Last year we told you about an exciting update at JBC: We reinvented our Herbert Tabor Young Investigator Awards to focus on those young scientists who are contributing the best papers to the journal (
- Gierasch L.M.
- DeMartino G.
The Herbert Tabor Best Paper Awards: Celebrating young authors who contribute top content to JBC.
). Our thinking was that this change would continue to recognize outstanding upcoming researchers, while more directly linking to our goal of mentoring the next generation, through the constructive feedback provided during the review process, and making a home for them at JBC, the ASBMB Annual Meeting, and beyond.
The challenge, of course, then becomes to identify the “best” out of the long list of outstanding content in JBC. We created our initial short list by looking through our Editors' Picks, Accelerated Communications, and papers that appeared on our most read lists or had high numbers of downloads or citations. We added in papers that our Associate Editors noted as being otherwise striking, and we took a careful look at papers nominated by you, our readers, in response to our initial announcement. This list was curated to make sure that the first authors of the papers were up-and-coming scientists, since our goal was to bring attention to those on the rise rather than those who are continuing an already vibrant career. And finally, we considered the various ways that individual papers can impact their fields, whether by solving long-standing mysteries, proposing new hypotheses, or creating new methods and tools, and what metrics (of any kind) can ever really tell us about the true quality of a manuscript. Of course, there will always be some element of subjectivity to any selection of this kind; what seems cool and amazing to one scientist reflects not only the quality of the science but their own point of reference. To mitigate this, the final decisions were made via blind voting of the assembled Award Committee, consisting of six Associate Editors whose own expertise spans from protein structure to cancer mechanisms to lipid biology and beyond.
With that said, we are inspired and thrilled to introduce you to the 2018 awardees!
Maria Fe Lanfranco
, a postdoc in Rodrigo Maillard's lab at Georgetown University, led a study focused on dissecting the allosteric mechanisms of receptor signaling, using engineered homodimeric constructs of the transcription factor cAMP receptor protein as a testbed (
- Lanfranco M.F.
- Gárate F.
- Engdahl A.J.
- Maillard R.A.
Asymmetric configurations in a reengineered homodimer reveal multiple subunit communication pathways in protein allostery.
). One of the reviewers of the paper was impressed that “the authors found that a single mutation is sufficient to change the global allosteric behavior of the dimer and that the mutations in the same and different subunits produced drastically different cooperative effects, suggesting the distinct role of intrasubunit interactions and intersubunit communication in allostery.”
, whose interest in the regulatory mechanisms of iron metabolism began during a rotation with his Ph.D. advisor Richard Eisenstein at the University of Wisconsin, led a project dissecting the coordination between two pathways to maintain iron homeostasis. Specifically, Johnson and his colleagues demonstrated that the ubiquitin E3 ligase FBXL5 keeps the iron regulatory proteins IRP1 and IRP2 in check when regulation provided by the Fe-S cluster insertion machinery is disrupted (
- Johnson N.B.
- Deck K.M.
- Nizzi C.P.
- Eisenstein R.S.
A synergistic role of IRP1 and FBXL5 proteins in coordinating iron metabolism during cell proliferation.
). The referees of the paper were excited that the paper not only explained seemingly contradictory results in the literature but “for the first time showed a negative feedback loop” in the process. In an Editors' Pick Highlight (
Checks and balances for the iron bank.
), Caryn Outten further describes the work as having “opened up new avenues of study to explore, while providing a deeper understanding of the checks and balances in place to control the intracellular iron bank.”
Richard Karpowicz, Jr.
, a postdoc in Virginia Lee's lab at the University of Pennsylvania, led a study merging fluorescence imaging of neurodegenerative disease–associated protein aggregates with site-specific protein labeling to explore mechanisms by which pathological α-synuclein seeds are internalized and processed by neurons (
- Karpowicz Jr., R.J.
- Haney C.M.
- Mihaila T.S.
- Sandler R.M.
- Petersson E.J.
- Lee V.M.
Selective imaging of internalized proteopathic α-synuclein seeds in primary neurons reveals mechanistic insight into transmission of synucleinopathies.
). One of the referees found the methodological advances particularly innovative, noting they could “see this paper serving as a compelling guide for other investigators in the synucleinopathy field.” Masato Hasegawa and Genjiro Suzuki, authors of the Editors' Pick Highlight linked to this work (
Following the fate of endocytosed fibrils.
), described the study as taking “new strides toward mechanistic understanding by following the fate of α-synuclein as it interacts with an uninfected cell.”
, then a joint Ph.D. student in the labs of Howard Jenkinson, Angela Nobbs, and Paul Race at the University of Bristol, led a study on the mechanisms of bacterial pathogenicity that yielded new insights into protein recognition as well as initiated an ongoing collaboration between the two labs. In particular, Back and her colleagues describe a “catch-clamp” mechanism, in which a disordered domain in an adhesin from Streptococcus gordonii
forms an initial, weak-affinity interaction with its host target, promoting a second, high-affinity interaction with the adhesin's ligand-binding domain (
- Back C.R.
- Sztukowska M.N.
- Till M.
- Lamont R.J.
- Jenkinson H.F.
- Nobbs A.H.
- Race P.R.
The Streptococcus gordonii adhesin CshA protein binds host fibronectin via a catch-clamp mechanism.
). One of the referees described this paper as “a pleasure to review,” saying it “brings long-awaited insights.”
, then a Ph.D. candidate in Michael Root's lab at Thomas Jefferson University, led a study exploring the interactions between two classes of HIV-1 inhibitors, with implications for our basic understanding of both viral entry and antiviral strategies for HIV treatment (
Complex interplay of kinetic factors governs the synergistic properties of HIV-1 entry inhibitors.
). In a linked Editors' Pick Highlight, Gregory Melikyan suggested “this study helps reconcile the divergent findings … by demonstrating a complex dependence of synergy on viral and cellular factors that affect the fusion and inactivation kinetics” (
How entry inhibitors synergize to fight HIV.
). One of the referees also complimented the authors' effort, saying “they make a number of intriguing and important observations of the conditions of synergy, which are fitted into a cogent theoretical framework.”
To learn more about these rising stars, please read the March issue of ASBMB Today
, which includes more information about their career paths and how these papers took shape (
). And join us at the ASBMB Annual Meeting, taking place in San Diego, April 21–25, where the winners will receive their awards and present invited short talks about their work in a special session on Sunday, April 22, 2:30–3:45. If you want to find more exciting content from the 2017 issues of JBC, please check out our virtual issue, “The Year in JBC: 2017” (
), which highlights one great paper from each of our Table of Contents categories; the five papers from our awardees were excluded from this collection, since there were already too many good candidates to feature.
Congratulations to our awardees, and see you in San Diego!
Published online: March 02, 2018
© 2018 by The American Society for Biochemistry and Molecular Biology, Inc.