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Exploring thermal signatures in the experimentally heated CM carbonaceous chondrite Allan Hills 83100
Comparison of the meteorology and surface energy balance at Storbreen and Midtdalsbreen, two glaciers in southern Norway
We compare 5 years of meteorological records from automatic weather stations (AWSs) on Storbreen and Midtdalsbreen, two glaciers in southern Norway, located approximately 120 km apart. The records are obtained from identical AWSs with an altitude difference of 120 m and cover the period September 2001 to September 2006. Air temperature at the AWS locations is found to be highly correlated, even with the seasonal cycle removed. The most striking difference between the two sites is the difference in wind climate. Midtdalsbreen is much more under influence of the large-scale circulation with wind speeds on average a factor 1.75 higher. On Storbreen, weaker katabatic winds are dominant. The main melt season is from May to September at both locations. During the melt season, incoming and net solar radiation are larger on Midtdalsbreen, whereas incoming and net longwave radiation are larger on Storbreen, primarily caused by thicker clouds on the latter. The turbulent fluxes are a factor 1.7 larger on Midtdalsbreen, mainly due to the higher wind speeds. Inter-daily fluctuations in the surface energy fluxes are very similar at the AWS sites. On average, melt energy is a factor 1.3 larger on Midtdalsbreen, a result of both larger net radiation and larger turbulent fluxes. The relative contribution of net radiation to surface melt is larger on Storbreen (76%) than on Midtdalsbreen (66%). As winter snow depth at the two locations is comparable in most years, the larger amount of melt energy results in an earlier disappearance of the snowpack on Midtdalsbreen and 70% more ice melt than on Storbreen. We compare the relative and absolute values of the energy fluxes on Storbreen and Midtdalsbreen with reported values for glaciers at similar latitudes. Furthermore, a comparison is made with meteorological variables measured at two nearby weather stations, showing that on-site measurements are essential for an accurate calculation of the surface energy balance and melt rate
PALB2 (partner and localizer of BRCA2)
PALB2 (Partner and Localizer of BRCA2) was first identified as a BRCA2-interacting protein. Subsequently, PALB2 has been recognized as a cog in the cellular machinery for DNA repair by homologous recombination (HR). PALB2 also mediates S and G2 DNA damage checkpoints, and has an apparent function in protecting transcriptionally active genes from genotoxic stress. PALB2 also interacts with, is localized by, and functions downstream of BRCA1. Further, PALB2 interacts with other essential effector
Observation of the Decay B^-→D_s^((*)+)K^-ℓ^-ν̅ _ℓ
We report the observation of the decay B^- → D_s^((*)+)K^-ℓ^-ν̅ _ℓ based on 342  fb^(-1) of data collected at the Υ(4S) resonance with the BABAR detector at the PEP-II e^+e^- storage rings at SLAC. A simultaneous fit to three D_s^+ decay chains is performed to extract the signal yield from measurements of the squared missing mass in the B meson decay. We observe the decay B^- → D_s^((*)+)K^-ℓ^-ν̅ _ℓ with a significance greater than 5 standard deviations (including systematic uncertainties) and measure its branching fraction to be B(B^- → D_s^((*)+)K^-ℓ^-ν̅ _ℓ)=[6.13_(-1.03)^(+1.04)(stat)±0.43(syst)±0.51(B(D_s))]×10^(-4), where the last error reflects the limited knowledge of the D_s branching fractions
XRCC2 (X-ray repair cross complementing 2)
XRCC2 is one of five somatic RAD51 paralogs, all of which have Walker A and B ATPase motifs. Each of the paralogs, including XRCC2, has a function in DNA double-strand break repair by homologous recombination (HR). However, their individual roles are not as well understood as that of RAD51 itself. The XRCC2 protein forms a complex (BCDX2) with three other RAD51 paralogs, RAD51B, RAD51C and RAD51D. It is believed that the BCDX2 complex mediates HR downstream of BRCA2 but upstream of RAD51, as XRCC2 is involved in the assembly of RAD51 into DNA damage foci. XRCC2 can bind DNA and, along with RAD51D, can promote homologous pairing in vitro. Consistent with its role in HR, XRCC2-deficient cells have increased levels of spontaneous chromosome instability, and exhibit hypersensitivity to DNA interstrand crosslinking agents such as mitomycin C and cisplatin as well as ionizing radiation, alkylating agents and aldehydes. XRCC2 also functions in promoting DNA replication and chromosome segregation. Biallelic mutation of XRCC2 (FANCU) causes the FA-U subtype of FA, while heterozygosity for deleterious mutations in XRCC2 may be associated with an increased breast cancer risk. XRCC2 appears to function 'downstream' in the FA pathway, since it is not required for FANCD2 monoubiquitination, which is the central step in the FA pathway. Clinically, the only known FA-U patient in the world exhibits severe congenital abnormalities, but had not developed, by seven years of age, the bone marrow failure and cancer that are often seen in patients from other FA complementation groups
BREAST CANCER-ASSOCIATED MISSENSE MUTANTS OF THE PALB2 WD40 DOMAIN, WHICH DIRECTLY BINDS RAD51C, RAD51 AND BRCA2, DISRUPT DNA REPAIR
Heterozygous carriers of germ-line mutations in the BRCA2/FANCD1, PALB2/FANCN, and RAD51C/FANCO DNA repair genes have an increased life-time risk to develop breast, ovarian and other cancers; bi-allelic mutations in these genes clinically manifest as Fanconi anemia (FA). Here, we demonstrate that RAD51C is part of a novel protein complex that contains PALB2 and BRCA2. Further, the PALB2 WD40 domain can directly and independently bind RAD51C and BRCA2. To understand the role of these homologous recombination (HR) proteins in DNA repair, we functionally characterize effects of missense mutations of the PALB2 WD40 domain that have been reported in breast cancer patients. In contrast to large truncations of PALB2, which display a complete loss of interaction, the L939W, T1030I, and L1143P missense mutants/variants of PALB2 WD40 domain are associated with altered direct binding patterns to the RAD51C, RAD51 and BRCA2 HR proteins in biochemical assays. Further, the T1030I missense mutant is unstable, while the L939W and L1143P proteins are stable but partially disrupt the PALB2-RAD51C-BRCA2 complex in cells. Functionally, the L939W and L1143P mutants display a decreased capacity for DNA double-strand break-induced HR and an increased cellular sensitivity to ionizing radiation. As further evidence for the functional importance of the HR complex, RAD51C mutants that are associated with cancer susceptibility and FA also display decreased complex formation with PALB2. Together, our results suggest that three different cancer susceptibility and FA proteins function in a DNA repair pathway based upon the PALB2 WD40 domain binding to RAD51C and BRCA2
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