Michael L. Jennings
Professor and Chair
Also affiliated: University of Iowa (1982–1991); Harvard University (1976–1980); Fukuoka University (1994); Max Planck Institute of Biophysics (1978–1982); The University of Texas Medical Branch at Galveston (1988–1996)
Research Areas
Biomedical Subjects
Links
Biography and Research Information
OverviewAI-generated summary
Michael L. Jennings' research has focused on the structure and function of membrane proteins, particularly the red blood cell anion transport protein, also known as band 3 protein. His work has investigated the kinetics of anion transport across the erythrocyte membrane, examining how factors like cell swelling and chemical agents influence transport rates. Jennings has also explored the proteolysis of band 3 protein and its interaction with specific chemical compounds, contributing to the understanding of its topography and function.
His research extends to other cell types, including mitochondria-rich cells in the collecting duct, where he has studied the cytochemistry of lectin and band 3. Jennings' work has been supported by significant publication and citation metrics, with an h-index of 41 and over 4,900 citations across more than 100 publications. He is recognized as a highly cited researcher and maintains an active research group at the University of Arkansas for Medical Sciences, collaborating with colleagues such as Samuel G. Mackintosh, Ricky D. Edmondson, Renny S. Lan, and Nükhet Aykin‐Burns.
Metrics
- h-index: 40
- Publications: 92
- Citations: 4,644
Positions
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Professor and Chair 1995–presentUniversity of Arkansas for Medical Sciences Physiology and Biophysics ORCID
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Professor 1987–1995University of Texas Medical Branch at Galveston Physiology and Biophysics ORCID
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Associate Professor 1983–1987University of Iowa Physiology and Biophysics ORCID
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Assistant Professor 1978–1983University of Iowa Physiology and Biophysics ORCID
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Postdoc 1976–1978Max-Planck-Institut für Biophysik Zell Physiologie ORCID
Selected Publications
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A complete set of rate constants for a transporter’s catalytic cycle (2025)
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Role of transporters in regulating mammalian intracellular inorganic phosphate (2023)
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Author response: Transferrin receptor 1-mediated iron uptake regulates bone mass in mice via osteoclast mitochondria and cytoskeleton (2022)
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Transferrin receptor 1-mediated iron uptake regulates bone mass in mice via osteoclast mitochondria and cytoskeleton (2022)
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Cell physiology and molecular mechanism of anion transport by erythrocyte band 3/AE1 (2021)
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Transferrin receptor 1-mediated iron uptake regulates bone mass in mice via osteoclast mitochondria and cytoskeleton (2021)
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Decoding the epitranscriptional landscape from native RNA sequences (2020)
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Decoding the Epitranscriptional Landscape from Native RNA Sequences (2018)
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Carriers, exchangers, and cotransporters in the first 100 years of the <i>Journal of General Physiology</i> (2018)
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Deletion of ferroportin in murine myeloid cells increases iron accumulation and stimulates osteoclastogenesis in vitro and in vivo (2018)
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Asymmetry of inverted-topology repeats in the AE1 anion exchanger suggests an elevator-like mechanism (2017)
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The Murine Osteoclasts Lacking Transferrin Receptor 1 have Altered Mitochondrial Metabolism, Cytoskeletal Organization and Increased Trabecular Bone Mass (2017)
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Repeat-Swap Homology Modeling of the Anion Exchanger AE1 Reveals an Elevator-Like Antiport Mechanism (2017)
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Acidic Eye‐Drops De‐Swell the Edematous Corneas of <i>Slc4a11</i> ‐null Mice; Evidence for Functional Coupling between Slc4a11 and the H <sup>+</sup> /lactate Cotransporter Mct1 (2016)
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Mouse Slc4a11 expressed in <i>Xenopus</i> oocytes is an ideally selective H<sup>+</sup>/OH<sup>−</sup> conductance pathway that is stimulated by rises in intracellular and extracellular pH (2016)
Collaboration Network
Top Collaborators
- Transferrin receptor 1-mediated iron uptake regulates bone mass in mice via osteoclast mitochondria and cytoskeleton
- Deletion of ferroportin in murine myeloid cells increases iron accumulation and stimulates osteoclastogenesis in vitro and in vivo
- Transferrin receptor 1-mediated iron uptake regulates bone mass in mice via osteoclast mitochondria and cytoskeleton
- Author response: Transferrin receptor 1-mediated iron uptake regulates bone mass in mice via osteoclast mitochondria and cytoskeleton
- The Murine Osteoclasts Lacking Transferrin Receptor 1 have Altered Mitochondrial Metabolism, Cytoskeletal Organization and Increased Trabecular Bone Mass
- Transferrin receptor 1-mediated iron uptake regulates bone mass in mice via osteoclast mitochondria and cytoskeleton
- Deletion of ferroportin in murine myeloid cells increases iron accumulation and stimulates osteoclastogenesis in vitro and in vivo
- Transferrin receptor 1-mediated iron uptake regulates bone mass in mice via osteoclast mitochondria and cytoskeleton
- Author response: Transferrin receptor 1-mediated iron uptake regulates bone mass in mice via osteoclast mitochondria and cytoskeleton
- The Murine Osteoclasts Lacking Transferrin Receptor 1 have Altered Mitochondrial Metabolism, Cytoskeletal Organization and Increased Trabecular Bone Mass
- Transferrin receptor 1-mediated iron uptake regulates bone mass in mice via osteoclast mitochondria and cytoskeleton
- Deletion of ferroportin in murine myeloid cells increases iron accumulation and stimulates osteoclastogenesis in vitro and in vivo
- Transferrin receptor 1-mediated iron uptake regulates bone mass in mice via osteoclast mitochondria and cytoskeleton
- Author response: Transferrin receptor 1-mediated iron uptake regulates bone mass in mice via osteoclast mitochondria and cytoskeleton
- The Murine Osteoclasts Lacking Transferrin Receptor 1 have Altered Mitochondrial Metabolism, Cytoskeletal Organization and Increased Trabecular Bone Mass
- Transferrin receptor 1-mediated iron uptake regulates bone mass in mice via osteoclast mitochondria and cytoskeleton
- Deletion of ferroportin in murine myeloid cells increases iron accumulation and stimulates osteoclastogenesis in vitro and in vivo
- Transferrin receptor 1-mediated iron uptake regulates bone mass in mice via osteoclast mitochondria and cytoskeleton
- Author response: Transferrin receptor 1-mediated iron uptake regulates bone mass in mice via osteoclast mitochondria and cytoskeleton
- The Murine Osteoclasts Lacking Transferrin Receptor 1 have Altered Mitochondrial Metabolism, Cytoskeletal Organization and Increased Trabecular Bone Mass
- Mouse Slc4a11 expressed in <i>Xenopus</i> oocytes is an ideally selective H<sup>+</sup>/OH<sup>−</sup> conductance pathway that is stimulated by rises in intracellular and extracellular pH
- The Mammalian Bicarbonate Transporter Related Protein BTR1 ( <i>Slc4a11</i> ) Promotes Boron Accumulation In Yeast
- Acidic Eye‐Drops De‐Swell the Edematous Corneas of <i>Slc4a11</i> ‐null Mice; Evidence for Functional Coupling between Slc4a11 and the H <sup>+</sup> /lactate Cotransporter Mct1
- Mouse Slc4a11 expressed in <i>Xenopus</i> oocytes is an ideally selective H<sup>+</sup>/OH<sup>−</sup> conductance pathway that is stimulated by rises in intracellular and extracellular pH
- The Mammalian Bicarbonate Transporter Related Protein BTR1 ( <i>Slc4a11</i> ) Promotes Boron Accumulation In Yeast
- Acidic Eye‐Drops De‐Swell the Edematous Corneas of <i>Slc4a11</i> ‐null Mice; Evidence for Functional Coupling between Slc4a11 and the H <sup>+</sup> /lactate Cotransporter Mct1
- Transport and regulatory characteristics of the yeast bicarbonate transporter homolog Bor1p
- Chloride Homeostasis in <i>Saccharomyces cerevisiae</i>: High Affinity Influx, V-ATPase-dependent Sequestration, and Identification of a Candidate Cl− Sensor
- Inactivation of Saccharomyces cerevisiae Sulfate Transporter Sul2p: Use It and Lose It
- Biotin dependency due to a defect in biotin transport
- Biotin dependency due to a defect in biotin transport
- Biotin dependency due to a defect in biotin transport
- Biotin dependency due to a defect in biotin transport
- Biotin dependency due to a defect in biotin transport
- Biotin dependency due to a defect in biotin transport
- Biotin dependency due to a defect in biotin transport
- Biotin dependency due to a defect in biotin transport
- Biotin dependency due to a defect in biotin transport
- Biotin dependency due to a defect in biotin transport
- Biotin dependency due to a defect in biotin transport
- Biotin dependency due to a defect in biotin transport
- Biotin dependency due to a defect in biotin transport
- Biotin dependency due to a defect in biotin transport
- Biotin dependency due to a defect in biotin transport
- Biotin dependency due to a defect in biotin transport
- Biotin dependency due to a defect in biotin transport
- Biotin dependency due to a defect in biotin transport
- Biotin dependency due to a defect in biotin transport
- Biotin dependency due to a defect in biotin transport
- Biotin dependency due to a defect in biotin transport
- Transferrin receptor 1-mediated iron uptake regulates bone mass in mice via osteoclast mitochondria and cytoskeleton
- Deletion of ferroportin in murine myeloid cells increases iron accumulation and stimulates osteoclastogenesis in vitro and in vivo
- Transferrin receptor 1-mediated iron uptake regulates bone mass in mice via osteoclast mitochondria and cytoskeleton
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