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Stephen Harrison

Stephen Harrison

· Academic Tutor, Professor of Pediatrics, Investigator, Howard Hughes Medical Institute, Giovanni Armenise - Professor of Basic Biomedical Science

Harvard University · Molecular and Cellular Biology

Active 1965–2025

h-index162
Citations102.8k
Papers807117 last 5y
Funding$928.2M2 active

Academic metrics are sourced from OpenAlex and public funding records; values may differ from Google Scholar.

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About

Stephen C. Harrison is a Professor of Biological Chemistry and Molecular Pharmacology at Harvard University who has played a central role in guiding the Biochemical Sciences Tutorial Program for decades. He served as Head Tutor of the program from 1972 to 1996, contributing significantly to its development and enduring legacy. Harrison emphasizes that the tutorial program was designed not merely for students to absorb biological facts but to learn how to think critically about scientific problems and understand how discoveries emerge from evidence. Under his guidance, the program fostered intellectual relationships between students and practicing scientists, encouraging students to read and discuss primary research papers, analyze experiments, and interpret scientific evidence. Harrison highlights that tutors also serve as primary academic advisors, mentoring students throughout their undergraduate concentration and helping them pursue laboratory research and senior honors thesis projects. He notes that one advantage of the tutorial system was its ability to recruit faculty working in emerging scientific fields, thereby exposing undergraduates to new areas of science before they became standard parts of the curriculum. Through his leadership, the Biochemical Sciences Tutorial Program has remained a defining feature of Harvard's life sciences education, shaping generations of students by cultivating curiosity, critical thinking, and scientific conversation.

Research topics

  • Biology
  • Biochemistry
  • Biophysics
  • Chemistry
  • Cell biology
  • Crystallography
  • Immunology
  • Nanotechnology
  • Evolutionary biology
  • Virology

Selected publications

  • Structure of a nascent membrane protein as it folds on the BAM complex

    Nature · 2020 · 175 citations

  • Structures of the ATP-fueled ClpXP proteolytic machine bound to protein substrate

    eLife · 2020 · 148 citations

    enzyme that show how asymmetric hexameric rings of ClpX bind symmetric heptameric rings of ClpP and interact with protein substrates. Subunits in the ClpX hexamer assume a spiral conformation and interact with two-residue segments of substrate in the axial channel, as observed for other AAA+ proteases and protein-remodeling machines. Strictly sequential models of ATP hydrolysis and a power stroke that moves two residues of the substrate per translocation step have been inferred from these struct…

  • Recapitulation of HIV-1 Env-antibody coevolution in macaques leading to neutralization breadth

    Science · 2020 · 99 citations

    Neutralizing antibodies elicited by HIV-1 coevolve with viral envelope proteins (Env) in distinctive patterns, in some cases acquiring substantial breadth. We report that primary HIV-1 envelope proteins-when expressed by simian-human immunodeficiency viruses in rhesus macaques-elicited patterns of Env-antibody coevolution very similar to those in humans, including conserved immunogenetic, structural, and chemical solutions to epitope recognition and precise Env-amino acid substitutions, insertio…

  • Structure of the Ndc80 complex and its interactions at the yeast kinetochore–microtubule interface

    Open Biology · 2023-03-01 · 30 citations

    articleOpen accessSenior authorCorresponding

    The conserved Ndc80 kinetochore complex, Ndc80c, is the principal link between mitotic spindle microtubules and centromere-associated proteins. We used AlphaFold 2 (AF2) to obtain predictions of the Ndc80 'loop' structure and of the Ndc80 : Nuf2 globular head domains that interact with the Dam1 subunit of the heterodecameric DASH/Dam1 complex (Dam1c). The predictions guided design of crystallizable constructs, with structures close to the predicted ones. The Ndc80 'loop' is a stiff, α-helical 's…

  • A communication hub for phosphoregulation of kinetochore-microtubule attachment

    Current Biology · 2024-05-21 · 17 citations

    articleOpen accessSenior authorCorresponding

    The Mps1 and Aurora B kinases regulate and monitor kinetochore attachment to spindle microtubules during cell division, ultimately ensuring accurate chromosome segregation. In yeast, the critical spindle attachment components are the Ndc80 and Dam1 complexes (Ndc80c and DASH/Dam1c, respectively). Ndc80c is a 600-Å-long heterotetramer that binds microtubules through a globular "head" at one end and centromere-proximal kinetochore components through a globular knob at the other end. Dam1c is a het…

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