Details for: CAMP
Associated with
Other Information
Genular Protein ID: 544523925
Symbol: CAMP_HUMAN
Name: N/A
UniProtKB Accession Codes:
Database IDs:
Citations:
PubMed ID: 7529412
Title: FALL-39, a putative human peptide antibiotic, is cysteine-free and expressed in bone marrow and testis.
PubMed ID: 7529412
PubMed ID: 7615076
Title: hCAP-18, a cathelin/pro-bactenecin-like protein of human neutrophil specific granules.
PubMed ID: 7615076
PubMed ID: 7890387
Title: Human CAP18: a novel antimicrobial lipopolysaccharide-binding protein.
PubMed ID: 7890387
PubMed ID: 8946956
Title: Structural, functional analysis and localization of the human CAP18 gene.
PubMed ID: 8946956
PubMed ID: 8681941
Title: The human gene FALL39 and processing of the cathelin precursor to the antibacterial peptide LL-37 in granulocytes.
PubMed ID: 8681941
PubMed ID: 11238224
Title: Rhesus monkey (Macaca mulatta) mucosal antimicrobial peptides are close homologues of human molecules.
PubMed ID: 11238224
PubMed ID: 15489334
Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
PubMed ID: 15489334
DOI: 10.1101/gr.2596504
PubMed ID: 9736536
Title: Activities of LL-37, a cathelin-associated antimicrobial peptide of human neutrophils.
PubMed ID: 9736536
PubMed ID: 10417311
Title: Structure and organization of the human antimicrobial peptide LL-37 in phospholipid membranes: relevance to the molecular basis for its non-cell-selective activity.
PubMed ID: 10417311
DOI: 10.1042/bj3410501
PubMed ID: 11389039
Title: Human cathelicidin, hCAP-18, is processed to the antimicrobial peptide LL-37 by extracellular cleavage with proteinase 3.
PubMed ID: 11389039
PubMed ID: 14978112
Title: Postsecretory processing generates multiple cathelicidins for enhanced topical antimicrobial defense.
PubMed ID: 14978112
PubMed ID: 15778390
Title: Structure-function relationships among human cathelicidin peptides: dissociation of antimicrobial properties from host immunostimulatory activities.
PubMed ID: 15778390
PubMed ID: 21463582
Title: Transmembrane pores formed by human antimicrobial peptide LL-37.
PubMed ID: 21463582
PubMed ID: 22879591
Title: Cathepsin G-regulated release of formyl peptide receptor agonists modulate neutrophil effector functions.
PubMed ID: 22879591
PubMed ID: 34708076
Title: Quorum Sensing Pseudomonas Quinolone Signal Forms Chiral Supramolecular Assemblies With the Host Defense Peptide LL-37.
PubMed ID: 34708076
PubMed ID: 16637646
Title: Solution structures of human LL-37 fragments and NMR-based identification of a minimal membrane-targeting antimicrobial and anticancer region.
PubMed ID: 16637646
DOI: 10.1021/ja0584875
PubMed ID: 18818205
Title: Structures of human host defense cathelicidin LL-37 and its smallest antimicrobial peptide KR-12 in lipid micelles.
PubMed ID: 18818205
PubMed ID: 22185690
Title: 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.
PubMed ID: 22185690
DOI: 10.1021/bi2016266
PubMed ID: 23406372
Title: Structural and functional analysis of the pro-domain of human cathelicidin, LL-37.
PubMed ID: 23406372
DOI: 10.1021/bi301008r
PubMed ID: 29087182
Title: Conformational Aspects of High Content Packing of Antimicrobial Peptides in Polymer Microgels.
PubMed ID: 29087182
PubMed ID: 29133814
Title: Structural remodeling and oligomerization of human cathelicidin on membranes suggest fibril-like structures as active species.
PubMed ID: 29133814
PubMed ID: 29317506
Title: The interplay between citrullination and HLA-DRB1 polymorphism in shaping peptide binding hierarchies in rheumatoid arthritis.
PubMed ID: 29317506
PubMed ID: 32753597
Title: The Human LL-37(17-29) antimicrobial peptide reveals a functional supramolecular structure.
PubMed ID: 32753597
PubMed ID: 33060695
Title: The structure of the antimicrobial human cathelicidin LL-37 shows oligomerization and channel formation in the presence of membrane mimics.
PubMed ID: 33060695
PubMed ID: 35061360
Title: Rare by Natural Selection: Disulfide-Bonded Supramolecular Antimicrobial Peptides.
PubMed ID: 35061360
Sequence Information:
- Length: 170
- Mass: 19301
- Checksum: 055B07DCA95A7D16
- Sequence:
MKTQRDGHSL GRWSLVLLLL GLVMPLAIIA QVLSYKEAVL RAIDGINQRS SDANLYRLLD LDPRPTMDGD PDTPKPVSFT VKETVCPRTT QQSPEDCDFK KDGLVKRCMG TVTLNQARGS FDISCDKDNK RFALLGDFFR KSKEKIGKEF KRIVQRIKDF LRNLVPRTES
Genular Protein ID: 261572625
Symbol: J3KNB4_HUMAN
Name: N/A
UniProtKB Accession Codes:
Database IDs:
Citations:
PubMed ID: 11181995
PubMed ID: 16641997
Title: The DNA sequence, annotation and analysis of human chromosome 3.
PubMed ID: 16641997
DOI: 10.1038/nature04728
Sequence Information:
- Length: 173
- Mass: 19591
- Checksum: 5D1D86D6A0038858
- Sequence:
MGTMKTQRDG HSLGRWSLVL LLLGLVMPLA IIAQVLSYKE AVLRAIDGIN QRSSDANLYR LLDLDPRPTM DGDPDTPKPV SFTVKETVCP RTTQQSPEDC DFKKDGLVKR CMGTVTLNQA RGSFDISCDK DNKRFALLGD FFRKSKEKIG KEFKRIVQRI KDFLRNLVPR TES
Database document:
This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.