User:IONTRANSP

References[edit]

{{Cite journal | last1 = Feske | first1 = S. | title = CRAC channelopathies | doi = 10.1007/s00424-009-0777-5 | journal = Pflügers Archiv - European Journal of Physiology | volume = 460 | issue = 2 | pages = 417–435 | year = 2010 | pmid = 20111871 | pmc =2885504 }}Feske, S. (2010). "CRAC channelopathies". Pflügers Archiv - European Journal of Physiology. 460 (2): 417–435. doi:10.1007/s00424-009-0777-5. PMC 2885504. PMID 20111871.

Parkinson disease[edit]

LRRK2 G2019S accounts for parkinsonism in several families^[1]

There is a functional interaction between LRRK2 and ADP-ribosylation factor GTPase-activating protein 1 (ArfGAP1)^[2]

Unlike other known genetic causes of parkinsonism, G2019S LRRK2 mutation causes late onset disease^[3]

G2019S LRRK2 mutation is associated with Lewy body formation which is also characteristic of most cases of Parkinson disease^[4]

PARK8-causing mutations in LRRK2. Some of the first identified individuals with these mutation were of Basque descent so the protein was called "dardarin" after the Basque word ("dardara") for "tremor".^[5]

COR domain mutation analysis for LRRK2.^[6]

LRRK2 dimerization ^[7]

References[edit]

^ Kachergus, J.; Mata, I. F.; Hulihan, M.; Taylor, J. P.; Lincoln, S.; Aasly, J.; Gibson, J. M.; Ross, O. A.; Lynch, T.; Wiley, J.; Payami, H.; Nutt, J.; Maraganore, D. M.; Czyzewski, K.; Styczynska, M.; Wszolek, Z. K.; Farrer, M. J.; Toft, M. (2005). "Identification of a Novel LRRK2 Mutation Linked to Autosomal Dominant Parkinsonism: Evidence of a Common Founder across European Populations". The American Journal of Human Genetics. 76 (4): 672–680. doi:10.1086/429256. PMC 1199304. PMID 15726496.
^ Stafa, K.; Trancikova, A.; Webber, P. J.; Glauser, L.; West, A. B.; Moore, D. J. (2012). Orr, Harry T (ed.). "GTPase Activity and Neuronal Toxicity of Parkinson's Disease–Associated LRRK2 is Regulated by ArfGAP1". PLoS Genetics. 8 (2): e1002526. doi:10.1371/journal.pgen.1002526. PMC 3280333. PMID 22363216.{{cite journal}}: CS1 maint: unflagged free DOI (link)
^ Kett, L. R.; Dauer, W. T. (2012). "Leucine-rich repeat kinase 2 for beginners: Six key questions". Cold Spring Harbor perspectives in medicine. 2 (3): a009407. doi:10.1101/cshperspect.a009407. PMC 3282500. PMID 22393539.
^ Cookson, M. R.; Hardy, J.; Lewis, P. A. (2008). "Genetic neuropathology of Parkinson's disease". International journal of clinical and experimental pathology. 1 (3): 217–231. PMC 2480564. PMID 18784814.
^ Paisán-Ruı́z, C.; Jain, S.; Evans, E. W.; Gilks, W. P.; Simón, J.; Van Der Brug, M.; López De Munain, A. L. P.; Aparicio, S.; Gil, A. M. ́N.; Khan, N.; Johnson, J.; Martinez, J. R.; Nicholl, D.; Carrera, I. M.; Pena, A. S. N.; De Silva, R.; Lees, A.; Martí-Massó, J. F. L.; Pérez-Tur, J.; Wood, N. W.; Singleton, A. B. (2004). "Cloning of the Gene Containing Mutations that Cause PARK8-Linked Parkinson's Disease". Neuron. 44 (4): 595–600. doi:10.1016/j.neuron.2004.10.023. PMID 15541308.
^ Daniëls, V.; Vancraenenbroeck, R. E.; Law, B. M. H.; Greggio, E.; Lobbestael, E.; Gao, F.; De Maeyer, M.; Cookson, M. R.; Harvey, K.; Baekelandt, V.; Taymans, J. M. (2011). "Insight into the mode of action of the LRRK2 Y1699C pathogenic mutant". Journal of Neurochemistry. 116 (2): 304–315. doi:10.1111/j.1471-4159.2010.07105.x. PMC 3005098. PMID 21073465.
^ Civiero, L.; Vancraenenbroeck, R. E.; Belluzzi, E.; Beilina, A.; Lobbestael, E.; Reyniers, L.; Gao, F.; Micetic, I.; De Maeyer, M.; Bubacco, L.; Baekelandt, V.; Cookson, M. R.; Greggio, E.; Taymans, J. M. (2012). Yue, Zhenyu (ed.). "Biochemical Characterization of Highly Purified Leucine-Rich Repeat Kinases 1 and 2 Demonstrates Formation of Homodimers". PLoS ONE. 7 (8): e43472. doi:10.1371/journal.pone.0043472. PMC 3430690. PMID 22952686.{{cite journal}}: CS1 maint: unflagged free DOI (link)

Databases[edit]

Orientations of Proteins in Membranes database

Images[edit]

[pmid15726496-1] Kachergus, J.; Mata, I. F.; Hulihan, M.; Taylor, J. P.; Lincoln, S.; Aasly, J.; Gibson, J. M.; Ross, O. A.; Lynch, T.; Wiley, J.; Payami, H.; Nutt, J.; Maraganore, D. M.; Czyzewski, K.; Styczynska, M.; Wszolek, Z. K.; Farrer, M. J.; Toft, M. (2005). "Identification of a Novel LRRK2 Mutation Linked to Autosomal Dominant Parkinsonism: Evidence of a Common Founder across European Populations". The American Journal of Human Genetics. 76 (4): 672–680. doi:10.1086/429256. PMC 1199304. PMID 15726496.

[pmid22363216-2] Stafa, K.; Trancikova, A.; Webber, P. J.; Glauser, L.; West, A. B.; Moore, D. J. (2012). Orr, Harry T (ed.). "GTPase Activity and Neuronal Toxicity of Parkinson's Disease–Associated LRRK2 is Regulated by ArfGAP1". PLoS Genetics. 8 (2): e1002526. doi:10.1371/journal.pgen.1002526. PMC 3280333. PMID 22363216.{{cite journal}}: CS1 maint: unflagged free DOI (link)

[pmid22393539-3] Kett, L. R.; Dauer, W. T. (2012). "Leucine-rich repeat kinase 2 for beginners: Six key questions". Cold Spring Harbor perspectives in medicine. 2 (3): a009407. doi:10.1101/cshperspect.a009407. PMC 3282500. PMID 22393539.

[pmid18784814-4] Cookson, M. R.; Hardy, J.; Lewis, P. A. (2008). "Genetic neuropathology of Parkinson's disease". International journal of clinical and experimental pathology. 1 (3): 217–231. PMC 2480564. PMID 18784814.

[pmid15541308-5] Paisán-Ruı́z, C.; Jain, S.; Evans, E. W.; Gilks, W. P.; Simón, J.; Van Der Brug, M.; López De Munain, A. L. P.; Aparicio, S.; Gil, A. M. ́N.; Khan, N.; Johnson, J.; Martinez, J. R.; Nicholl, D.; Carrera, I. M.; Pena, A. S. N.; De Silva, R.; Lees, A.; Martí-Massó, J. F. L.; Pérez-Tur, J.; Wood, N. W.; Singleton, A. B. (2004). "Cloning of the Gene Containing Mutations that Cause PARK8-Linked Parkinson's Disease". Neuron. 44 (4): 595–600. doi:10.1016/j.neuron.2004.10.023. PMID 15541308.

[pmid21073465-6] Daniëls, V.; Vancraenenbroeck, R. E.; Law, B. M. H.; Greggio, E.; Lobbestael, E.; Gao, F.; De Maeyer, M.; Cookson, M. R.; Harvey, K.; Baekelandt, V.; Taymans, J. M. (2011). "Insight into the mode of action of the LRRK2 Y1699C pathogenic mutant". Journal of Neurochemistry. 116 (2): 304–315. doi:10.1111/j.1471-4159.2010.07105.x. PMC 3005098. PMID 21073465.

[pmid22952686-7] Civiero, L.; Vancraenenbroeck, R. E.; Belluzzi, E.; Beilina, A.; Lobbestael, E.; Reyniers, L.; Gao, F.; Micetic, I.; De Maeyer, M.; Bubacco, L.; Baekelandt, V.; Cookson, M. R.; Greggio, E.; Taymans, J. M. (2012). Yue, Zhenyu (ed.). "Biochemical Characterization of Highly Purified Leucine-Rich Repeat Kinases 1 and 2 Demonstrates Formation of Homodimers". PLoS ONE. 7 (8): e43472. doi:10.1371/journal.pone.0043472. PMC 3430690. PMID 22952686.{{cite journal}}: CS1 maint: unflagged free DOI (link)

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[2]

[3]

[4]

[5]

[6]

[7]

v t e Proteins: carrier proteins
Fatty acid	FABP1 FABP2 FABP3 FABP4 FABP5 FABP6 FABP7
Hormone	peptide hormone: Follistatin Growth hormone binding protein Insulin-like growth factor binding protein IGFBP1 IGFBP2 IGFBP3 IGFBP4 IGFBP5 IGFBP6 IGFBP7 Neurophysins Neurophysin I II steroid hormone: Sex hormone binding globulin/Androgen binding protein Transcortin Thyroxine-binding globulin Transthyretin
Metal/element	calcium Calcium-binding protein Calmodulin-binding proteins copper Ceruloplasmin iron Iron-binding proteins Transferrin receptor
Vitamin	Retinol binding protein 1 2 3 4 Transcobalamin
Pigment	Plant Light-Harvesting Complex Orange Carotenoid Protein Phycobiliprotein Photosynthetic Reaction Centers Phytochrome Rhodopsin
Other	Acyl carrier protein Adaptor protein Cholesterylester transfer protein F-box protein GTP-binding protein Latent TGF-beta binding protein Major urinary proteins Membrane transport protein Odorant binding protein

v t e Membrane transport protein: neurotransmitter transporters (TC 2.A.1.2)
Vesicular	Vesicular monoamine VMAT1 VMAT2 Vesicular acetylcholine Vesicular glutamate Vesicular GABA
Other	Monoamine DAT NET SERT PMAT Excitatory amino-acid transporter GABA transporter

v t e Membrane proteins, carrier proteins: membrane transport proteins ABC transporter (TC 3A1)
A	A1 A2 A3 A4 A7 A8 A12 A13
B	B1 B2-3 (B2 B3) B4 B5 B6 B7 B9 B11
C	C1 C2 C3 C4 C5 C6 C7 C8-9 (C8, C9) C10 C11 C13
D	D1 D2 D3 D4
E	E1
F	F1 F2
G	G1 G2 G4 Sterolin (G5, G8)
see also ABC transporter disorders

v t e Carrier proteins, metalloproteins: Non-heme iron protein
heme	Ferritin Bacterioferritin Lactoferrin Transferrin
nonheme	Hemerythrin Inositol oxygenase Iron–sulfur protein Lipoxygenase Tyrosine hydroxylase

v t e Acute-phase proteins
Amyloid	SAP SAA
Other positive	Alpha 1-antichymotrypsin Alpha 1-antitrypsin Alpha 2-macroglobulin C-reactive protein Ceruloplasmin C3 Ferritin Fibrin Haptoglobin Haptoglobin-related protein Hemopexin Orosomucoid
Negative	Serum albumin Transferrin

User:IONTRANSP

Chloride channel[edit]

Sodium–hydrogen antiporter 3[edit]

Voltage-gated proton channel[edit]

voltage-sensor containing phosphatase[edit]

References[edit]

Parkinson disease[edit]

References[edit]

Databases[edit]

Images[edit]