6 results match your criteria: "National Cancer Institute Building[Affiliation]"
Neurooncol Pract
November 2018
Neuro-Oncology Branch, National Cancer Institute Building, Room, Bethesda, MD.
Body image dissatisfaction is a common issue among patients with cancer and is associated with difficulty coping, anxiety, and depression. Patients with tumors involving the head and neck are at increased risk of body image dissatisfaction due to the visible disfigurement that can occur from their illness and its treatment. Patients with primary central nervous system (CNS) malignancies often face similar tumor-related and treatment-related effects, yet there is limited research conducted in this population.
View Article and Find Full Text PDFNat Microbiol
October 2017
Department of Microbiology, Icahn School of Medicine at Mount Sinai, 1 Gustave L. Levy Place, New York, NY, 10029, USA.
A substantial proportion of influenza-related childhood deaths are due to infection with influenza B viruses, which co-circulate in the human population as two antigenically distinct lineages defined by the immunodominant receptor binding protein, haemagglutinin. While broadly cross-reactive, protective monoclonal antibodies against the haemagglutinin of influenza B viruses have been described, none targeting the neuraminidase, the second most abundant viral glycoprotein, have been reported. Here, we analyse a panel of five murine anti-neuraminidase monoclonal antibodies that demonstrate broad binding, neuraminidase inhibition, in vitro antibody-dependent cell-mediated cytotoxicity and in vivo protection against influenza B viruses belonging to both haemagglutinin lineages and spanning over 70 years of antigenic drift.
View Article and Find Full Text PDFChembiochem
May 2014
Laboratory of Cancer Biology and Genetics, Center for Cancer Research, National Cancer Institute Building 37, Room 4048, 37 Convent Drive MSC 4255, Bethesda, MD 20892-4255, U.S.A.
The C1 domain, which represents the recognition motif on protein kinase C for the lipophilic second messenger diacylglycerol and its ultrapotent analogues, the phorbol esters, has emerged as a promising therapeutic target for cancer and other indications. Potential target selectivity is markedly enhanced both because binding reflects ternary complex formation between the ligand, C1 domain, and phospholipid, and because binding drives membrane insertion of the C1 domain, permitting aspects of the C1 domain surface outside the binding site, per se, to influence binding energetics. Here, focusing on charged residues identified in atypical C1 domains which contribute to their loss of ligand binding activity, we showed that increasing charge along the rim of the binding cleft of the protein kinase C δ C1 b domain raises the requirement for anionic phospholipids.
View Article and Find Full Text PDFNat Med
August 2006
Women's Cancers Section, Laboratory of Molecular Pharmacology, Center for Cancer Research, National Cancer Institute Building 37, Room 1122, National Institutes of Health, Bethesda, Maryland 20892, USA.
Gynecol Oncol
July 2003
Center for Cancer Research, National Cancer Institute Building 10/12C103, 9000 Rockville Pike, Bethesda, MD 20892, USA.
Objective: The incidence of recurrent cervical adenocarcinoma is rising relative to the squamous subtype. There are limited therapeutic options for women with advanced cervical adenocarcinoma. Only a few chemotherapy agents have demonstrated activity in this disease.
View Article and Find Full Text PDFMicrobes Infect
December 1999
Laboratory of Cell Regulation and Carcinogenesis, National Cancer Institute Building 41, Room C629, 41 Library Drive, MSC 5055, Bethesda, MD 20892-5055, USA.
In the past three years, a novel signal transduction pathway downstream of the transforming growth factor-beta (TGF-beta) superfamily receptor serine-threonine kinases has been shown to be mediated by a family of latent transcription factors called 'Smads'. These proteins mediate a short-circuited pathway in which a set of receptor-activated Smads are phosphorylated directly by the receptor kinase and then translocate to the nucleus complexed to the common mediator, Smad4, to participate in transcriptional complexes. Smads 2 and 3 mediate signals predominantly from the TGF-beta receptors.
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