(Q35582184)

9 August 2017

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title

Cathelicidin family of antimicrobial peptides: proteolytic processing and protease resistance (English)

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9 August 2017

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antimicrobial peptide

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inferred from title

author name string

Ann Eisenberg Shinnar

series ordinal

1

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9 August 2017

Kathryn L Butler

series ordinal

2

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9 August 2017

Hyon Ju Park

series ordinal

3

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9 August 2017

publication date

1 December 2003

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9 August 2017

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9 August 2017

volume

31

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9 August 2017

issue

6

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9 August 2017

page(s)

425-436

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Antimicrobial peptides of multicellular organisms

9 August 2017

cites work

1 reference

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Structural features and biological activities of the cathelicidin-derived antimicrobial peptides

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7 January 2021

Cathelicidins: a novel protein family with a common proregion and a variable C‐terminal antimicrobial domain

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The proprotein convertases

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Precursor processing by kex2/furin proteases

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Amidation of bioactive peptides: the structure of peptidylglycine alpha-hydroxylating monooxygenase

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

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Hagfish intestinal antimicrobial peptides are ancient cathelicidins

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Cathelicidin peptides as candidates for a novel class of antimicrobials

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Pro-rich antimicrobial peptides from animals: structure, biological functions and mechanism of action

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On the size of the active site in proteases. I. Papain

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Serine protease mechanism and specificity

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7 January 2021

Specificity of human cathepsin G.

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The role of proline in the proteolytic regulation of biologically active peptides

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Amino acid sequence restriction in relation to proteolysis

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7 January 2021

Secondary structure and membrane interaction of PR-39, a Pro+Arg-rich antibacterial peptide.

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The lysosomal cysteine proteases

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7 January 2021

Naturally Occurring Organohalogen Compounds†

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A novel post-translational modification involving bromination of tryptophan. Identification of the residue, L-6-bromotryptophan, in peptides from Conus imperialis and Conus radiatus venom

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7 January 2021

Bromocontryphan: post-translational bromination of tryptophan

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Morulin Pm: a modified polypeptide containing TOPA and 6-bromotryptophan from the morula cells of the ascidian, Phallusia mammillata.

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Styelin D, an extensively modified antimicrobial peptide from ascidian hemocytes

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Structure-activity studies on magainins and other host defense peptides

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7 January 2021

Development of protegrins for the treatment and prevention of oral mucositis: structure-activity relationships of synthetic protegrin analogues

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7 January 2021

Mimicry of bioactive peptides via non-natural, sequence-specific peptidomimetic oligomers

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7 January 2021

Prophenin-1, an exceptionally proline-rich antimicrobial peptide from porcine leukocytes.

1 reference

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7 January 2021

Interaction of hagfish cathelicidin antimicrobial peptides with model lipid membranes

1 reference

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7 January 2021

10.1016/S0045-2068(03)00080-4

Identifiers

DOI

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9 August 2017

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