OpenAlex Citation Counts

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OpenAlex is a bibliographic catalogue of scientific papers, authors and institutions accessible in open access mode, named after the Library of Alexandria. It's citation coverage is excellent and I hope you will find utility in this listing of citing articles!

If you click the article title, you'll navigate to the article, as listed in CrossRef. If you click the Open Access links, you'll navigate to the "best Open Access location". Clicking the citation count will open this listing for that article. Lastly at the bottom of the page, you'll find basic pagination options.

Requested Article:

Polarized PtdIns(4,5)P 2 distribution mediated by a voltage-sensing phosphatase (VSP) regulates sperm motility
Takafumi Kawai, Haruhiko Miyata, Hiroki Nakanishi, et al.
Proceedings of the National Academy of Sciences (2019) Vol. 116, Iss. 51, pp. 26020-26028
Open Access | Times Cited: 28

Showing 1-25 of 28 citing articles:

Homozygous mutation in SLO3 leads to severe asthenoteratozoospermia due to acrosome hypoplasia and mitochondrial sheath malformations
Mingrong Lv, Chunyu Liu, Chunjie Ma, et al.
Reproductive Biology and Endocrinology (2022) Vol. 20, Iss. 1
Open Access | Times Cited: 25

The sperm specific Na+,K+-ATPase α4 shows a highly structured and dynamic distribution at the sperm flagellum
Mumtarin Jannat Oishee, Jeff S. McDermott, Gladis Sánchez, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2025)
Closed Access

Activation of motility and chemotaxis in the spermatozoa
Manabu Yoshida, Kaoru Yoshida
Reproductive Medicine and Biology (2025) Vol. 24, Iss. 1
Open Access

Zinc is a Key Regulator of the Sperm-Specific K+ Channel (Slo3) Function
Rizki Tsari Andriani, Tanadet Pipatpolkai, Haruhiko Miyata, et al.
(2025)
Open Access

Zinc is a Key Regulator of the Sperm-Specific K+ Channel (Slo3) Function
Rizki Tsari Andriani, Tanadet Pipatpolkai, Haruhiko Miyata, et al.
(2025)
Open Access

The Ca2+ channel CatSper is not activated by cAMP/PKA signaling but directly affected by chemicals used to probe the action of cAMP and PKA
Tao Wang, Samuel Young, Henrike Krenz, et al.
Journal of Biological Chemistry (2020) Vol. 295, Iss. 38, pp. 13181-13193
Open Access | Times Cited: 36

Physiological role of potassium channels in mammalian germ cell differentiation, maturation, and capacitation
Ariadna Delgado‐Bermúdez, Marc Yeste, Sergi Bonet, et al.
Andrology (2024)
Open Access | Times Cited: 3

Role of K364 next to the active site cysteine in voltage-dependent phosphatase activity of Ci-VSP
Ian Costa Paixao, Natsuki Mizutani, M. Matsuda, et al.
Biophysical Journal (2023) Vol. 122, Iss. 11, pp. 2267-2284
Open Access | Times Cited: 6

Interaction between S4 and the phosphatase domain mediates electrochemical coupling in voltage-sensing phosphatase (VSP)
Natsuki Mizutani, Akira Kawanabe, Yuka Jinno, et al.
Proceedings of the National Academy of Sciences (2022) Vol. 119, Iss. 26
Open Access | Times Cited: 10

Coupling sensor to enzyme in the voltage sensing phosphatase
Yawei Yu, Zhang Lin, Baobin Li, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 1

The sperm-specific K+ channel Slo3 is inhibited by albumin and steroids contained in reproductive fluids
Johannes Lorenz, Clara Eisenhardt, Teresa Mittermair, et al.
Frontiers in Cell and Developmental Biology (2024) Vol. 12
Open Access | Times Cited: 1

Voltage-sensing phosphatase (Vsp) regulates endocytosis-dependent nutrient absorption in chordate enterocytes
Adisorn Ratanayotha, M. Matsuda, Yukiko Kimura, et al.
Communications Biology (2022) Vol. 5, Iss. 1
Open Access | Times Cited: 6

Long-term depression in neurons involves temporal and ultra-structural dynamics of phosphatidylinositol-4,5-bisphosphate relying on PIP5K, PTEN and PLC
Sarah Ann Hofbrucker-MacKenzie, Eric Seemann, Martin Westermann, et al.
Communications Biology (2023) Vol. 6, Iss. 1
Open Access | Times Cited: 3

Spotlight on the Binding Affinity of Ion Channels for Phosphoinositides: From the Study of Sperm Flagellum
Takafumi Kawai, Yasushi Okamura
Frontiers in Physiology (2022) Vol. 13
Open Access | Times Cited: 4

Editorial: The key role of lipids in the regulation of ion channels
Andrea Saponaro, Marco Lolicato
Frontiers in Physiology (2022) Vol. 13
Open Access | Times Cited: 4

Engineering voltage sensing phosphatase (VSP)
Hidekazu Tsutsui, Natsuki Mizutani, Yasushi Okamura
Methods in enzymology on CD-ROM/Methods in enzymology (2021), pp. 85-114
Closed Access | Times Cited: 4

Occurrence of Calcium Oscillations in Human Spermatozoa Is Based on Spatial Signaling Enzymes Distribution
Julia-Jessica D. Korobkin, Fedor Balabin, S.A. Yakovenko, et al.
International Journal of Molecular Sciences (2021) Vol. 22, Iss. 15, pp. 8018-8018
Open Access | Times Cited: 4

Insight into the function of voltage-sensing phosphatase (VSP) in hind-gut derived pseudoplacenta of a viviparous teleost Xenotoca eiseni
Adisorn Ratanayotha, Atsuo Iida, Jumpei Nomura, et al.
AJP Regulatory Integrative and Comparative Physiology (2024) Vol. 326, Iss. 6, pp. R461-R471
Closed Access

The significance of electrical signals in maturing spermatozoa for phosphoinositide regulation through voltage-sensing phosphatase
Takafumi Kawai, Shin Morioka, Haruhiko Miyata, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access

Voltage- and Ca2+-inducible PLC activity for analyzing PI(4,5)P2 sensitivity of ion channels in Xenopus oocytes
Takafumi Kawai, Natsuki Mizutani, Yasushi Okamura
Biochimica et Biophysica Acta (BBA) - Biomembranes (2024), pp. 184396-184396
Open Access

Zinc is a Key Regulator of the Sperm-Specific K+Channel (Slo3) Function
Rizki Tsari Andriani, Tanadet Pipatpolkai, Haruhiko Miyata, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access

Comparative Investigation of the Mechanisms of Calcium Response in Human and Murine Spermatozoa
J. D. Korobkina, Mikhail A. Panteleev, А. Н. Свешникова
Biochemistry (Moscow) Supplement Series A Membrane and Cell Biology (2024) Vol. 18, Iss. 2, pp. 110-126
Closed Access

Comparative Investigation of the Mechanisms of Calcium Response in Human and Murine Spermatozoa
J. D. Korobkina, Mikhail A. Panteleev, А. Н. Свешникова
Биологические мембраны Журнал мембранной и клеточной биологии (2024) Vol. 41, Iss. 3, pp. 254-274
Closed Access

Shedding light on the control of CatSper Ca2+channels by cAMP and chemicals used to probe cAMP signaling
Tao Wang, Samuel Young, Frank Tüttelmann, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2020)
Open Access | Times Cited: 3

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