BIAcore for macromolecular interaction

Fivash, Matthew J.; Towler, Eric M.; Fisher, Robert J.

doi:10.1016/s0958-1669(98)80091-8

Cited by 193 publications

(106 citation statements)

References 30 publications

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“…The refractive index is directly related to the mass concentration in the surface layer and increases when the analyte binds to the immobilized ligand. [46][47][48] BIA experiments are performed under continuous, precisely controlled flow conditions, using the microfluid system of a BIAcore 2000 (Pharmacia Biosensor). The ligand is covalently bound or captured by affinity on a matrix present on the sensor chip.…”

Section: Methodsmentioning

confidence: 99%

Hepatitis C virus core protein binds to apolipoprotein AII and its secretion is modulated by fibrates

et al. 1999

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Hepatitis C virus (HCV) is the major etiologic agent of post-transfusion and sporadic non-A, non-B hepatitis. 1 Persistent HCV infection, which develops in at least 70% to 80% of infected patients, often progresses to chronic hepatitis and is highly correlated with the development of cirrhosis and hepatocellular carcinoma. 2-4 Neither a vaccine, nor effective therapy are currently available for HCV, other than interferon alfa combined with ribavirin. 5,6

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Section: Methodsmentioning

confidence: 99%

Hepatitis C virus core protein binds to apolipoprotein AII and its secretion is modulated by fibrates

et al. 1999

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“…We used surface plasmon resonance (48,49) to investigate the dynamics of Smad-TFE3 complex formation and dissociation at the PE2.1 element. To examine the dynamics of Smad binding to DNA, a biotinylated oligonucleotide containing the PE2.1 element was immobilized on a streptavidin-coated sensor chip and different concentrations of Smad3 or Smad4 were applied to the flow chamber (Fig.…”

Section: Fig 2 Analysis Of the Protein Domains Required For Smad-tfmentioning

confidence: 99%

Both Max and TFE3 Cooperate with Smad Proteins to Bind the Plasminogen Activator Inhibitor-1 Promoter, but They Have Opposite Effects on Transcriptional Activity

Grinberg¹,

Kerppola²

2003

Journal of Biological Chemistry

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“…It can monitor and quantitative the kinetics of binding and dissociation constants between molecules in real-time and without labels. [31][32][33] We utilized the BIACORE system to quantitate differential binding and dissociation constants between the peptide and mutant and wt p53.…”

mentioning

confidence: 99%

Selective induction of apoptosis through the FADD/caspase‐8 pathway by a p53 c‐terminal peptide in human pre‐malignant and malignant cells

Mao

Rosal

et al. 2005

Intl Journal of Cancer

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A p53 C-terminal peptide (aa 361-382, p53p), fused at its Cterminus to the minimal carrier peptide of antennapedia (17 aa, Ant; p53p-Ant), induced rapid apoptosis in human cancer cells, via activation of the Fas pathway. We examined p53p-Ant mechanism of action, toxicity in various human normal, non-malignant, pre-malignant and malignant cancer cells and investigated its biophysical characteristics. p53p-Ant selectively induced cell death in only pre-malignant or malignant cells in a p53-dependent manner and was not toxic to normal and non-malignant cells. p53p-Ant was more toxic to the mutant p53 than wild-type p53 phenotype in H1299 lung cancer cells stably expressing human temperature-sensitive p53 mutant 143Ala. Surface plasmon resonance (BIACORE) analysis demonstrated that this peptide had higher binding affinity to mutant p53 as compared to wild-type p53. p53p-Ant induced-cell death had the classical morphological characteristics of apoptosis and had no features of necrosis. The The p53 tumor suppressor gene is one of the most commonly mutated genes found in human malignancies. 1 More than 50% of human tumors, including breast cancers, are associated with missense mutations or deletions of p53 and most of the missense mutations map to the DNA-binding domain of the protein. 2,3 p53 protein functions in the transcription of growth inhibiting genes, apoptosis, cell cycle arrest and DNA repair. 4 -6 p53 is a sequencespecific transcription factor that transactivates a number of genes whose products are involved in cell growth regulation. These include p21 (a cyclin-dependent kinase inhibitor known to arrest the cell cycle mainly in G1/S phase), GADD45 for DNA repair and Bax and Fas/APO-1 for apoptosis. 7-11 p53 induced Fas-FADD binding and transiently sensitized cells to Fas-induced apoptosis. 12 Programmed cell death depends on conserved structural moieties that transmit and regulate the death signal. This is most evident in death receptors of the tumor necrosis factor receptor (TNF-R) super-family. The intracellular regions of the Fas/CD95 and TNFR1 death receptors have a moderately well conserved NH2-region of about 80 residues that is required for death signalling and has been called the 'death domain' (DD). 13,14 Fas/CD95 induces rapid apoptosis upon binding to Fas ligand through the autocrine/paracrine signalling pathway. 15 When activated, the intracellular death domain in Fas/CD95 binds to FADD/MORT-1 at its C-terminus, which then recruits caspase-8 to FADD. A member of the TNF ligand family identified more recently is TNF-related apoptosis-inducing ligand (TRAIL). TRAIL shows high homology to Fas Ligand and binds to the TRAIL receptor family. TRAILinduced caspase activation shares many of same caspases involved in Fas/CD95 and TNF-induced cell death mechanisms. 16 FADD/ MORT-1 is a cytosolic adaptor protein, which is critical for signalling from Fas/APO-1 and other TNF-R family members. 17 Two protein interaction domains have been identified in FADD/ MORT-1. The C-terminal 'death domain' is needed for ...

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BIAcore for macromolecular interaction

Cited by 193 publications

References 30 publications

Hepatitis C virus core protein binds to apolipoprotein AII and its secretion is modulated by fibrates

Hepatitis C virus core protein binds to apolipoprotein AII and its secretion is modulated by fibrates

Both Max and TFE3 Cooperate with Smad Proteins to Bind the Plasminogen Activator Inhibitor-1 Promoter, but They Have Opposite Effects on Transcriptional Activity

Selective induction of apoptosis through the FADD/caspase‐8 pathway by a p53 c‐terminal peptide in human pre‐malignant and malignant cells

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