47995066
Snakin-1, a peptide from potato that is active against plant pathogensQ47995084
GASA, a gibberellin-regulated gene family from Arabidopsis thaliana related to the tomato GAST1 geneQ48075242
Oral administration of proteinase inhibitor II from potatoes reduces energy intake in man.Q48891493
The octadecanoid signalling pathway in plants mediates a response to ultraviolet radiation.Q52199366
Pseudothionin-St1, a potato peptide active against potato pathogens.Q52542353
Pathogen-induced proteins with inhibitory activity toward Phytophthora infestansQ67908763
Isolation of soybean trypsin inhibitors by affinity chromatography on anhydrotrypsin-Sepharose 4BQ67966301
Biospecific haemosorbents based on proteinase inhibitor. I. Synthesis and propertiesQ70540668
Kunitz-type proteinase inhibitors from intact and Phytophthora-infected potato tubersQ74582949
The Bowman-Birk inhibitor from soybeans as an anticarcinogenic agentQ77665005
P275copyright licenseCreative Commons Attribution 3.0 UnportedQ14947546
P6216copyright statuscopyrightedQ50423863
P433issue6
P407language of work or nameEnglishQ1860
P921main subjecteukaryoteQ19088
mechanism of actionQ3271540
P304page(s)2860-2872
P577publication date2009-06-23
P1433published inInternational Journal of Molecular SciencesQ3153277
P1476titleProtease inhibitors from plants with antimicrobial activity
P478volume10