نتایج جستجو برای: fragile histidine triad protein

تعداد نتایج: 1262078  

Journal: :Cancer research 2001
H Ishii K R Dumon A Vecchione F Trapasso K Mimori H Alder M Mori G Sozzi R Baffa K Huebner C M Croce

Reintroduction of a tumor suppressor gene product in cancer cells is a promising strategy for cancer gene therapy. The fragile histidine triad (FHIT) gene has been identified in a region at chromosome 3p14.2, which is deleted in many tumors, including esophageal cancer. Previous studies have shown frequent biallelic alterations of the FHIT gene in numerous tumors, and have demonstrated a tumor ...

2015
Anna M. Wojdyła-Mamoń Andrzej Guranowski

Fhits (fragile histidine triad proteins) occur in eukaryotes but their function is largely unknown, although human Fhit is believed to act as a tumour suppressor. Fhits also exhibit dinucleoside triphosphatase, adenylylsulfatase and nucleoside phosphoramidase activities that in each case yield nucleoside 5'-monophosphate as a product. Due to the dinucleoside triphosphatase activity, Fhits may a...

Journal: :Cancer research 2003
Cinzia Sevignani George A Calin Rossano Cesari Manuela Sarti Hideshi Ishii Sai Yendamuri Andrea Vecchione Francesco Trapasso Carlo M Croce

The fragile histidine triad (FHIT) gene at chromosome 3p14.2 is a tumor suppressor gene that is altered mainly by deletion in a large fraction of human tumors, including breast cancers. To evaluate the potential of FHIT gene therapy in this type of cancer, we have studied the biological effects of adenoviral FHIT transduction (Ad-FHIT) in breast cancer cell lines. The results showed that, after...

2015
ZHIWEI CHANG WEIJIE ZHANG ZHIJUN CHANG MIN SONG YANRU QIN FUBAO CHANG HAIYUN GUO QINGLI WEI

The aim of the present study was to determine the changes to the expression levels of fragile histidine triad (FHIT), breast cancer type 2 susceptibility protein (BRCA2), MutL homolog 1 (MLH1) and tumour protein 53 (p53) exhibited by families with a history of oesophageal cancer in a region that has a high incidence of oesophageal cancer, and to determine the association of these changes with t...

Journal: :Cell cycle 2014
Jennifer A Boylston Charles Brenner

Fragile histidine triad (FHIT) gene deletions are among the earliest and most frequent events in carcinogenesis, particularly in carcinogen-exposed tissues. Though FHIT has been established as an authentic tumor suppressor, the mechanism underlying tumor suppression remains opaque. Most experiments designed to clarify FHIT function have analyzed the consequence of re-expressing FHIT in FHIT-neg...

Journal: :Journal of the National Cancer Institute 1998
G A Otterson G H Xiao J Geradts F Jin W D Chen W Niklinska F J Kaye R S Yeung

BACKGROUND The fragile histidine triad (FHIT) gene at chromosome 3p14.2 has been proposed to be a candidate tumor suppressor gene in human cancers. To test whether FHIT exhibits the functional properties of a tumor suppressor gene, we studied the expression of its protein (pFHIT) in human carcinoma cells and examined the ability of FHIT to inhibit the neoplastic phenotype of cancer cells. MET...

Journal: :Cancer research 1997
D L Greenspan D C Connolly R Wu R Y Lei J T Vogelstein Y T Kim J E Mok N Muñoz F X Bosch K Shah K R Cho

Allelic deletions involving the short arm of chromosome 3 (3p13-21.1) have been observed frequently in cervical carcinomas. Recently, a candidate tumor suppressor gene, FHIT (Fragile Histidine Triad), was cloned and mapped to this chromosomal region (3p14.2). Abnormal FHIT transcripts have been identified previously in a variety of tumor cell lines and primary carcinomas, although their signifi...

2014
Ameneh Eslamparast Mohammad Hossein Ghahremani Soroush Sardari

BACKGROUND Fragile Histidine Triad protein (FHIT), as a known tumor suppressor protein, has been proposed to play crucial role in inhibiting p53 degradation by MDM2. Studies have confirmed FHIT interaction with p53 or MDM2, although functional interacting domains of FHIT with MDM2 and/or p53 are not completely defined. Thus, through determining the significant structural interacting domains of ...

Journal: :Acta crystallographica. Section D, Biological crystallography 2004
Katherine E McAuley Allan Svendsen Shamkant A Patkar Keith S Wilson

The crystallographic structure of feruloyl esterase from Aspergillus niger has been determined to a resolution of 1.5 A by molecular replacement. The protein has an alpha/beta-hydrolase structure with a Ser-His-Asp catalytic triad; the overall fold of the protein is very similar to that of the fungal lipases. The structure of the enzyme-product complex was determined to a resolution of 1.08 A a...

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