User:IONTRANSP

• ANO1 Chloride Channels: Often enigmatic, rarely predictable

• Role of NH3 and NH4+ transporters in renal acid-base transport
• Luminal Na+/H+ exchange in the proximal tubule

• Function of the HVCN1 proton channel in airway epithelia and a naturally occurring mutation, M91T

• Voltage-sensing phosphatase: actions and potentials

{{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.

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]