Toshimitsu Kawate Molecular Medicine, Cornell University, USA, USA,
2 protocols
Alexandros Kokotos Weill Cornell Medicine
18 protocols

Arif Kabir Hokkaido University
4 protocols

Beatrice Li University of Oxford
7 protocols

Carey Huh University of California
4 protocols

Reviewer
Akira Karasawa
  • Staff scientist, New York Structural Biology Center
Research focus
  • Membrane protein biochemistry/biophysics
  • 2 Author merit

Education

PhD in Biology, Osaka University, 2008

Lab information

https://www.comppaa.org/

Publications

https://www.ncbi.nlm.nih.gov/myncbi/1Riz5PBvtfRM9b/bibliography/public/
1. Karasawa, A. and Kawate, T. High-throughput YO-PRO-1 Uptake Assay for P2X7 Receptors Expressed in HEK Cells.
Bio-101: e2943 (2018)

2. Karasawa, A., Michalski, K., Mikhelzon, P., and Kawate, T.
The P2X7 receptor forms a dye-permeable pore independent of its intracellular domain but dependent on membrane lipid composition.
Elife 6, e31186 (2017)

3. Karasawa, A., and Kawate, T.
Expression and Purification of a Mammalian P2X7 Receptor from Sf9 Insect Cells.
Bio-protocol 7, e2544 (2017).

4. Karasawa, A., and Kawate, T.
Structural basis for subtype-specific inhibition of the P2X7 receptor.
Elife 5, e22153 (2016)

5. Karasawa A., Swier L.J., Stuart M.C., Brouwers J., Helms B., Poolman B.
Physicochemical factors controlling the activity and energy coupling of an ionic strength-gated ATP-binding cassette (ABC) transporter.
J. Biol. Chem. 288, 29862-71 (2013)

6. Gul N., Schuurman-Wolters G., Karasawa A., Poolman B.
Functional characterization of amphipathic a-helix in the osmoregulatory ABC transporter OpuA.
Biochemistry. 51, 5142-52 (2012)

7. Karasawa A., Erkens G.B., Berntsson R.P., Otten R., Schuurman-Wolters G.K., Mulder F.A., Poolman B.
Cystathionine b synthase CBS domains 1 and 2 fulfill different roles in ionic strength-sensing of the ABC transporter OpuA.
J. Biol. Chem. 286, 37280-37291, (2011)

8. Wolters J.C., Berntsson R.P., Gul N., Karasawa A, Thunnissen A.M., Slotboom D.J., Poolman B.
Ligand binding and crystal structures of the substrate-binding domain of the ABC transporter OpuA.
PLoS One. 5: e10361 (2010)

9. Karasawa A, Mitsui K., Matsushita M., Kanazawa H.
Intermolecular cross-linking of monomers in H. pylori Na+/H+ antiporter NhaA at dimer interface inhibits antiporter activity.
Biochem J. 426, 99–108 (2010)

10. Karasawa A., Mitsui K., Matsushita M., Kanazawa H.
Functional Assembly of the Na+/H+ Antiporter of Helicobacter pylori from Partial Fragments in vivo.
Biochemistry. 46, 14272-83 (2007)

11. Karasawa A., Tsuboi Y., Inoue H., Kinoshita R., Nakamura N., Kanazawa H.
Detection of oligomerization and conformational changes in the Na+/H+ antiporter from Helicobacter pylori by fluorescence resonance energy transfer.
J. Biol. Chem. 280, 41900-41911, (2005)
2 Protocols published
High-throughput YO-PRO-1 Uptake Assay for P2X7 Receptors Expressed in HEK Cells
Authors:  Akira Karasawa and Toshimitsu Kawate, date: 07/20/2018, view: 6537, Q&A: 0
P2X7 receptors are extracellular ATP-gated ion channels that play broad physiological and pathological roles in animals (Sluyter, 2017). Activation of P2X7 receptors lead to the opening of membrane channels permeable for small cations like Na+ ...
Expression and Purification of a Mammalian P2X7 Receptor from Sf9 Insect Cells
Authors:  Akira Karasawa and Toshimitsu Kawate, date: 09/05/2017, view: 10399, Q&A: 0
The P2X7 receptor is an extracellular ATP-gated ion channel found only in eukaryotes (Bartlett et al., 2014). Due to its unique properties among P2X receptors, such as formation of a large conductance pore, the P2X7 receptor has been ...
10 Protocols reviewed
Isolation of tdTomato Expressing Inter-follicular Epidermal Melanocytes or Keratinocytes from Mouse Tail Skin
Authors:  Samuel Pop, Oscar Urtatiz and Catherine D. Van Raamsdonk, date: 04/20/2022, view: 1294, Q&A: 0

The epidermis is the outermost layer of the skin. It is made up of mostly keratinocytes along with a small number of melanocytes and Langerhans cells. Melanocytes produce a pigment called melanin, which is transferred to the keratinocytes, and

...
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An in vitro Blood-brain Barrier Model to Study the Penetration of Nanoparticles
Authors:  Sezin Aday, Wen Li, Jeffrey M. Karp and Nitin Joshi, date: 02/20/2022, view: 4290, Q&A: 0

The blood-brain barrier (BBB), a crucial protection mechanism in the central nervous system (CNS), is a selective barrier comprised of endothelial cells. It hampers the development of therapeutic and diagnostic tools for neurological diseases due to

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