CLC (gene): Difference between revisions

Jump to navigation Jump to search
m (Bot: HTTP→HTTPS)
imported>Prosthetic Head
(Added free to read link in citations with OAbot #oabot)
 
Line 32: Line 32:
*{{cite journal  | author=Ackerman SJ |title=Molecular cloning and characterization of human eosinophil Charcot-Leyden crystal protein (lysophospholipase). Similarities to IgE binding proteins and the S-type animal lectin superfamily |journal=J. Immunol. |volume=150 |issue= 2 |pages= 456–68 |year= 1993 |pmid= 8419478 |doi=  |name-list-format=vanc| author2=Corrette SE  | author3=Rosenberg HF  | display-authors=3  | last4=Bennett  | first4=JC  | last5=Mastrianni  | first5=DM  | last6=Nicholson-Weller  | first6=A  | last7=Weller  | first7=PF  | last8=Chin  | first8=DT  | last9=Tenen  | first9=DG  }}
*{{cite journal  | author=Ackerman SJ |title=Molecular cloning and characterization of human eosinophil Charcot-Leyden crystal protein (lysophospholipase). Similarities to IgE binding proteins and the S-type animal lectin superfamily |journal=J. Immunol. |volume=150 |issue= 2 |pages= 456–68 |year= 1993 |pmid= 8419478 |doi=  |name-list-format=vanc| author2=Corrette SE  | author3=Rosenberg HF  | display-authors=3  | last4=Bennett  | first4=JC  | last5=Mastrianni  | first5=DM  | last6=Nicholson-Weller  | first6=A  | last7=Weller  | first7=PF  | last8=Chin  | first8=DT  | last9=Tenen  | first9=DG  }}
*{{cite journal  | author=Leonidas DD |title=Crystal structure of human Charcot-Leyden crystal protein, an eosinophil lysophospholipase, identifies it as a new member of the carbohydrate-binding family of galectins |journal=Structure |volume=3 |issue= 12 |pages= 1379–93 |year= 1996 |pmid= 8747464 |doi=10.1016/S0969-2126(01)00275-1  |name-list-format=vanc| author2=Elbert BL  | author3=Zhou Z  | display-authors=3  | last4=Leffler  | first4=Hakon  | last5=Ackerman  | first5=Steven J  | last6=Acharya  | first6=K.Ravi  }}
*{{cite journal  | author=Leonidas DD |title=Crystal structure of human Charcot-Leyden crystal protein, an eosinophil lysophospholipase, identifies it as a new member of the carbohydrate-binding family of galectins |journal=Structure |volume=3 |issue= 12 |pages= 1379–93 |year= 1996 |pmid= 8747464 |doi=10.1016/S0969-2126(01)00275-1  |name-list-format=vanc| author2=Elbert BL  | author3=Zhou Z  | display-authors=3  | last4=Leffler  | first4=Hakon  | last5=Ackerman  | first5=Steven J  | last6=Acharya  | first6=K.Ravi  }}
*{{cite journal  | vauthors=Dyer KD, Handen JS, Rosenberg HF |title=The genomic structure of the human Charcot-Leyden crystal protein gene is analogous to those of the galectin genes |journal=Genomics |volume=40 |issue= 2 |pages= 217–21 |year= 1997 |pmid= 9119387 |doi= 10.1006/geno.1996.4590 }}
*{{cite journal  | vauthors=Dyer KD, Handen JS, Rosenberg HF |title=The genomic structure of the human Charcot-Leyden crystal protein gene is analogous to those of the galectin genes |journal=Genomics |volume=40 |issue= 2 |pages= 217–21 |year= 1997 |pmid= 9119387 |doi= 10.1006/geno.1996.4590 |url=https://zenodo.org/record/1229719/files/article.pdf }}
*{{cite journal  | author=Swaminathan GJ |title=Selective recognition of mannose by the human eosinophil Charcot-Leyden crystal protein (galectin-10): a crystallographic study at 1.8 A resolution |journal=Biochemistry |volume=38 |issue= 42 |pages= 13837–43 |year= 1999 |pmid= 10529229 |doi=10.1021/bi990756e  |name-list-format=vanc| author2=Leonidas DD  | author3=Savage MP  | display-authors=3  | last4=Ackerman  | first4=Steven J.  | last5=Acharya  | first5=K. Ravi  }}
*{{cite journal  | author=Swaminathan GJ |title=Selective recognition of mannose by the human eosinophil Charcot-Leyden crystal protein (galectin-10): a crystallographic study at 1.8 A resolution |journal=Biochemistry |volume=38 |issue= 42 |pages= 13837–43 |year= 1999 |pmid= 10529229 |doi=10.1021/bi990756e  |name-list-format=vanc| author2=Leonidas DD  | author3=Savage MP  | display-authors=3  | last4=Ackerman  | first4=Steven J.  | last5=Acharya  | first5=K. Ravi  }}
*{{cite journal  | author=Larramendy ML |title=Overexpression of translocation-associated fusion genes of FGFRI, MYC, NPMI, and DEK, but absence of the translocations in acute myeloid leukemia. A microarray analysis |journal=Haematologica |volume=87 |issue= 6 |pages= 569–77 |year= 2003 |pmid= 12031912 |doi=  |name-list-format=vanc| author2=Niini T  | author3=Elonen E  | display-authors=3  | last4=Nagy  | first4=B  | last5=Ollila  | first5=J  | last6=Vihinen  | first6=M  | last7=Knuutila  | first7=S  }}
*{{cite journal  | author=Larramendy ML |title=Overexpression of translocation-associated fusion genes of FGFRI, MYC, NPMI, and DEK, but absence of the translocations in acute myeloid leukemia. A microarray analysis |journal=Haematologica |volume=87 |issue= 6 |pages= 569–77 |year= 2003 |pmid= 12031912 |doi=  |name-list-format=vanc| author2=Niini T  | author3=Elonen E  | display-authors=3  | last4=Nagy  | first4=B  | last5=Ollila  | first5=J  | last6=Vihinen  | first6=M  | last7=Knuutila  | first7=S  }}

Latest revision as of 08:44, 25 October 2018

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Eosinophil lysophospholipase is an enzyme that in humans is encoded by the CLC gene.[1][2]

Lysophospholipases are enzymes that act on biological membranes to regulate the multifunctional lysophospholipids. The protein encoded by this gene is a lysophospholipase expressed in eosinophils and basophils. It hydrolyzes lysophosphatidylcholine to glycerophosphocholine and a free fatty acid. This protein may possess carbohydrate or IgE-binding activities. It is both structurally and functionally related to the galectin family of beta-galactoside binding proteins. It may be associated with inflammation and some myeloid leukemias.[2]

See also

References

  1. Mastrianni DM, Eddy RL, Rosenberg HF, Corrette SE, Shows TB, Tenen DG, Ackerman SJ (Jun 1992). "Localization of the human eosinophil Charcot-Leyden crystal protein (lysophospholipase) gene (CLC) to chromosome 19 and the human ribonuclease 2 (eosinophil-derived neurotoxin) and ribonuclease 3 (eosinophil cationic protein) genes (RNS2 and RNS3) to chromosome 14". Genomics. 13 (1): 240–2. doi:10.1016/0888-7543(92)90237-M. PMID 1577491.
  2. 2.0 2.1 "Entrez Gene: CLC Charcot-Leyden crystal protein".

External links

Further reading