I am an MD/PhD student in Jan Skotheim's lab. My research uses live cell imaging to measure changes in key cell cycle regulatory proteins as cells undergo growth and division.

Education & Certifications

  • Doctor of Philosophy, Stanford University, BIO-PHD (2019)
  • Bachelor of Science, Yale University, Molecular Biophysics & Biochem (2013)


  • 2019 Spring - FAMMED 301A Family Medicine Core Clerkship
  • 2019 Spring - MED 303B Cardiology Clerkship

Lab Affiliations

All Publications

  • LMKB/MARF1 Localizes to mRNA Processing Bodies, Interacts with Ge-1, and Regulates IFI44L Gene Expression PLOS ONE Bloch, D. B., Li, P., Bloch, E. G., Berenson, D. F., Galdos, R. L., Arora, P., Malhotra, R., Wu, C., Yang, W. 2014; 9 (4)


    The mRNA processing body (P-body) is a cellular structure that regulates the stability of cytoplasmic mRNA. MARF1 is a murine oocyte RNA-binding protein that is associated with maintenance of mRNA homeostasis and genomic stability. In this study, autoantibodies were used to identify Limkain B (LMKB), the human orthologue of MARF1, as a P-body component. Indirect immunofluorescence demonstrated that Ge-1 (a central component of the mammalian core-decapping complex) co-localized with LMKB in P-bodies. Two-hybrid and co-immunoprecipitation assays were used to demonstrate interaction between Ge-1 and LMKB. The C-terminal 120 amino acids of LMKB mediated interaction with Ge-1 and the N-terminal 1094 amino acids of Ge-1 were required for interaction with LMKB. LMKB is the first protein identified to date that interacts with this portion of Ge-1. LMKB was expressed in human B and T lymphocyte cell lines; depletion of LMKB increased expression of IFI44L, a gene that has been implicated in the cellular response to Type I interferons. The interaction between LMKB/MARF1, a protein that contains RNA-binding domains, and Ge-1, which interacts with core-decapping proteins, suggests that LMKB has a role in the regulation of mRNA stability. LMKB appears to have different functions in different cell types: maintenance of genomic stability in developing oocytes and possible dampening of the inflammatory response in B and T cells.

    View details for DOI 10.1371/journal.pone.0094784

    View details for Web of Science ID 000335240300016

    View details for PubMedID 24755989

    View details for PubMedCentralID PMC3995692

  • Small, Highly Active DNAs That Hydrolyze DNA JOURNAL OF THE AMERICAN CHEMICAL SOCIETY Gu, H., Furukawa, K., Weinberg, Z., Berenson, D. F., Breaker, R. R. 2013; 135 (24): 9121-9129


    DNA phosphoester bonds are exceedingly resistant to hydrolysis in the absence of chemical or enzymatic catalysts. This property is particularly important for organisms with large genomes, as resistance to hydrolytic degradation permits the long-term storage of genetic information. Here we report the creation and analysis of two classes of engineered deoxyribozymes that selectively and rapidly hydrolyze DNA. Members of class I deoxyribozymes carry a catalytic core composed of only 15 conserved nucleotides and attain an observed rate constant (k(obs)) of ~1 min(-1) when incubated near neutral pH in the presence of Zn(2+). Natural DNA sequences conforming to the class I consensus sequence and structure were found that undergo hydrolysis under selection conditions (2 mM Zn(2+), pH 7), which demonstrates that the inherent structure of certain DNA regions might promote catalytic reactions, leading to genomic instability.

    View details for DOI 10.1021/ja403585e

    View details for Web of Science ID 000320899200052

    View details for PubMedID 23679108

    View details for PubMedCentralID PMC3763483

  • Insulin analogs for the treatment of diabetes mellitus: therapeutic applications of protein engineering YEAR IN DIABETES AND OBESITY Berenson, D. F., Weiss, A. R., Wan, Z., Weiss, M. A. 2011; 1243: E40-E54


    The engineering of insulin analogs represents a triumph of structure-based protein design. A framework has been provided by structures of insulin hexamers. Containing a zinc-coordinated trimer of dimers, such structures represent a storage form of the active insulin monomer. Initial studies focused on destabilization of subunit interfaces. Because disassembly facilitates capillary absorption, such targeted destabilization enabled development of rapid-acting insulin analogs. Converse efforts were undertaken to stabilize the insulin hexamer and promote higher-order self-assembly within the subcutaneous depot toward the goal of enhanced basal glycemic control with reduced risk of hypoglycemia. Current products either operate through isoelectric precipitation (insulin glargine, the active component of Lantus(®); Sanofi-Aventis) or employ an albumin-binding acyl tether (insulin detemir, the active component of Levemir(®); Novo-Nordisk). To further improve pharmacokinetic properties, modified approaches are presently under investigation. Novel strategies have recently been proposed based on subcutaneous supramolecular assembly coupled to (a) large-scale allosteric reorganization of the insulin hexamer (the TR transition), (b) pH-dependent binding of zinc ions to engineered His-X(3)-His sites at hexamer surfaces, or (c) the long-range vision of glucose-responsive polymers for regulated hormone release. Such designs share with wild-type insulin and current insulin products a susceptibility to degradation above room temperature, and so their delivery, storage, and use require the infrastructure of an affluent society. Given the global dimensions of the therapeutic supply chain, we envisage that concurrent engineering of ultra-stable protein analog formulations would benefit underprivileged patients in the developing world.

    View details for DOI 10.1111/j.1749-6632.2012.06468.x

    View details for Web of Science ID 000301504400002

    View details for PubMedID 22641195

    View details for PubMedCentralID PMC3360579