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Biology and Biochemistry

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83
Citations
21632
World Ranking
3558
National Ranking
1781

Medicine

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83
Citations
22184
World Ranking
15749
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Overview

Ronald L. Nagel was affiliated with the Albert Einstein College of Medicine in the United States during their career. Their professional work as a scientist was associated with this institution.

Information regarding specific research papers, fields of study, subfields, main topics of work, co-authors, and publication venues has not been provided. There are no records of published books or awards attributed to this scientist in the available data.

The absence of recent papers and co-author data limits a detailed overview of their research contributions and collaborations. Likewise, without details on primary and subfields of study or main research topics, it is not possible to delineate the scientific areas in which Ronald L. Nagel specialized.

Ronald L. Nagel is recorded as deceased. This profile presents factual information about the scientist based solely on the provided source data, without additional interpretation or assessment of their work.

Best Publications

  • Sickle-cell disease.

    Marie J Stuart;Ronald L Nagel

  • Correction of Sickle Cell Disease in Transgenic Mouse Models by Gene Therapy

    Robert Pawliuk;Karen A. Westerman;Mary E. Fabry;Emmanuel Payen

  • Shear stress enhances the proteolysis of von Willebrand factor in normal plasma

    Han-Mou Tsai;Ira I. Sussman;Ronald L. Nagel

  • Evidence for the multicentric origin of the sickle cell hemoglobin gene in Africa

    J Pagnier;J G Mears;O Dunda-Belkhodja;K E Schaefer-Rego

  • Polymerase chain reaction amplification applied to the determination of β‐like globin gene cluster haplotypes

    Millicent Sutton;Eric E. Bouhassira;Ronald L. Nagel;Ronald L. Nagel

  • Hematologically and genetically distinct forms of sickle cell anemia in Africa. The Senegal type and the Benin type.

    Ronald L. Nagel;Mary E. Fabry;Josee Pagnier;Isidore Zohoun

  • Common haplotype dependency of high G gamma-globin gene expression and high Hb F levels in beta-thalassemia and sickle cell anemia patients.

    D Labie;J Pagnier;C Lapoumeroulie;F Rouabhi

  • Erythrocytes in sickle cell anemia are heterogeneous in their rheological and hemodynamic characteristics.

    D K Kaul;M E Fabry;P Windisch;S Baez

  • The paradox of hemoglobin SC disease.

    Ronald L. Nagel;Mary E. Fabry;Martin H. Steinberg

  • The Binding of Hemoglobin to Haptoglobin and Its Relation to Subunit Dissociation of Hemoglobin

    Ronald L. Nagel;Quentin H. Gibson

  • Structural bases of the inhibitory effects of hemoglobin F and hemoglobin A2 on the polymerization of hemoglobin S.

    Ronald L. Nagel;Robert M. Bookchin;Joyce Johnson;Dominique Labie

  • Sickle cell anemia day hospital: an approach for the management of uncomplicated painful crises.

    Lennette J. Benjamin;Gwendolyn I. Swinson;Ronald L. Nagel

  • Liquid-liquid Separation in Solutions of Normal and Sickle Cell Hemoglobin

    Oleg Galkin;Kai Chen;Ronald L. Nagel;Rhoda Elison Hirsch

  • Rosetting of Plasmodium falciparum-infected red blood cells with uninfected red blood cells enhances microvascular obstruction under flow conditions.

    DK Kaul;EF Roth;RL Nagel;RJ Howard

  • Permanent and panerythroid correction of murine β thalassemia by multiple lentiviral integration in hematopoietic stem cells

    Suzan Imren;Emmanuel Payen;Karen A. Westerman;Robert Pawliuk

  • Glucose-6-phosphate dehydrogenase deficiency inhibits in vitro growth of Plasmodium falciparum.

    Eugene F. Roth;Carmen Raventos-Suarez;Antoniettina Rinaldi;Ronald L. Nagel

  • The pathophysiology of vascular obstruction in the sickle syndromes

    D.K. Kaul;M.E. Fabry;R.L. Nagel

  • Ligand-induced conformational dependence of hemoglobin in sickling interactions☆

    Robert M. Bookchin;Ronald L. Nagel

  • Plasmodium falciparum: inhibition of in vitro growth by desferrioxamine.

    Carmen Raventos-Suarez;Simeon Pollack;Ronald L. Nagel

  • Structure and properties of hemoglobin C-Harlem, a human hemoglobin variant with amino acid substitutions in 2 residues of the beta-polypeptide chain.

    Robert M. Bookchin;Ronald L. Nagel;Helen M. Ranney

Frequent Co-Authors

Rajagopal Krishnamoorthy
Rajagopal Krishnamoorthy Inserm : Institut national de la santé et de la recherche médicale
Eric E. Bouhassira
Eric E. Bouhassira Albert Einstein College of Medicine
Martin H. Steinberg
Martin H. Steinberg Boston University
Peter G. Vekilov
Peter G. Vekilov University of Houston
Connie J. Eaves
Connie J. Eaves University of British Columbia
Gerard A. Lutty
Gerard A. Lutty Johns Hopkins University School of Medicine
Jacques Elion
Jacques Elion Université Paris Cité
Frank Costantini
Frank Costantini Columbia University
Herbert B. Tanowitz
Herbert B. Tanowitz Albert Einstein College of Medicine
R. Keith Humphries
R. Keith Humphries University of British Columbia

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