Evolution of the primate cathelicidin. Correlation between structural variations and antimicrobial activity. - Wikidata - wikimedia - TriplyDB

Evolution of the primate cathelicidin. Correlation between structural variations and antimicrobial activity.

Evolution of the primate cathelicidin. Correlation between structural variations and antimicrobial activity.

http://www.wikidata.org/entity/Q38312969

about

Potential Use of Antimicrobial Peptides as Vaginal Spermicides/Microbicides Structures of human host defense cathelicidin LL-37 and its smallest antimicrobial peptide KR-12 in lipid micelles Structure, Dynamics, and Antimicrobial and Immune Modulatory Activities of Human LL-23 and Its Single-Residue Variants Mutated on the Basis of Homologous Primate Cathelicidins Highly selective end-tagged antimicrobial peptides derived from PRELP Cathelicidin-like helminth defence molecules (HDMs): absence of cytotoxic, anti-microbial and anti-protozoan activities imply a specific adaptation to immune modulation Trans-species polymorphism at antimicrobial innate immunity cathelicidin genes of Atlantic cod and related species Promiscuity and the rate of molecular evolution at primate immunity genes Evolution of the hepcidin gene in primates Mast cell cathelicidin antimicrobial peptide prevents invasive group A Streptococcus infection of the skin.Structure-function relationship of the human antimicrobial peptide LL-37 and LL-37 fragments in the modulation of TLR responses.Broad-spectrum activity against bacterial mastitis pathogens and activation of mammary epithelial cells support a protective role of neutrophil cathelicidins in bovine mastitis Expression and activity of a novel cathelicidin from domestic cats.Lipopolysaccharide Phosphorylation by the WaaY Kinase Affects the Susceptibility of Escherichia coli to the Human Antimicrobial Peptide LL-37.Characterization of selective antibacterial peptides by polarity index.Antimicrobial peptides in human skin disease.The human cathelicidin LL-37 modulates the activities of the P2X7 receptor in a structure-dependent manner.Antimicrobial peptides, skin infections, and atopic dermatitis Identification of Human Cathelicidin Peptide LL-37 as a Ligand for Macrophage Integrin αMβ2 (Mac-1, CD11b/CD18) that Promotes Phagocytosis by Opsonizing Bacteria.Human cathelicidin LL-37 prevents bacterial biofilm formation.Destabilization of α-Helical Structure in Solution Improves Bactericidal Activity of Antimicrobial Peptides: Opposite Effects on Bacterial and Viral Targets.Critical Role of Antimicrobial Peptide Cathelicidin for Controlling Helicobacter pylori Survival and Infection.NAD-dependent ADP-ribosylation of the human antimicrobial and immune-modulatory peptide LL-37 by ADP-ribosyltransferase-1.Human beta-defensin 3 inhibits cell wall biosynthesis in Staphylococci.Positive selection in cathelicidin host defense peptides: adaptation to exogenous pathogens or endogenous receptors?Saliva enables the antimicrobial activity of LL-37 in the presence of proteases of Porphyromonas gingivalis.Ultrastructural immunolocalization of beta-defensin-27 in granulocytes of the dermis and wound epidermis of lizard suggests they contribute to the anti-microbial skin barrier.Salt-resistant homodimeric bactenecin, a cathelicidin-derived antimicrobial peptide.New aspects of the structure and mode of action of the human cathelicidin LL-37 revealed by the intrinsic probe p-cyanophenylalanine.Vipericidins: a novel family of cathelicidin-related peptides from the venom gland of South American pit vipers.Evolutionary analysis of the contact system indicates that kininogen evolved adaptively in mammals and in human populations.The Sam-Sam interaction between Ship2 and the EphA2 receptor: design and analysis of peptide inhibitors.Preservation of antimicrobial properties of complement peptide C3a, from invertebrates to humans.Deep Learning Improves Antimicrobial Peptide Recognition.Optimized Microwave Assisted Synthesis of LL37, a Cathelicidin Human Antimicrobial Peptide

P2860

Q26765450-7CB171B5-051F-4991-A723-66401EC2FA57 Q27652293-372D47AF-302B-4BE5-A13A-2A6D9ADFCBC8 Q27676333-FCB81F9F-13C6-44A4-9916-180228F45A7A Q28476835-10C30EB0-017A-4F49-99F7-0856A725F277 Q28534617-64094F94-640D-4EC3-91CE-65CD04EC33D7 Q28646290-BCFB1E1B-92C2-4817-AAA3-8D56FC7D78BB Q28749670-F65E6CB4-89AD-4FCE-9B60-324C3F3FB1DD Q33322611-B89E0F89-D102-452A-888C-E27171775E1B Q33336048-AA5E8421-6D77-4C74-BFD6-B294A506D3D0 Q33402604-DD7D5F6C-509D-4662-9927-132A0DEC16FE Q33769066-FE3760BB-DDD1-47E8-AD64-1AE5942EB4E4 Q33886915-11710704-24CD-4F6E-A5F7-1997AD04C70E Q35925899-021818C4-A303-4E12-9492-0A09E3B96FB2 Q35947562-64A0CC0C-6C9A-4284-88B9-A0B2EBA7152E Q37034707-22071CE7-D4F7-4CE6-9D1A-27432D140EA6 Q37142680-8A5CD776-997C-4FBD-BF81-E1198B63B918 Q37213664-42339C7B-6EB9-4CCE-A721-B7E3EAC0A5AC Q37505380-66F82CDD-8DEE-4D94-9929-8717047F5232 Q38037192-868530EE-F06E-4C33-B7F3-151717B78970 Q38798266-89AC8814-64E6-42E1-A023-F55115B3613A Q38800391-A0F9F914-590B-4EBE-9BF6-7C9DDEC53B54 Q38965476-93749833-1280-45F1-9140-1549A917D19B Q40755190-D5D1AF63-E5E8-4EA2-A170-4CB198A94FC2 Q41469857-CD36F733-BCC7-4FB9-AD84-790BB3073E30 Q42078203-F2A82B9A-C0FA-437F-B179-568D56134AA5 Q42770099-31945353-8986-43FA-B541-A973822375C2 Q43958057-9E0FFCFC-6527-48F9-9938-1331544849E3 Q46816985-CBCFA768-29D5-4870-8358-C07D175DE3DC Q46855761-52962DF1-9684-406C-8193-D92E6343AE9A Q46914473-79DEDA04-2F92-49E4-9528-4479572AD7DC Q47133936-F6017835-6B78-425D-9FD7-DE5F77980D07 Q47831006-EA43703A-79FA-4BA8-8A68-5D8F1E6D0C00 Q52625530-4F1BDBC5-9A22-4AE7-9F90-21A79699B026 Q57179930-DC414384-E355-42BE-B48E-2F55207AB1E1

P2860

Evolution of the primate cathelicidin. Correlation between structural variations and antimicrobial activity.

http://www.wikidata.org/entity/Q38312969

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

Evolution of the primate cathe ...... ns and antimicrobial activity.

@en

type

label

Evolution of the primate cathe ...... ns and antimicrobial activity.

@en

prefLabel

Evolution of the primate cathe ...... ns and antimicrobial activity.

@en

P1433

Q38312969-9B8FCE6D-0530-4704-B49C-4942F43C54AD

P1476

Q38312969-46018BFD-9BA9-4950-9B8A-C7E10F2DA460

P2093

Q38312969-0BFCE4CB-7B7B-45E3-9331-21E22B9AD463

Q38312969-409FC74B-5A65-4B2F-816F-B003AF3C1D2A

Q38312969-8921DFB7-0CFA-4352-BDAB-9EEBFC873640

Q38312969-AC7E173C-82FA-4D9F-9E4A-0B2D07354CFE

Q38312969-C099A663-6015-4048-B6B1-1AA1B23B234B

Q38312969-C1028D57-160D-4664-A130-F2D2FF353F14

Q38312969-DC8D3657-91FC-4675-A3E1-19871F43617D

Q38312969-FD949E34-167F-4C1A-8FB7-D35A770F90DA

P2860

Q38312969-0B07992A-D913-429A-899E-D15B2AC6C7D8

Q38312969-10815E87-1C20-4335-AC1B-542C3C55D296

Q38312969-1198163F-1EAB-40CD-8B25-28482265C8B9

Q38312969-317318D9-3932-4C27-8FE0-3DC651EDF4FF

Q38312969-44A231AE-7D6C-42CA-8A97-6BFC65E72329

Q38312969-4D98107E-5ED8-4EB2-B4A2-D60282CC9E0F

Q38312969-515EDEFB-F66E-4DC7-84FD-538347063313

Q38312969-51DC4324-2A9C-4824-AFA5-BB1DE38D65A9

Q38312969-6673498D-A0DD-424A-8EFF-519F2C2AF33A

Q38312969-72C77178-5D55-4DFD-9F1D-9C17B087B55F

P304

Q38312969-BF12392D-6617-4DF6-B2DC-55E7A1ECA843

P31

Q38312969-52CEA375-8BB9-4F92-9E56-6B92F31D25D0

P356

Q38312969-6CF50F9B-428D-4302-A081-225301E19B76

P407

Q38312969-97B6C36B-D42B-4B1A-A991-9BDB8D61A963

P433

Q38312969-6022F1EE-AF96-40B6-8F3B-C8C1A83B4571

P478

Q38312969-11414836-485D-42B7-893F-62C84461C87C

P577

Q38312969-47B056DA-C50C-4792-B0BC-13B774DEA39D

P5875

Q38312969-B59C4375-9B42-434D-B443-43C4E56AE6D2

P698

Q38312969-527142F4-17FD-4473-A390-4ED44BF8BC17

P356

P1433

Journal of Biological Chemistry

P1476

Evolution of the primate cathe ...... ns and antimicrobial activity.

@en

P2093

Alessandra Pontillo

http://www.w3.org/2001/XMLSchema#string

Alessandro Tossi

http://www.w3.org/2001/XMLSchema#string

Igor Zelezetsky

http://www.w3.org/2001/XMLSchema#string

Luca Puzzi

http://www.w3.org/2001/XMLSchema#string

Ludovica Segat

http://www.w3.org/2001/XMLSchema#string

Nikolinka Antcheva

http://www.w3.org/2001/XMLSchema#string

Sabrina Pacor

http://www.w3.org/2001/XMLSchema#string

Sergio Crovella

http://www.w3.org/2001/XMLSchema#string

P2860

Postsecretory processing generates multiple cathelicidins for enhanced topical antimicrobial defense

The human gene FALL39 and processing of the cathelin precursor to the antibacterial peptide LL-37 in granulocytes

LL-37, the neutrophil granule- and epithelial cell-derived cathelicidin, utilizes formyl peptide receptor-like 1 (FPRL1) as a receptor to chemoattract human peripheral blood neutrophils, monocytes, and T cells

PAML: a program package for phylogenetic analysis by maximum likelihood

Human cathelicidin, hCAP-18, is processed to the antimicrobial peptide LL-37 by extracellular cleavage with proteinase 3

Antimicrobial and protease inhibitory functions of the human cathelicidin (hCAP18/LL-37) prosequence

Cathelicidins, multifunctional peptides of the innate immunity

Likelihood ratio tests for detecting positive selection and application to primate lysozyme evolution

Structure-function relationships among human cathelicidin peptides: dissociation of antimicrobial properties from host immunostimulatory activities.

Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides.

P304

19861-19871

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1074/JBC.M511108200

http://www.w3.org/2001/XMLSchema#string

P407

P433

29

http://www.w3.org/2001/XMLSchema#string

P478

281

http://www.w3.org/2001/XMLSchema#string

P577

2006-05-23T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

7061296

http://www.w3.org/2001/XMLSchema#string

P698

16720578

http://www.w3.org/2001/XMLSchema#string