Bio

Honors & Awards


  • ASCO/AACR Workshop: Methods in Clinical Cancer Research, ASCO/AACR (2013)
  • Clinical Research Training Institute, American Society of Hematology (2013)
  • Trainee Research Award, American Society of Hematology (2010)
  • Illinois General Assembly Legislative Scholarship, State of Illinois (2005-2007)
  • Student Research Program Award, American Pediatric Society (2005)
  • NIH Postbaccalaureate Cancer Research Training Award, National Cancer Institute (2003-2004)
  • Summer Research Fellowship, Howard Hughes Medical Institute (2002)

Boards, Advisory Committees, Professional Organizations


  • Member, AACR (2013 - Present)
  • Member, American Society of Hematology (2012 - Present)
  • Member, American Society of Clinical Oncology (2012 - Present)

Professional Education


  • Residency, University of Chicago, Internal Medicine (2011)
  • Internship, University of Chicago, Internal Medicine (2009)
  • Doctor of Medicine, University of Illinois Chicago (2008)
  • Bachelor of Arts, University of Chicago (2003)

Stanford Advisors


Research & Scholarship

Lab Affiliations


Publications

Journal Articles


  • Blood consult: monosomal karyotype acute myeloid leukemia BLOOD Garcia, J. S., Medeiros, B. C., Appelbaum, F. R. 2012; 119 (24): 5659-5660

    View details for DOI 10.1182/blood-2012-01-405225

    View details for Web of Science ID 000307396500015

    View details for PubMedID 22498746

  • Identification and molecular characterization of a novel 3 ' mutation in RUNX1 in a family with familial platelet disorder LEUKEMIA & LYMPHOMA Churpek, J. E., Garcia, J. S., Madzo, J., Jackson, S. A., Onel, K., Godley, L. A. 2010; 51 (10): 1931-1935

    View details for DOI 10.3109/10428194.2010.503821

    View details for Web of Science ID 000282895200027

    View details for PubMedID 20846103

  • An update on the safety and efficacy of decitabine in the treatment of myelodysplastic syndromes ONCOTARGETS AND THERAPY Garcia, J. S., Jain, N., Godley, L. A. 2010; 3: 1-13

    Abstract

    Myelodysplastic syndromes (MDS) are clonal bone marrow malignancies characterized by peripheral cytopenias and dysplastic changes in the bone marrow with various clinical features. Patients with MDS, in particular those with intermediate-2 (Int-2) and high-risk disease, have a poor prognosis. The mainstay of treatment includes cytoxic chemotherapy and supportive care. Over the last decade, promising results from studies focusing on hypomethylating agents, such as decitabine (5-aza-deoxycytidine) and 5-azacitidine, have led to the expansion of the therapeutic arsenal for MDS. This review presents the current data available on the clinical efficacy and safety profile for decitabine as a treatment for MDS. Although not fully understood, decitabine's antitumor activity may involve its ability to induce hypomethylation and reactivation of genes responsible for cellular differentiation, stimulate an immune response, induce DNA damage/apoptotic response pathways, and/or augment stem cell renewal. Future studies that use epigenetic therapies that combine hypomethylating agents with histone deacetylase inhibitors (HDACi) and head-to-head comparison studies of decitabine and 5-azacitidine will provide valuable pre-clinical and clinical data, enhancing our understanding of these drugs.

    View details for Web of Science ID 000286669200001

    View details for PubMedID 20616953

  • Morphogenesis signaling components influence cell cycle regulation by cyclin dependent kinase CELL DIVISION Tobe, B. T., Kitazono, A. A., Garcia, J. S., Gerber, R. A., Bevis, B. J., Choy, J. S., Chasman, D., Kron, S. J. 2009; 4

    Abstract

    The yeast cell cycle is largely controlled by the cyclin-dependent kinase (CDK) Cdc28. Recent evidence suggests that both CDK complex stability as well as function during mitosis is determined by precise regulation of Swe1, a CDK inhibitory kinase and cyclin binding partner. A model of mitotic progression has been provided by study of filamentous yeast. When facing nutrient-limited conditions, Ras2-mediated PKA and MAPK signaling cascades induce a switch from round to filamentous morphology resulting in delayed mitotic progression.To delineate how the dimorphic switch contributes to cell cycle regulation, temperature sensitive cdc28 mutants exhibiting constitutive filamentation were subjected to epistasis analyses with RAS2 signaling effectors. It was found that Swe1-mediated inhibitory tyrosine phosphorylation of Cdc28 during filamentous growth is in part mediated by Ras2 activation of PKA, but not Kss1-MAPK, signaling. This pathway is further influenced by Cks1, a conserved CDK-binding partner of elusive function with multiple proposed roles in CDK activation, transcriptional regulation and ubiquitin-mediated proteasome degradation.The dynamic balance between Cks1- and Swe1-dependent regulation of Cdc28 and, thereby, the timing of mitosis during yeast dimorphism is regulated in part by Ras2/cAMP-mediated PKA signaling, a key pathway controlling filamentous growth.

    View details for DOI 10.1186/1747-1028-4-12

    View details for Web of Science ID 000283781300001

    View details for PubMedID 19566963

  • Cutaneous squamous cell carcinoma responding serially to single-agent cetuximab ANTI-CANCER DRUGS Suen, J. K., Bressler, L., Shord, S. S., Warso, M., Villano, J. L. 2007; 18 (7): 827-829

    Abstract

    Cetuximab (Erbitux) is a recombinant, chimeric monoclonal antibody that binds with high affinity to the extracellular ligand-binding domain of human epidermal growth factor receptor. We report a case of repeated responses to cetuximab in a patient with nonresectable squamous cell skin cancer having strong human epidermal growth factor receptor expression. Nonmelanoma skin cancer is the most common cancer in the US, with more than 1 million new cases detected annually, of which 20-25% are squamous cell carcinomas. Although most primary cutaneous squamous cell carcinomas have a high clinical cure rate and are easily treated, the small subset of cancers that recur or metastasize has a poor prognosis, and accounts for approximately 2000 deaths per year. Treatment with cetuximab should be considered for human epidermal growth factor receptor expressing tumors in a palliative setting.

    View details for Web of Science ID 000248169900011

    View details for PubMedID 17581306

  • Dissection of the Kaposi's sarcoma-associated herpesvirus gene expression program by using the viral DNA replication inhibitor cidofovir JOURNAL OF VIROLOGY Lu, M., Suen, J., Frias, C., Pfeiffer, R., Tsai, M. H., Chuang, E., Zeichner, S. L. 2004; 78 (24): 13637-13652

    Abstract

    Treatment of primary effusion lymphoma cells latently infected by Kaposi's sarcoma-associated herpesvirus (KSHV; human herpesvirus-8 [HHV-8]) with agents such as 12-O-tetradecanoylphorbol-13-acetate (TPA) induces a lytic viral replication cycle, with an ordered gene expression program. Initial studies of the KSHV expression program following TPA induction using viral microarrays yielded useful information concerning the viral expression program, but precise kinetic assignments for some genes remained unclear. Classically, late herpesvirus genes require viral DNA replication for maximal expression. We used cidofovir (CDV), a nucleotide-analogue KSHV DNA polymerase inhibitor, to dissect KSHV expression into two components: genes expressed without viral DNA replication and those requiring it. The expression of known immediate-early or early genes (e.g., open reading frames [ORFs] 50, K8 bZIP, and 57) serving lytic regulatory roles was relatively unaffected by the presence of CDV, while known late capsid and tegument structural genes (e.g., ORFs 25, 26, 64, and 67) were CDV sensitive. Latency-associated transcript ORF 73 was unaffected by the presence of TPA or CDV, suggesting that it was constitutively expressed. Expression of several viral cellular gene homologs, including K2 (vIL-6), ORF 72 (vCyclin), ORF 74 (vGPCR), and K9 (vIRF-1), was unaffected by the presence of CDV, while that of others, such as K4.1 (vMIP-III), K11.1 (vIRF-2), and K10.5 (LANA2, vIRF-3), was inhibited. The results distinguish KSHV genes whose full expression required viral DNA replication from those that did not require it, providing additional insights into KSHV replication and pathogenesis strategies and helping to show which viral cell homologs are expressed at particular times during the lytic process.

    View details for DOI 10.1128/JVI.78.24.13637-13652.2004

    View details for Web of Science ID 000225409900025

    View details for PubMedID 15564474

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