Comparison of biophysical and biologic properties of alpha-helical enantiomeric antimicrobial peptides.
about
Effect of BMAP-28 antimicrobial peptides on Leishmania major promastigote and amastigote growth: role of leishmanolysin in parasite survivalA retro-inverso cell-penetrating peptide for siRNA delivery."Specificity Determinants" Improve Therapeutic Indices of Two Antimicrobial Peptides Piscidin 1 and Dermaseptin S4 Against the Gram-negative Pathogens Acinetobacter baumannii and Pseudomonas aeruginosaDiscovery of a small peptide from combinatorial libraries that can activate the plant immune system by a jasmonic acid signaling pathway.Hydrophobicity and helicity regulate the antifungal activity of 14-helical β-peptides.Rational design of α-helical antimicrobial peptides to target Gram-negative pathogens, Acinetobacter baumannii and Pseudomonas aeruginosa: utilization of charge, 'specificity determinants,' total hydrophobicity, hydrophobe type and location as desigEvolution of antimicrobial peptides to self-assembled peptides for biomaterial applicationsA D-peptide analog of the second extracellular loop of claudin-3 and -4 leads to mislocalized claudin and cellular apoptosis in mammary epithelial cells.Structure-guided RP-HPLC chromatography of diastereomeric α-helical peptide analogs substituted with single amino acid stereoisomersAnti-tuberculosis activity of α-helical antimicrobial peptides: de novo designed L- and D-enantiomers versus L- and D-LL-37.Role of peptide hydrophobicity in the mechanism of action of alpha-helical antimicrobial peptides.The Acinetobacter baumannii Oxymoron: Commensal Hospital Dweller Turned Pan-Drug-Resistant Menace.Effects of hydrophobicity on the antifungal activity of alpha-helical antimicrobial peptides.Effects of net charge and the number of positively charged residues on the biological activity of amphipathic alpha-helical cationic antimicrobial peptides.An antibacterial and absorbable silk-based fixation material with impressive mechanical properties and biocompatibilityCationic amphiphiles, a new generation of antimicrobials inspired by the natural antimicrobial peptide scaffoldAlpha-helical cationic antimicrobial peptides: relationships of structure and functionThe potential of antimicrobial peptides as biocides.Beyond conventional antibiotics - New directions for combination products to combat biofilm.Synthesis of composites SBA-15 mesoporous particles carrying oxytocin and evaluation of their properties, functions, and in vitro biological activities.Design of potent, non-toxic anticancer peptides based on the structure of the antimicrobial peptide, temporin-1CEa.Enhanced Antimicrobial Activity of AamAP1-Lysine, a Novel Synthetic Peptide Analog Derived from the Scorpion Venom Peptide AamAP1.Knowledge-based computational methods for identifying or designing novel, non-homologous antimicrobial peptides.Preliminary investigations into developing all-D Omiganan for treating Mupirocin-resistant MRSA skin infections.Novel antimicrobial peptide CPF-C1 analogs with superior stabilities and activities against multidrug-resistant bacteria.Preparative reversed-phase high-performance liquid chromatography collection efficiency for an antimicrobial peptide on columns of varying diameters (1mm to 9.4mm I.D.).Novel method to identify the optimal antimicrobial peptide in a combination matrix, using anoplin as an example.In vitro activities of synthetic host defense propeptides processed by neutrophil elastase against cystic fibrosis pathogensRole of helicity on the anticancer mechanism of action of cationic-helical peptides.Improved protease stability of the antimicrobial peptide Pin2 substituted with D-amino acids.D-form KLKLLLLLKLK-NH2 peptide exerts higher antimicrobial properties than its L-form counterpart via an association with bacterial cell wall components.New linear antiplasmodial peptides related to angiotensin II.Lipid-packing perturbation of model membranes by pH-responsive antimicrobial peptides.D-Cateslytin, a new antimicrobial peptide with therapeutic potential.Origin of low mammalian cell toxicity in a class of highly active antimicrobial amphipathic helical peptides.Synthetic host defense peptide IDR-1002 reduces inflammation in Pseudomonas aeruginosa lung infection.Co-administration of iRGD with peptide HPRP-A1 to improve anticancer activity and membrane penetrability.Role of positively charged residues on the polar and non-polar faces of amphipathic α-helical antimicrobial peptides on specificity and selectivity for Gram-negative pathogens.Tryptophan as a probe to study the anticancer mechanism of action and specificity of α-helical anticancer peptides.Functional synergy of α-helical antimicrobial peptides and traditional antibiotics against Gram-negative and Gram-positive bacteria in vitro and in vivo.
P2860
Q28478343-B08A4EDA-549F-41BF-8D4A-9AA467F55477Q30847307-E57AC2CC-B9F7-4742-8050-ADBEC3977CE6Q33584712-BFE4D8BD-DD23-445B-B4B1-5C86EEBA7F9AQ33897986-0D363C22-99FE-4671-9B5D-B6C7A248557AQ33926906-2E9C880C-5E51-467A-A43F-0C98B5C5980FQ34713859-C78B8379-11D8-46B5-870D-FD1936B27B41Q34809662-4FDE1E92-D24B-4084-B34A-F5380BF78195Q34823180-81675569-8084-4043-8D2A-226A677F9EA1Q35017565-9199DCF1-4699-4BCC-BE8C-6EBD630D1ECAQ35687730-EE0486C1-9218-429D-A65B-D3EE478A075EQ35758832-FED29B00-C7F8-4F28-A934-FF0ACC0E1F39Q35905605-CEF3A778-8A4A-4BC8-B809-60A6F7C3050DQ37313642-B76DEA7D-AE30-49B6-B50A-AAF97E043E02Q37385746-22A5963C-F1A6-414D-AC43-DE9AE78CF9D0Q37424896-49BEE1EE-0611-436A-9928-17D68876B062Q37778941-CC67A050-0AE9-400B-8DF9-5034BECD2758Q37825833-E7C90AD3-B336-41BC-94CD-690A6542DE5CQ37954604-06C37824-289B-4E7A-907D-498B1A494A39Q38920223-4E3B11C6-0C5C-41B5-AF31-B7675A124121Q38964531-AEBEEA68-ADE1-4A27-8932-5E45411B7C46Q39162082-A7BCDD1B-C3E7-442A-B22C-63814074AB1DQ39202053-88684661-BF70-462A-A007-C7CAF4127B4BQ39788897-5F8DD9EA-8023-41D9-A0CE-798BEAAA7C71Q40185116-86D06195-7D93-4042-A87A-808E3AEAEF5BQ40266754-1F973EB8-2B1A-4A20-AA83-FB5DC93E70E5Q41897373-806AF7EF-1FD9-406C-828D-135963DE96F4Q41907555-CC41B630-063C-4C45-8B50-9CFFE67D1EDCQ42058965-291C39BE-C66B-4462-AF8F-DF19532CB6D8Q42237870-F1A39697-45E4-4F06-9D32-F7C356AF4854Q42251963-2BBA20BB-ABA9-4F79-BF0B-D50CF4E83908Q42318156-3A37A585-4995-4FD5-BBE3-F1011D246278Q42612783-BA11345A-2188-4FDF-B04B-BE0E87C1EA61Q44385177-76DADAD7-C9C9-4BA8-AEB2-B014011645A8Q44520859-C3B18F10-D1A7-49CF-A950-96FDF049ED77Q46628699-9BC86553-D737-4C61-9032-FBE14C37F4D7Q47118800-2EBC24C9-1BA2-4F33-B52F-C9FAB40B6B4EQ48112477-EF163228-E366-49FA-BFB3-B02BACEF5B53Q48242962-FE576A27-ED20-41CA-A974-BAB84085F6D7Q53473484-79D3CCB8-CF5E-4133-AFAF-283E785E50A8Q54282937-0330CAD1-396F-490E-B2A5-F14CE9D6D8E4
P2860
Comparison of biophysical and biologic properties of alpha-helical enantiomeric antimicrobial peptides.
description
2006 nî lūn-bûn
@nan
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
2006年论文
@zh
2006年论文
@zh-cn
name
Comparison of biophysical and ...... omeric antimicrobial peptides.
@en
type
label
Comparison of biophysical and ...... omeric antimicrobial peptides.
@en
prefLabel
Comparison of biophysical and ...... omeric antimicrobial peptides.
@en
P2093
P2860
P1476
Comparison of biophysical and ...... omeric antimicrobial peptides.
@en
P2093
Adriana I Vasil
Colin T Mant
Jane L Burns
Michael L Vasil
Robert S Hodges
Yuxin Chen
P2860
P304
P356
10.1111/J.1747-0285.2006.00349.X
P577
2006-02-01T00:00:00Z