Dielectric properties, electrical modulus and current transport mechanisms of Au/ZnO/n-Si structures

Au/Zn O/n-Si(MIS)structures were fabricated by using the RF sputtering method and their complex dielectric constant(ε~*=ε’-jε’’),electric modulus(M~*=M′+j M’’)and electrical conductivity(σ=σ_(dc)+σ_(ac))values were investigated as a function of frequency(0.7 k Hz-1 MHz)and voltage(-6–(+6 V))by capacitance-voltage(C-V)and conductance-voltage(G/ω-V)measurements to get more information on the conduction mechanisms and formation of barrier height between Au and n-Si.The lnσ-Lnf plots have two different regions corresponding to low-intermediate and high frequencies.Such behavior of lnσ-lnf plots shows that the existence of two different conduction mechanisms(CMs)at low-intermediate and high frequencies.Moreover,the reverse bias saturation current(I_o),ideality factor(n),barrier height(Φ_(Bo))were determined from the forward bias I-V data and they were found as a strong function of temperature.The value of n especially at low temperature is considerably higher than unity.The values ofΦ_(B0)and standard deviation(σ_s)were found from the intercept and slope ofΦ_(Bo)-q/2k T plots as 0.551 e V and 0.075 V for the region I(80–220 K)and 1.126 e V and 0.053 V for the region II(220–400 K),respectively.The values ofΦ_(Bo)and effective Richardson constant(A~*)were found from slope and intercept of activation energy plots as 0.564 e V and 101.084 Acm~(-2)K~(-2)for the region I and 1.136 e V and41.87 Acm~(-2)K~(-2)for the region II,respectively.These results confirm that the current-voltage-temperature(I-V-T)characteristics of the fabricated Au/Zn O/n-Si SBDs can satisfactorily be explained on the basis of TE theory with double GD of the BHs.     

BRCA1 regulates the G2/M checkpoint by activating Chk1 kinase upon DNA damage

The breast cancer tumor-suppressor gene, BRCA1, encodes a protein with a BRCT domain-a motif that is found in many proteins that are implicated in DNA damage response and in genome stability. Phosphorylation of BRCA1 by the DNA damage-response proteins ATM, ATR and hCds1/Chk2 changes in response to DNA damage and at replication-block checkpoints. Although cells that lack BRCA1 have an abnormal response to DNA damage, the exact role of BRCA1 in this process has remained unclear. Here we show that BRCA1 is essential for activating the Chk1 kinase that regulates DNA damage-induced G2/M arrest. Thus, BRCA1 controls the expression, phosphorylation and cellular localization of Cdc25C and Cdc2/cyclin B kinase-proteins that are crucial for the G2/M transition. We show that BRCA1 regulates the expression of both Wee1 kinase, an inhibitor of Cdc2/cyclin B kinase, and the 14-3-3 family of proteins that sequesters phosphorylated Cdc25C and Cdc2/cyclin B kinase in the cytoplasm. We conclude that BRCA1 regulates key effectors that control the G2/M checkpoint and is therefore involved in regulating the onset of mitosis.     

Structure of the receptor for platelet-derived growth factor helps define a family of closely related growth factor receptors

The primary structure of the receptor for platelet-derived growth factor (PDGF), determined by means of cloning a cDNA that encodes the murine pre-PDGF receptor, is closely related to that of the v-kit oncogene product and the receptor for macrophage colony stimulating factor (CSF-1). Common structural features include the presence of long sequences that interrupt the tyrosine-specific protein kinase domains of each molecule. The PDGF and CSF-1 receptors also share a characteristic distribution of extracellular cysteine residues. Ubiquitin is covalently bound to the purified PDGF receptor, the human gene for which is on chromosome 5.     

Human epidermal growth factor receptor cDNA sequence and aberrant expression of the amplified gene in A431 epidermoid carcinoma cells

The complete 1,210-amino acid sequence of the human epidermal growth factor (EGF) receptor precursor, deduced from cDNA clones derived from placental and A431 carcinoma cells, reveals close similarity between the entire predicted v-erb-B mRNA oncogene product and the receptor transmembrane and cytoplasmic domains. A single transmembrane region of 23 amino acids separates the extracellular EGF binding and cytoplasmic domains. The receptor gene is amplified and apparently rearranged in A431 cells, generating a truncated 2.8-kilobase mRNA which encodes only the extracellular EGF binding domain.     

Close similarity of epidermal growth factor receptor and v-erb-B oncogene protein sequences

Each of six peptides derived from the human epidermal growth factor (EGF) receptor very closely matches a part of the deduced sequence of the v-erb-B transforming protein of avian erythroblastosis virus (AEV). In all, the peptides contain 83 amino acid residues, 74 of which are shared with v-erb-B. The AEV progenitor may have acquired the cellular gene sequences of a truncated EGF receptor (or closely related protein) lacking the external EGF-binding domain but retaining the transmembrane domain and a domain involved in stimulating cell proliferation. Transformation of cells by AEV may result, in part, from the inappropriate acquisition of a truncated EGF receptor from the c-erb-B gene.