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词条 CALB1
释义

  1. Function

  2. References

  3. Further reading

{{Infobox_gene}}

Calbindin 1 is a protein that in humans is encoded by the CALB1 gene.

[1]

Function

The protein encoded by this gene is a member of the calcium-binding protein superfamily that includes calmodulin and troponin C. Originally described as a 27 kDa protein, it is now known to be a 28 kDa protein. It contains four active calcium-binding domains, and has two modified domains that are thought to have lost their calcium binding capability.[2] This protein is thought to buffer entry of calcium upon stimulation of glutamate receptors. Depletion of this protein was noted in patients with Huntington disease. [provided by RefSeq, Jan 2015].

References

1. ^{{cite web| title = Entrez Gene: Calbindin 1| url = https://www.ncbi.nlm.nih.gov/gene/793| accessdate = 2018-10-04}}
2. ^{{cite journal | vauthors = Noble JW, Almalki R, Roe SM, Wagner A, Duman R, Atack JR | title = The X-ray structure of human calbindin-D28K: an improved model | journal = Acta Crystallographica Section D | volume = 74 | issue = Pt 10 | pages = 1008–1014 | date = October 2018 | pmid = 30289411 | pmc = 6173056 | doi = 10.1107/s2059798318011610 }}

Further reading

{{refbegin | 30em}}
  • {{cite journal |vauthors=Tao L, Murphy ME, English AM |title=S-nitrosation of Ca(2+)-loaded and Ca(2+)-free recombinant calbindin D(28K) from human brain |journal=Biochemistry |volume=41 |issue=19 |pages=6185–92 |date=May 2002 |pmid= |doi= |url=}}
  • {{cite journal |vauthors=Berggard T, Szczepankiewicz O, Thulin E, Linse S |title=Myo-inositol monophosphatase is an activated target of calbindin D28k |journal=J. Biol. Chem. |volume=277 |issue=44 |pages=41954–9 |date=November 2002 |pmid=12176979 |doi=10.1074/jbc.M203492200 |url=}}
  • {{cite journal |vauthors=Belkacemi L, Gariépy G, Mounier C, Simoneau L, Lafond J |title=Expression of calbindin-D28k (CaBP28k) in trophoblasts from human term placenta |journal=Biol. Reprod. |volume=68 |issue=6 |pages=1943–50 |date=June 2003 |pmid=12606474 |doi=10.1095/biolreprod.102.009373 |url=}}
  • {{cite journal |vauthors=Cedervall T, Berggård T, Borek V, Thulin E, Linse S, Akerfeldt KS |title=Redox sensitive cysteine residues in calbindin D28k are structurally and functionally important |journal=Biochemistry |volume=44 |issue=2 |pages=684–93 |date=January 2005 |pmid=15641794 |doi=10.1021/bi049232r |url=}}
  • {{cite journal |vauthors=Vanbelle C, Halgand F, Cedervall T, Thulin E, Akerfeldt KS, Laprévote O, Linse S |title=Deamidation and disulfide bridge formation in human calbindin D28k with effects on calcium binding |journal=Protein Sci. |volume=14 |issue=4 |pages=968–79 |date=April 2005 |pmid=15741335 |pmc=2253450 |doi=10.1110/ps.041157705 |url=}}
  • {{cite journal |vauthors=Valencia I, Legido A, Yelin K, Khurana D, Kothare SV, Katsetos CD |title=Anomalous inhibitory circuits in cortical tubers of human tuberous sclerosis complex associated with refractory epilepsy: aberrant expression of parvalbumin and calbindin-D28k in dysplastic cortex |journal=J. Child Neurol. |volume=21 |issue=12 |pages=1058–63 |date=December 2006 |pmid=17156698 |doi=10.1177/7010.2006.00242 |url=}}
  • {{cite journal |vauthors=Vig PJ, Wei J, Shao Q, Hebert MD, Subramony SH, Sutton LT |title=Role of tissue transglutaminase type 2 in calbindin-D28k interaction with ataxin-1 |journal=Neurosci. Lett. |volume=420 |issue=1 |pages=53–7 |date=June 2007 |pmid=17442486 |pmc=1949022 |doi=10.1016/j.neulet.2007.04.005 |url=}}
  • {{cite journal |vauthors=Zhang C, Sun Y, Wang W, Zhang Y, Ma M, Lou Z |title=Crystallization and preliminary crystallographic analysis of human Ca 2+-loaded calbindin-D28k |journal=Acta Crystallographica Section F |volume=64 |issue=Pt 2 |pages=133–6 |date=February 2008 |pmid=18259068 |pmc=2374171 |doi=10.1107/S1744309108001905 |url=}}
  • {{cite journal |vauthors=Bauer MC, Nilsson H, Thulin E, Frohm B, Malm J, Linse S |title=Zn2+ binding to human calbindin D(28k) and the role of histidine residues |journal=Protein Sci. |volume=17 |issue=4 |pages=760–7 |date=April 2008 |pmid=18359862 |pmc=2271158 |doi=10.1110/ps.073381108 |url=}}
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