MeSH Browser

MeSH Heading: Cathelicidins
Tree Number(s): D12.644.050.099; D12.644.066.500.099; D12.776.543.695.054.099
Unique ID: D054804
RDF Unique Identifier: http://id.nlm.nih.gov/mesh/D054804
Scope Note: Antimicrobial cationic peptides with a highly conserved amino terminal cathelin-like domain and a more variable carboxy terminal domain. They are initially synthesized as preproproteins and then cleaved. They are expressed in many tissues of humans and localized to EPITHELIAL CELLS. They kill nonviral pathogens by forming pores in membranes.
Entry Term(s): ALL-38 Peptide; Antibacterial Peptide LL-37; Antimicrobial Peptide LL-37; Bac4 Protein, Bos taurus; CAP-18; CAP18; CAP18 Lipopolysaccharide-Binding Protein; CATH-1 Protein; Cathelicidin; Cathelicidin 1; Cathelicidin Antimicrobial Peptide; Cathelicidin LL-37; Cathelicidin-1; Cathelin-Like Protein; Cathelin-Related Antimicrobial Peptide; FA-LL-37; K9CATH; LL-37 Antibacterial Peptide; LL-37 Peptide; Myeloid Cathelicidin 1 Protein, Equus caballus; Ropocamptide; eCATH-1; eCATH-1 protein, Equus caballus; hCAP-18
Related Numbers: 143108-26-3
Public MeSH Note: 2023; ROPOCAMPTIDE was indexed under ANTIMICROBIAL CATIONIC PEPTIDES 2008-2022
History Note: 2023 (2008)
Date Established: 2008/01/01
Date of Entry: 2007/07/09
Revision Date: 2022/07/14

Allowable Qualifiers: administration & dosage (AD)

adverse effects (AE)

agonists (AG)

analysis (AN)

antagonists & inhibitors (AI)

biosynthesis (BI)

blood (BL)

cerebrospinal fluid (CF)

chemical synthesis (CS)

chemistry (CH)

classification (CL)

deficiency (DF)

drug effects (DE)

economics (EC)

genetics (GE)

history (HI)

immunology (IM)

isolation & purification (IP)

metabolism (ME)

pharmacokinetics (PK)

pharmacology (PD)

physiology (PH)

poisoning (PO)

radiation effects (RE)

standards (ST)

supply & distribution (SD)

therapeutic use (TU)

toxicity (TO)

urine (UR)

Concept UI: M0507778
Related Numbers: 143108-26-3
Scope Note: Antimicrobial cationic peptides with a highly conserved amino terminal cathelin-like domain and a more variable carboxy terminal domain. They are initially synthesized as preproproteins and then cleaved. They are expressed in many tissues of humans and localized to EPITHELIAL CELLS. They kill nonviral pathogens by forming pores in membranes.
Terms: Cathelicidins Preferred Term
Term UI T693823
Date03/16/2007
LexicalTag NON
ThesaurusID NLM (2008); Cathelicidin Antimicrobial Peptide
Term UI T001110494
Date08/23/2021
LexicalTag NON
ThesaurusID NLM (2023); Cathelicidin
Term UI T001110495
Date08/23/2021
LexicalTag NON
ThesaurusID NLM (2023)

Concept UI: M0192257
Terms: CAP-18 Preferred Term
Term UI T222257
Date01/01/1955
LexicalTag NON
ThesaurusID NLM (1991); CAP18 Lipopolysaccharide-Binding Protein
Term UI T001122400
Date07/14/2022
LexicalTag NON
ThesaurusID NLM (2023); FA-LL-37
Term UI T434910
Date02/01/2001
LexicalTag NON
ThesaurusID NLM (2001); Antimicrobial Peptide LL-37
Term UI T001118088
Date02/10/2022
LexicalTag NON
ThesaurusID NLM (2023); Antibacterial Peptide LL-37
Term UI T001118087
Date02/10/2022
LexicalTag NON
ThesaurusID NLM (2023); LL-37 Antibacterial Peptide
Term UI T001118085
Date02/10/2022
LexicalTag NON
ThesaurusID NLM (2023); LL-37 Peptide
Term UI T001118086
Date02/10/2022
LexicalTag NON
ThesaurusID NLM (2023); CAP18
Term UI T222258
Date01/01/1955
LexicalTag NON
ThesaurusID NLM (1991); Cathelicidin LL-37
Term UI T001116658
Date01/05/2022
LexicalTag NON
ThesaurusID NLM (2023); Ropocamptide
Term UI T001116657
Date01/05/2022
LexicalTag NON
ThesaurusID NLM (2023)

Cathelicidins MeSH Descriptor Data 2024