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{{Infobox_gene}}


'''Leucine-rich repeat-containing protein 8E''' is a [[protein]] that in humans is encoded by the ‘’LRRC8E’’ [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: LRRC8A leucine rich repeat containing 8 family, member A| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=56262| accessdate = }}</ref> Researchers have found out that this protein, along with the other LRRC8 proteins [[LRRC8A]], [[LRRC8B]], [[LRRC8C]], and [[LRRC8D]], is sometimes a subunit of the heteromer protein [[VRAC|Volume-Regulated Anion Channel]].<ref name="Voss_2014">{{cite journal | vauthors = Voss FK, Ullrich F, Münch J, Lazarow K, Lutter D, Mah N, Andrade-Navarro MA, von Kries JP, Stauber T, Jentsch TJ | title = Identification of LRRC8 heteromers as an essential component of the volume-regulated anion channel VRAC | journal = Science | volume = 344 | issue = 6184 | pages = 634–8 | date = May 2014 | pmid = 24790029 | doi = 10.1126/science.1252826 }}</ref> Volume-Regulated Anion Channels (VRACs) are crucial to the regulation of cell size by transporting chloride ions and various organic osmolytes, such as taurine or glutamate, across the plasma membrane,<ref name ="Jentsch_2016">{{cite journal | vauthors = Jentsch TJ | title = VRACs and other ion channels and transporters in the regulation of cell volume and beyond | journal = Nature Reviews. Molecular Cell Biology | volume = 17 | issue = 5 | pages = 293–307 | date = May 2016 | pmid = 27033257 | doi = 10.1038/nrm.2016.29 }}</ref> and that is not the only function these channels have been linked to.  
'''Leucine-rich repeat-containing protein 8E''' is a [[protein]] that in humans is encoded by the ''LRRC8E'' [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: LRRC8A leucine rich repeat containing 8 family, member A| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=56262| accessdate = }}</ref> Researchers have found out that this protein, along with the other LRRC8 proteins [[LRRC8A]], [[LRRC8B]], [[LRRC8C]], and [[LRRC8D]], is sometimes a subunit of the heteromer protein [[VRAC|Volume-Regulated Anion Channel]].<ref name="Voss_2014">{{cite journal | vauthors = Voss FK, Ullrich F, Münch J, Lazarow K, Lutter D, Mah N, Andrade-Navarro MA, von Kries JP, Stauber T, Jentsch TJ | title = Identification of LRRC8 heteromers as an essential component of the volume-regulated anion channel VRAC | journal = Science | volume = 344 | issue = 6184 | pages = 634–8 | date = May 2014 | pmid = 24790029 | doi = 10.1126/science.1252826 }}</ref> Volume-Regulated Anion Channels (VRACs) are crucial to the regulation of cell size by transporting chloride ions and various organic osmolytes, such as taurine or glutamate, across the plasma membrane,<ref name ="Jentsch_2016">{{cite journal | vauthors = Jentsch TJ | title = VRACs and other ion channels and transporters in the regulation of cell volume and beyond | journal = Nature Reviews Molecular Cell Biology | volume = 17 | issue = 5 | pages = 293–307 | date = May 2016 | pmid = 27033257 | doi = 10.1038/nrm.2016.29 }}</ref> and that is not the only function these channels have been linked to.


While LRRC8E is one of many proteins that can be part of VRAC, research has found that it is not as crucial to the activity of the channel in comparison to [[LRRC8A]] and [[LRRC8D]].<ref name =" Hyzinski-García_2014">{{cite journal | vauthors = Hyzinski-García MC, Rudkouskaya A, Mongin AA | title = LRRC8A protein is indispensable for swelling-activated and ATP-induced release of excitatory amino acids in rat astrocytes | journal = The Journal of Physiology | volume = 592 | issue = 22 | pages = 4855-62 | date = November 2014 | pmid = 25172945 | pmc = 4259531 | doi = 10.1113/jphysiol.2014.278887 }}</ref><ref name ="Yamada_2016">{{cite journal | vauthors = Yamada T, Wondergem R, Morrison R, Yin VP, Strange K | title = Leucine-rich repeat containing protein LRRC8A is essential for swelling-activated Cl- currents and embryonic development in zebrafish = | journal = Physiological Reports | volume = 4 | issue = 19 | pages = 16–27 | date = October 2016 | pmid = 27688432 | pmc = 5064130 | doi = 10.14814/phy2.12940 | trans-title = [Change of inulin- and chloride-spaces during acute metabolic acidosis in the rat] }}</ref><ref name="Planells-Cases_2015"/> However, while we know that [[LRRC8A]] and [[LRRC8D]] are necessary for VRAC function, other studies have found that they are not sufficient for the full range of usual VRAC activity.<ref name ="Okada_2017">{{cite journal | vauthors = Okada T, Islam MR, Tsiferova NA, Okada Y, Sabirov RZ | title = Specific and essential but not sufficient roles of LRRC8A in the activity of volume-sensitive outwardly rectifying anion channel (VSOR) | journal = Channels | volume = 11 | issue = 2 | pages = 109–120 | date = March 2017 | pmid = 27764579 | doi = 10.1080/19336950.2016.1247133 }}</ref> This is where the other LRRC8 proteins come in, such as LRRC8E, as the different composition of these subunits affects the range of specificity for VRACs.<ref name ="Lutter_2017">{{cite journal | vauthors = Lutter D, Ullrich F, Lueck JC, Kempa S, Jentsch TJ | title = Selective transport of neurotransmitters and modulators by distinct volume-regulated LRRC8 anion channels | journal = Journal of Cell Science | volume = 130 | issue = 6 | pages = 1122–1133 | date = March 2017 | pmid = 28193731 | doi = 10.1242/jcs.196253 }}</ref><ref name="Planells-Cases_2015">{{cite journal | vauthors = Planells-Cases R, Lutter D, Guyader C, Gerhards NM, Ullrich F, Elger DA, Kucukosmanoglu A, Xu G, Voss FK, Reincke SM, Stauber T, Blomen VA, Vis DJ, Wessels LF, Brummelkamp TR, Borst P, Rottenberg S, Jentsch TJ | title = Subunit composition of VRAC channels determines substrate specificity and cellular resistance to Pt-based anti-cancer drugs | journal = The EMBO Journal | volume = 34 | issue = 24 | pages = 2993–3008 | date = December 2015 | pmid = 26530471 | doi = 10.15252/embj.201592409 }}</ref>
While LRRC8E is one of many proteins that can be part of VRAC, research has found that it is not as crucial to the activity of the channel in comparison to [[LRRC8A]] and [[LRRC8D]].<ref name =" Hyzinski-García_2014">{{cite journal | vauthors = Hyzinski-García MC, Rudkouskaya A, Mongin AA | title = LRRC8A protein is indispensable for swelling-activated and ATP-induced release of excitatory amino acids in rat astrocytes | journal = The Journal of Physiology | volume = 592 | issue = 22 | pages = 4855–62 | date = November 2014 | pmid = 25172945 | pmc = 4259531 | doi = 10.1113/jphysiol.2014.278887 }}</ref><ref name ="Yamada_2016">{{cite journal | vauthors = Yamada T, Wondergem R, Morrison R, Yin VP, Strange K | title = Leucine-rich repeat containing protein LRRC8A is essential for swelling-activated Cl- currents and embryonic development in zebrafish = | journal = Physiological Reports | volume = 4 | issue = 19 | pages = 16–27 | date = October 2016 | pmid = 27688432 | pmc = 5064130 | doi = 10.14814/phy2.12940 | trans-title = [Change of inulin- and chloride-spaces during acute metabolic acidosis in the rat] }}</ref><ref name="Planells-Cases_2015"/> However, while we know that [[LRRC8A]] and [[LRRC8D]] are necessary for VRAC function, other studies have found that they are not sufficient for the full range of usual VRAC activity.<ref name ="Okada_2017">{{cite journal | vauthors = Okada T, Islam MR, Tsiferova NA, Okada Y, Sabirov RZ | title = Specific and essential but not sufficient roles of LRRC8A in the activity of volume-sensitive outwardly rectifying anion channel (VSOR) | journal = Channels | volume = 11 | issue = 2 | pages = 109–120 | date = March 2017 | pmid = 27764579 | doi = 10.1080/19336950.2016.1247133 | pmc=5398601}}</ref> This is where the other LRRC8 proteins come in, such as LRRC8E, as the different composition of these subunits affects the range of specificity for VRACs.<ref name ="Lutter_2017">{{cite journal | vauthors = Lutter D, Ullrich F, Lueck JC, Kempa S, Jentsch TJ | title = Selective transport of neurotransmitters and modulators by distinct volume-regulated LRRC8 anion channels | journal = Journal of Cell Science | volume = 130 | issue = 6 | pages = 1122–1133 | date = March 2017 | pmid = 28193731 | doi = 10.1242/jcs.196253 }}</ref><ref name="Planells-Cases_2015">{{cite journal | vauthors = Planells-Cases R, Lutter D, Guyader C, Gerhards NM, Ullrich F, Elger DA, Kucukosmanoglu A, Xu G, Voss FK, Reincke SM, Stauber T, Blomen VA, Vis DJ, Wessels LF, Brummelkamp TR, Borst P, Rottenberg S, Jentsch TJ | title = Subunit composition of VRAC channels determines substrate specificity and cellular resistance to Pt-based anti-cancer drugs | journal = The EMBO Journal | volume = 34 | issue = 24 | pages = 2993–3008 | date = December 2015 | pmid = 26530471 | doi = 10.15252/embj.201592409 | pmc=4687416}}</ref>


In addition to its role in VRACs, the LRRC8 protein family is also associated with [[agammaglobulinemia]]-5.<ref name="Sawada_2003">{{cite journal | vauthors = Sawada A, Takihara Y, Kim JY, Matsuda-Hashii Y, Tokimasa S, Fujisaki H, Kubota K, Endo H, Onodera T, Ohta H, Ozono K, Hara J | title = A congenital mutation of the novel gene LRRC8 causes agammaglobulinemia in humans | journal = The Journal of Clinical Investigation | volume = 112 | issue = 11 | pages = 1707–13 | date = December 2003 | pmid = 14660746 | doi = 10.1172/JCI18937 }}</ref>  
In addition to its role in VRACs, the LRRC8 protein family is also associated with [[agammaglobulinemia]]-5.<ref name="Sawada_2003">{{cite journal | vauthors = Sawada A, Takihara Y, Kim JY, Matsuda-Hashii Y, Tokimasa S, Fujisaki H, Kubota K, Endo H, Onodera T, Ohta H, Ozono K, Hara J | title = A congenital mutation of the novel gene LRRC8 causes agammaglobulinemia in humans | journal = The Journal of Clinical Investigation | volume = 112 | issue = 11 | pages = 1707–13 | date = December 2003 | pmid = 14660746 | doi = 10.1172/JCI18937 | pmc=281644}}</ref>


Specifically for LRRC8E, there has been a recent study that found that this gene was nominally associated with panic disorder.<ref name="Gregersen_2016">{{cite journal | vauthors = Gregersen NO, Buttenschøn HN, Hedemand A, Nielsen MN, Dahl HA, Kristensen AS, Johansen O, Woldbye DP, Erhardt A, Kruse TA, Wang AG, Børglum AD, Mors O | title = Association between genes on chromosome 19p13.2 and panic disorder | journal = Psychiatric Genetics | volume = 26 | issue = 6 | pages = 287–292 | date = December 2016 | pmid = 27610895 | doi = 10.1097/YPG.0000000000000147 }}</ref>  
Specifically for LRRC8E, there has been a recent study that found that this gene was nominally associated with panic disorder.<ref name="Gregersen_2016">{{cite journal | vauthors = Gregersen NO, Buttenschøn HN, Hedemand A, Nielsen MN, Dahl HA, Kristensen AS, Johansen O, Woldbye DP, Erhardt A, Kruse TA, Wang AG, Børglum AD, Mors O | title = Association between genes on chromosome 19p13.2 and panic disorder | journal = Psychiatric Genetics | volume = 26 | issue = 6 | pages = 287–292 | date = December 2016 | pmid = 27610895 | doi = 10.1097/YPG.0000000000000147 }}</ref>


== References ==
== References ==
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* {{cite journal | vauthors = Wiemann S, Arlt D, Huber W, Wellenreuther R, Schleeger S, Mehrle A, Bechtel S, Sauermann M, Korf U, Pepperkok R, Sültmann H, Poustka A | title = From ORFeome to biology: a functional genomics pipeline | journal = Genome Research | volume = 14 | issue = 10B | pages = 2136–44 | date = October 2004 | pmid = 15489336 | pmc = 528930 | doi = 10.1101/gr.2576704 }}
* {{cite journal | vauthors = Wiemann S, Arlt D, Huber W, Wellenreuther R, Schleeger S, Mehrle A, Bechtel S, Sauermann M, Korf U, Pepperkok R, Sültmann H, Poustka A | title = From ORFeome to biology: a functional genomics pipeline | journal = Genome Research | volume = 14 | issue = 10B | pages = 2136–44 | date = October 2004 | pmid = 15489336 | pmc = 528930 | doi = 10.1101/gr.2576704 }}
* {{cite journal | vauthors = Hartley JL, Temple GF, Brasch MA | title = DNA cloning using in vitro site-specific recombination | journal = Genome Research | volume = 10 | issue = 11 | pages = 1788–95 | date = November 2000 | pmid = 11076863 | pmc = 310948 | doi = 10.1101/gr.143000 }}
* {{cite journal | vauthors = Hartley JL, Temple GF, Brasch MA | title = DNA cloning using in vitro site-specific recombination | journal = Genome Research | volume = 10 | issue = 11 | pages = 1788–95 | date = November 2000 | pmid = 11076863 | pmc = 310948 | doi = 10.1101/gr.143000 }}
* {{cite journal | vauthors = Eggermont J, Trouet D, Carton I, Nilius B | title = Cellular function and control of volume-regulated anion channels | journal = Cell Biochemistry and Biophysics | volume = 35 | issue = 3 | pages = 263–74 | year = 2001 | pmid = 11894846 | doi = 10.1385/CBB:35:3:263 }}
* {{cite journal | vauthors = Eggermont J, Trouet D, Carton I, Nilius B | title = Cellular function and control of volume-regulated anion channels | journal = [[Cell Biochemistry and Biophysics]] | volume = 35 | issue = 3 | pages = 263–74 | year = 2001 | pmid = 11894846 | doi = 10.1385/CBB:35:3:263 }}
* {{cite journal | vauthors = Hsu LY, Kim HJ, Sujansky E, Kousseff B, Hirschhorn K | title = Reciprocal translocation versus centric fusion between two No. 13 chromosomes. A case of 46,XX,-13,+t(13;13)(p12;q13) and a case of 46,XY,-13,+t(13;13)(p12;p12) | journal = Cytogenetics and Cell Genetics | volume = 12 | issue = 4 | pages = 235–44 | year = 2016 | pmid = 4752865 | doi = 10.1007/s00424-015-1765-6 }}
* {{cite journal | vauthors = Hsu LY, Kim HJ, Sujansky E, Kousseff B, Hirschhorn K | title = Reciprocal translocation versus centric fusion between two No. 13 chromosomes. A case of 46,XX,-13,+t(13;13)(p12;q13) and a case of 46,XY,-13,+t(13;13)(p12;p12) | journal = Cytogenetics and Cell Genetics | volume = 12 | issue = 4 | pages = 235–44 | year = 2016 | pmid = 4752865 | doi = 10.1007/s00424-015-1765-6 | pmc = 4752865 }}
* {{cite journal | vauthors = Nagase T, Kikuno R, Ishikawa KI, Hirosawa M, Ohara O | title = Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro | journal = DNA Research | volume = 7 | issue = 1 | pages = 65–73 | date = February 2000 | pmid = 10718198 | doi = 10.1093/dnares/7.1.65 }}
* {{cite journal | vauthors = Nagase T, Kikuno R, Ishikawa KI, Hirosawa M, Ohara O | title = Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro | journal = DNA Research | volume = 7 | issue = 1 | pages = 65–73 | date = February 2000 | pmid = 10718198 | doi = 10.1093/dnares/7.1.65 }}
* {{cite journal | vauthors = Kubota K, Kim JY, Sawada A, Tokimasa S, Fujisaki H, Matsuda-Hashii Y, Ozono K, Hara J | title = LRRC8 involved in B cell development belongs to a novel family of leucine-rich repeat proteins | journal = FEBS Letters | volume = 564 | issue = 1-2 | pages = 147–52 | date = April 2004 | pmid = 15094057 | doi = 10.1016/S0014-5793(04)00332-1 }}
* {{cite journal | vauthors = Kubota K, Kim JY, Sawada A, Tokimasa S, Fujisaki H, Matsuda-Hashii Y, Ozono K, Hara J | title = LRRC8 involved in B cell development belongs to a novel family of leucine-rich repeat proteins | journal = FEBS Letters | volume = 564 | issue = 1–2 | pages = 147–52 | date = April 2004 | pmid = 15094057 | doi = 10.1016/S0014-5793(04)00332-1 }}
* {{cite journal | vauthors = Smits G, Kajava AV | title = LRRC8 extracellular domain is composed of 17 leucine-rich repeats | journal = Molecular Immunology | volume = 41 | issue = 5 | pages = 561–2 | date = July 2004 | pmid = 15183935 | doi = 10.1016/j.molimm.2004.04.001 }}
* {{cite journal | vauthors = Smits G, Kajava AV | title = LRRC8 extracellular domain is composed of 17 leucine-rich repeats | journal = Molecular Immunology | volume = 41 | issue = 5 | pages = 561–2 | date = July 2004 | pmid = 15183935 | doi = 10.1016/j.molimm.2004.04.001 }}
* {{cite journal | vauthors = Otsuki T, Ota T, Nishikawa T, Hayashi K, Suzuki Y, Yamamoto J, Wakamatsu A, Kimura K, Sakamoto K, Hatano N, Kawai Y, Ishii S, Saito K, Kojima S, Sugiyama T, Ono T, Okano K, Yoshikawa Y, Aotsuka S, Sasaki N, Hattori A, Okumura K, Nagai K, Sugano S, Isogai T | title = Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries | journal = DNA Research | volume = 12 | issue = 2 | pages = 117–26 | year = 2007 | pmid = 16303743 | doi = 10.1093/dnares/12.2.117 }}
* {{cite journal | vauthors = Otsuki T, Ota T, Nishikawa T, Hayashi K, Suzuki Y, Yamamoto J, Wakamatsu A, Kimura K, Sakamoto K, Hatano N, Kawai Y, Ishii S, Saito K, Kojima S, Sugiyama T, Ono T, Okano K, Yoshikawa Y, Aotsuka S, Sasaki N, Hattori A, Okumura K, Nagai K, Sugano S, Isogai T | title = Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries | journal = DNA Research | volume = 12 | issue = 2 | pages = 117–26 | year = 2007 | pmid = 16303743 | doi = 10.1093/dnares/12.2.117 }}
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{{refend}}
{{refend}}


[[Category:LRR proteins]]


[[Category:LRR proteins]]


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{{gene-19-stub}}

Latest revision as of 05:08, 14 June 2018

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Identifiers
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External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Leucine-rich repeat-containing protein 8E is a protein that in humans is encoded by the LRRC8E gene.[1] Researchers have found out that this protein, along with the other LRRC8 proteins LRRC8A, LRRC8B, LRRC8C, and LRRC8D, is sometimes a subunit of the heteromer protein Volume-Regulated Anion Channel.[2] Volume-Regulated Anion Channels (VRACs) are crucial to the regulation of cell size by transporting chloride ions and various organic osmolytes, such as taurine or glutamate, across the plasma membrane,[3] and that is not the only function these channels have been linked to.

While LRRC8E is one of many proteins that can be part of VRAC, research has found that it is not as crucial to the activity of the channel in comparison to LRRC8A and LRRC8D.[4][5][6] However, while we know that LRRC8A and LRRC8D are necessary for VRAC function, other studies have found that they are not sufficient for the full range of usual VRAC activity.[7] This is where the other LRRC8 proteins come in, such as LRRC8E, as the different composition of these subunits affects the range of specificity for VRACs.[8][6]

In addition to its role in VRACs, the LRRC8 protein family is also associated with agammaglobulinemia-5.[9]

Specifically for LRRC8E, there has been a recent study that found that this gene was nominally associated with panic disorder.[10]

References

  1. ↑ "Entrez Gene: LRRC8A leucine rich repeat containing 8 family, member A".
  2. ↑ Voss FK, Ullrich F, Münch J, Lazarow K, Lutter D, Mah N, Andrade-Navarro MA, von Kries JP, Stauber T, Jentsch TJ (May 2014). "Identification of LRRC8 heteromers as an essential component of the volume-regulated anion channel VRAC". Science. 344 (6184): 634–8. doi:10.1126/science.1252826. PMID 24790029.
  3. ↑ Jentsch TJ (May 2016). "VRACs and other ion channels and transporters in the regulation of cell volume and beyond". Nature Reviews Molecular Cell Biology. 17 (5): 293–307. doi:10.1038/nrm.2016.29. PMID 27033257.
  4. ↑ Hyzinski-García MC, Rudkouskaya A, Mongin AA (November 2014). "LRRC8A protein is indispensable for swelling-activated and ATP-induced release of excitatory amino acids in rat astrocytes". The Journal of Physiology. 592 (22): 4855–62. doi:10.1113/jphysiol.2014.278887. PMC 4259531. PMID 25172945.
  5. ↑ Yamada T, Wondergem R, Morrison R, Yin VP, Strange K (October 2016). "Leucine-rich repeat containing protein LRRC8A is essential for swelling-activated Cl- currents and embryonic development in zebrafish =" [[Change of inulin- and chloride-spaces during acute metabolic acidosis in the rat]]. Physiological Reports. 4 (19): 16–27. doi:10.14814/phy2.12940. PMC 5064130. PMID 27688432.
  6. ↑ 6.0 6.1 Planells-Cases R, Lutter D, Guyader C, Gerhards NM, Ullrich F, Elger DA, Kucukosmanoglu A, Xu G, Voss FK, Reincke SM, Stauber T, Blomen VA, Vis DJ, Wessels LF, Brummelkamp TR, Borst P, Rottenberg S, Jentsch TJ (December 2015). "Subunit composition of VRAC channels determines substrate specificity and cellular resistance to Pt-based anti-cancer drugs". The EMBO Journal. 34 (24): 2993–3008. doi:10.15252/embj.201592409. PMC 4687416. PMID 26530471.
  7. ↑ Okada T, Islam MR, Tsiferova NA, Okada Y, Sabirov RZ (March 2017). "Specific and essential but not sufficient roles of LRRC8A in the activity of volume-sensitive outwardly rectifying anion channel (VSOR)". Channels. 11 (2): 109–120. doi:10.1080/19336950.2016.1247133. PMC 5398601. PMID 27764579.
  8. ↑ Lutter D, Ullrich F, Lueck JC, Kempa S, Jentsch TJ (March 2017). "Selective transport of neurotransmitters and modulators by distinct volume-regulated LRRC8 anion channels". Journal of Cell Science. 130 (6): 1122–1133. doi:10.1242/jcs.196253. PMID 28193731.
  9. ↑ Sawada A, Takihara Y, Kim JY, Matsuda-Hashii Y, Tokimasa S, Fujisaki H, Kubota K, Endo H, Onodera T, Ohta H, Ozono K, Hara J (December 2003). "A congenital mutation of the novel gene LRRC8 causes agammaglobulinemia in humans". The Journal of Clinical Investigation. 112 (11): 1707–13. doi:10.1172/JCI18937. PMC 281644. PMID 14660746.
  10. ↑ Gregersen NO, Buttenschøn HN, Hedemand A, Nielsen MN, Dahl HA, Kristensen AS, Johansen O, Woldbye DP, Erhardt A, Kruse TA, Wang AG, Børglum AD, Mors O (December 2016). "Association between genes on chromosome 19p13.2 and panic disorder". Psychiatric Genetics. 26 (6): 287–292. doi:10.1097/YPG.0000000000000147. PMID 27610895.

Further reading


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