Results 11 to 20 of about 5,262 (204)
The Mitochondrial Routing of the Kv1.3 Channel
Frontiers in Oncology, 2022 Voltage-gated potassium channels control neuronal excitability and cardiac action potentials. In addition, these proteins are involved in a myriad of cellular processes.
Jesusa Capera +5 more
doaj +6 more sources
Tyrosine phosphorylation of the Kv1.3 potassium channel [PDF]
The Journal of Neuroscience, 1996 Kv1.3, a voltage-dependent potassium channel cloned from mammalian brain and T lymphocytes, contains multiple tyrosine residues that are putative targets for tyrosine kinases. We have examined the tyrosine phosphorylation of Kv1.3, expressed transiently in human embryonic kidney (or HEK) 293 cells, by endogenous and coexpressed tyrosine kinases ...
T C, Holmes, D A, Fadool, I B, Levitan
openaire +3 more sources
Kv1.3 modulates neuroinflammation and neurodegeneration in Parkinson’s disease [PDF]
Journal of Clinical Investigation, 2020 Characterization of the key cellular targets contributing to sustained microglial activation in neurodegenerative diseases, including Parkinson's disease (PD), and optimal modulation of these targets can provide potential treatments to halt disease progression.
Souvarish Sarkar +23 more
openaire +5 more sources
KCNE4-dependent modulation of Kv1.3 pharmacology [PDF]
Biochemical PharmacologyThe voltage-dependent potassium channel Kv1.3 is a promising therapeutic target for the treatment of autoimmune and chronic inflammatory disorders. Kv1.3 blockers are effective in treating multiple sclerosis (fampridine) and psoriasis (dalazatide).
Daniel Sastre +5 more
openaire +5 more sources
Protein kinase-dependent Kv1.3 biology [PDF]
, 2023 [eng] The voltage gated potassium channel Kv1.3 is a transmembrane protein that selectively drives potassium ions participating in the electrochemical gradient of cell membranes. This channel presents a wide distribution within the body, thereby playing an important role in several physiological processes, such as regulating the cell volume ...
Estadella Pérez, Irene
core +10 more sources
Cell Death and Disease, 2021 Cellular energy metabolism is fundamental for all biological functions. Cellular proliferation requires extensive metabolic reprogramming and has a high energy demand. The Kv1.3 voltage-gated potassium channel drives cellular proliferation.
Faye L. Styles +11 more
doaj +2 more sources
Kv1.5 Association Modifies Kv1.3 Traffic and Membrane Localization [PDF]
Journal of Biological Chemistry, 2008 Kv1.3 activity is determined by raft association. In addition to Kv1.3, leukocytes also express Kv1.5, and both channels control physiological responses. Because the oligomeric composition may modify the channel targeting to the membrane, we investigated heterotetrameric Kv1.3/Kv1.5 channel traffic and targeting in HEK cells.
Vicente García, Rubén, 1978- +7 more
openaire +5 more sources
Mitochondria-Targeting Moieties Based on N-Tethered Pyridinium Cations. [PDF]
Angew Chem Int Ed EnglPyridinium cations were benchmarked as mitochondria‐targeting moieties in a panel of N‐tethered fluorescent‐, bioactive‐, and inert‐cargo conjugates. 3,5‐Diphenylpyridinium (DPPy+) is a competent triphenylphosphonium (TPP+) surrogate, combining high mitochondria‐targeting efficiency with lower intrinsic effects on mitochondrial function.
Džajić I +27 more
europepmc +3 more sources
K+ Channels in Membrane Potential Dynamics and Migration of Neutrophil Granulocytes [PDF]
Arch Pharm (Weinheim)Neutrophil membrane potential dynamics regulate directed migration. Kir2.1 regulates neutrophil membrane potential and indirectly LTB4 secretion. Together with KCa3.1 and KV1.3, it is required for efficient chemotaxis. KCa3.1 and KV1.3 influence neutrophil migration without altering membrane potential, potentially through reduced LTB4 release (KCa3.1 ...
Ulu T +7 more
europepmc +2 more sources
Rearrangement of a unique Kv1.3 selectivity filter conformation upon binding of a drug [PDF]
, 2022 We report two structures of the human voltage-gated potassium channel (Kv) Kv1.3 in immune cells alone (apo-Kv1.3) and bound to an immunomodulatory drug called dalazatide (dalazatide–Kv1.3).
Vorobyov, Igor +33 more
core +1 more source