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E J Hill

Publications and source records attributed to E J Hill.

At least 19 recordsLinked to original sources
PubMed2006

Measurement of branching fractions and charge asymmetries in B decays to an eta meson and a K* meson.

We present measurements of branching fractions and charge asymmetries for the decays B-->etaK*, where K* indicates a spin 0, 1, or 2 Kpi system. The data sample corresponds to 344x10(6) BB pairs collected with the BABAR detector at the PEP-II asymmetric-energy e+ e- collider at SLAC. We measure the branching fractions (in units of 10(-6): B(B0-->etaK*0(892))=16.5+/-1.1+/-0.8, B(B+-->etaK*+(892))=18.9+/-1.8+/-1.3, B(B0-->eta(Kpi)0*0)=11.0+/-1.6+/-1.5, B(B+-->eta(Kpi)0*+)=18.2+/-2.6+/-2.6, B(B0-->etaK2*0(1430))=9.6+/-1.8+/-1.1, and B(B+-->etaK2*+(1430))=9.1+/-2.7+/-1.4. We also determine the charge asymmetries for all decay modes.

Journal Article↗
PubMed2006

Observation of B+ --> K0K+ and B0 --> K0K0.

We report observations of the b --> d penguin-dominated decays B+ --> K0K+ and B0 --> K0K0 in 316 fb(-1) of e+ e- collision data collected with the BABAR detector. We measure the branching fractions B(B+ --> K0K+) = (1.61+/-0.44+/-0.09) x 10(-6) and B(B0 --> K0K0 = (1.08+/-0.28+/-0.11) x 10(-6) and the CP-violating charge asymmetry A(CP)(K0K+) = 0.10+/-0.26+/-0.03. Using a vertexing technique previously employed in several analyses of all-neutral final states containing kaons, we report the first measurement of time-dependent CP-violating asymmetries in B0 --> K(S)0K(S)0, obtaining S = -1.28(-0.73-0.16)(+0.80+0.11) and C = -0.40+/-0.41+/-0.06. We also report improved measurements of the branching fraction B(B+ --> K0 pi+) = (23.9+/-1.1+/-1.0) x 10(-6) and CP-violating charge asymmetry A(CP)(K0 pi+) = -0.029+/-0.039+/-0.010.

Journal Article↗
PubMed2004

Search for the radiative decays B-->rhogamma and B0-->omegagamma.

A search of the exclusive radiative decays B-->rho(770)gamma and B0-->omega(782)gamma is performed on a sample of about 84x10(6) BBmacr; events collected by the BABAR detector at the SLAC PEP-II asymmetric-energy e+e- storage ring. No significant signal is seen in any of the channels. We set upper limits on the branching fractions B of B(B0-->rho(0)gamma)<1.2 x 10(-6), B(B+-->rho+gamma)<2.1 x 10(-6), and B(B0-->omegagamma)<1.0 x 10(-6) at 90% confidence level (C.L.). Using the assumption that Gamma(B-->rhogamma)=Gamma(B+-->rho(+)gamma)=2 x Gamma(B0-->rho(0)gamma), we find the combined limit B(B-->rhogamma)<1.9 x 10(-6), corresponding to B(B-->rhogamma)/B(B-->K*gamma)<0.047 at 90% C.L.

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PubMed2003

Search for D0-D(-)0 mixing and a measurement of the doubly Cabibbo-suppressed decay rate in D0-->Kpi decays.

We present results of a search for D0-D(-)0 mixing and a measurement of R(D), the ratio of doubly Cabibbo-suppressed decays to Cabibbo-favored decays, using D0-->K+pi- decays from 57.1 fb(-1) of data collected near sqrt[s]=10.6 GeV with the BABAR detector at the PEP-II collider. At the 95% confidence level, allowing for CP violation, we find the mixing parameters x('2)<0.0022 and -0.056<y(')<0.039, and the mixing rate R(M)<0.16%. In the limit of no mixing, R(D)=[0.357+/-0.022(stat)+/-0.027(syst)]% and the CP-violating asymmetry A(D)=0.095+/-0.061(stat)+/-0.083(syst).

Journal Article↗
PubMed2003

Measurements of CP-violating asymmetries and branching fractions in B meson decays to eta'K.

We present measurements of the branching fractions of the decays B+-->eta'K+ and B0-->eta'K0. For B0-->eta(')K(0)(S) we also measure the time-dependent CP-violation parameters S eta'(K(0)(S)) and C eta'(K(0)(S)), and for B+-->eta'K+ the time-integrated charge asymmetry A(ch). The data sample corresponds to 88.9 x 10(6) BB pairs produced by e(+)e(-) annihilation at the Upsilon(4S). The results are B(B+-->eta'K+)=(76.9+/-3.5+/-4.4) x 10(-6), B(B0-->eta'K0)=(60.6+/-5.6+/-4.6) x 10(-6), S eta'(K(0)(S))=0.02+/-0.34+/-0.03, C eta'(K(0)(S))=0.10+/-0.22+/-0.04, and A(ch)=0.037+/-0.045+/-0.011.

Journal Article↗
PubMed2003

Study of time-dependent CP asymmetry in neutral B decays to J/psi pi0.

We present the first study of the time-dependent CP-violating asymmetry in B0-->J/psi pi(0) decays using e(+)e(-) annihilation data collected with the BABAR detector at the Upsilon(4S) resonance during the years 1999-2002 at the PEP-II asymmetric-energy B Factory at SLAC. Using approximately 88 x 10(6) BB; pairs, our results for the coefficients of the cosine and sine terms of the CP asymmetry are C(J/psi pi(0))=0.38+/-0.41(stat)+/-0.09(syst) and S(J/psi pi(0))=0.05+/-0.49(stat)+/-0.16(syst).

Journal Article↗
PubMed2003

Measurements of the branching fractions and bounds on the charge asymmetries of charmless three-body charged B decays.

We present measurements of branching fractions and charge asymmetries for charmless B-meson decays to three-body final states of charged pions and kaons. The analysis uses 81.8 fb(-1) of data collected at the Upsilon(4S) resonance with the BABAR detector at the SLAC PEP-II asymmetric B Factory. We measure the branching fractions B(B+-->pi(+)pi(-)pi(+))=(10.9+/-3.3+/-1.6)x10(-6), B(B+-->K+pi(-)pi(+))=(59.1+/-3.8+/-3.2)x10(-6), and B(B+-->K+K-K+)=(29.6+/-2.1+/-1.6)x10(-6) and provide 90% C.L. upper limits for other decays. We observe no charge asymmetries for these modes.

Journal Article↗
PubMed2003

Observation of the decay B+/--->pi+/-pi0, study of B+/--->K+/-pi0, and search for B0-->pi0pi0.

We present results for the branching fractions and charge asymmetries in B+/--->h(+/-)pi(0) (where h(+/-)=pi(+/-),K+/-) and a search for the decay B0-->pi(0)pi(0) using a sample of approximately 88 x 10(6) BBmacr; pairs collected by the BABAR detector at the PEP-II asymmetric-energy B Factory at SLAC. We measure B(B+/--->pi(+/-)pi(0))=(5.5(+1.0)(-0.9)+/-0.6)x10(-6), where the first error is statistical and the second is systematic. The B+/--->pi(+/-)pi(0) signal has a significance of 7.7sigma including systematic uncertainties. We simultaneously measure the K+/-pi(0) branching fraction to be B(B+/--->K+/-pi(0))=(12.8(+1.2)(-1.1)+/-1.0)x10(-6). The charge asymmetries are Api(+/-)(pi(0))=-0.03(+0.18)(-0.17)+/-0.02 and AK+/-(pi(0))=-0.09+/-0.09+/-0.01. We place a 90% confidence-level upper limit on the branching fraction B(B0-->pi(0)pi(0)) of 3.6 x 10(-6).

Journal Article↗
PubMed2003

Evidence for B+-->J/psip(-)Lambda; and search for B0-->J/psip(-)p.

We have performed a search for the decays B+-->J/psip(-)Lambda; and search for B0-->J/psip(-)p. in a data set of (88.9+/-1.0) x 10(6) Upsilon(4S) decays collected by the BABAR experiment at the PEP-II e(+)e(-) storage ring at the Stanford Linear Accelerator Center. Four charged B candidates have been observed with an expected background of 0.21+/-0.14 events. The corresponding branching fraction is (12(+9)(-6)) x 10(-6), where statistical and systematic uncertainties have been combined. The result can be interpreted as a 90% confidence level (C.L.) upper limit of 26 x 10(-6). We also find one B0 candidate, with an expected background of 0.64+/-0.17 events, implying a 90% C.L. upper limit of 1.9 x 10(-6).

Journal Article↗
PubMed2003

Measurement of the branching fraction, and bounds on the CP-violating asymmetries, of neutral B decays to D*+/- D-/+.

We present measurements of the branching fraction and CP-violating asymmetries for neutral B decays to D(*+/-)D-/+. The measurement uses a data sample of approximately 88x10(6) Upsilon(4S)-->BBmacr; decays collected with the BABAR detector at the SLAC PEP-II asymmetric-energy e(+)-e(-) collider. By fully reconstructing the D(*+/-)D-/+ decay products, we measure the branching fraction to be (8.8+/-1.0+/-1.3)x10(-4) and the time-integrated CP-violating asymmetry between the rates to D(*-)D+ and D(*+)D- to be A=-0.03+/-0.11+/-0.05. We also measure the time-dependent CP-violating asymmetry parameters to be S(-+)=-0.24+/-0.69+/-0.12, C(-+)=-0.22+/-0.37+/-0.10 for B-->D(*-)D+ and S(+-)=-0.82+/-0.75+/-0.14, C(+-)=-0.47+/-0.40+/-0.12 for B-->D(*+)D-. In each case, the first error is statistical and the second error is systematic.

Journal Article↗
PubMed2003

Study of the rare decays B0-->D((*)+)(s)pi(-) and B0-->D((*)-)(s)K+.

We report evidence for the decays B0-->D(+)(s)pi(-) and B0-->D(-)(s)K+ and the results of a search for B0-->D(*+)(s)pi(-) and B0-->D(*-)(s)K+ in a sample of 84 x 10(6) upsilon(4S) decays into BB pairs collected with the BABAR detector at the PEP-II asymmetric-energy e(+)e(-) storage ring. We measure the branching fractions B(B0-->D(+)(s)pi(-))=[3.2+/-0.9(stat)+/-1.0(syst)] x 10(-5) and B(B0-->D(-)(s)K+)=[3.2+/-1.0(stat)+/-1.0(syst)] x 10(-5). We also set 90% C.L. limits B(B0-->D(*+)(s)pi(-))<4.1 x 10(-5) and B(B0-->D(*-)(s)K+)<2.5 x 10(-5).

Journal Article↗
PubMed2002

Measurements of branching fractions and CP-violating asymmetries in B0-->pi+pi-, K+pi-, K+K- decays.

We present measurements of branching fractions and CP-violating asymmetries for two-body neutral B meson decays to charged pions and kaons based on a sample of about 88x10(6) Upsilon(4S)-->BB decays. From a time-independent fit we measure the charge-averaged branching fractions B(B0-->pi+pi-)=(4.7+/-0.6+/-0.2)x10(-6), B(B0-->K+pi-)=(17.9+/-0.9+/-0.7)x10(-6), and the direct CP-violating charge asymmetry A(Kpi)=-0.102+/-0.050+/-0.016 [-0.188,-0.016], where the ranges in square brackets indicate the 90% confidence intervals. From a time-dependent fit we measure the B0-->pi+pi- CP-violating parameters S(pipi)=0.02+/-0.34+/-0.05 [-0.54,+0.58] and C(pipi)=-0.30+/-0.25+/-0.04 [-0.72,+0.12].

Journal Article↗
PubMed2002

Measurement of the CP asymmetry amplitude sin2beta with B0 mesons.

We present results on time-dependent CP asymmetries in neutral B decays to several CP eigenstates. The measurements use a data sample of about 88 x 10(6) Upsilon(4S)-->B(-)B decays collected between 1999 and 2002 with the BABAR detector at the PEP-II asymmetric-energy B factory at SLAC. We study events in which one neutral B meson is fully reconstructed in a final state containing a charmonium meson and the other B meson is determined to be either a B(0) or B(-0) from its decay products. The amplitude of the CP asymmetry, which in the standard model is proportional to sin2beta, is derived from the decay-time distributions in such events. We measure sin2beta=0.741+/-0.067(stat)+/-0.034(syst) and |lambda|=0.948+/-0.051(stat)+/-0.030(syst). The magnitude of lambda is consistent with unity, in agreement with the standard model expectation of no direct CP violation in these modes.

Journal Article↗
PubMed1987

Interactions of vitamin E and penicillamine in the treatment of hereditary avian muscular dystrophy.

Our prior work demonstrated that penicillamine treatment of dystrophic chickens delayed the onset of symptoms, partially alleviated contractures, improved muscle function, and lowered serum creatine kinase. Penicillamine, a sulfhydryl compound with reducing properties, also prevented inactivation of glycolytic enzymes by protecting thiol groups. The present study shows that vitamin E enhances the therapeutic effects of penicillamine. Interaction of these two reductants is dose related. With vitamin E as adjunct therapy, the dosage level of penicillamine could be lowered by 50%, thereby minimizing side effects. The therapeutic rationale for two antioxidants is that penicillamine may act primarily in the cytoplasm to prevent oxidative damage, whereas the more hydrophobic vitamin E may protect membrane bilayers. Additionally, penicillamine may prevent collagen cross-linking and, deposition of insoluble collagen in muscle and thus decrease contracture formation. General applications of combined penicillamine and vitamin E therapy are discussed regarding prevention of free radical and oxidative damage in Duchenne dystrophy and a wide range of human diseases.

Animals↗
PubMed1979

Mechanism of action of penicillamine in the treatment of avian muscular dystrophy.

Penicillamine, a cysteine analog with a reduced sulfhydryl group, has been used in this laboratory for the treatment of hereditary avian dystrophy. The drug delays the onset of symptoms and alleviates the debilitating aspects of the disease. To study the mechanism of drug action, the effects of penicillamine on white and red muscles of dystrophic chickens were examined with regard to the specific activities of the soluble enzymes glyceraldehyde-3-phosphate dehydrogenase, acetylphosphatase, glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, glutathione reductase, glutathione preoxidase, superoxide dismutase, and catalase. The sulfhydryl contents of the soluble proteins and the concentration of myoglobin were also determined. In white dystrophic muscle (pectoral), there were large alterations in the various enzymatic activities compared to normal levels. In the DISCUSSION, these changes are related to the pathogenesis of the disease and to the adaptive response for protection of the severely affected fast fibers. Red dystrophic muscles (thigh) were minimally involved, in accordance with the known sparing action of the slow fiber type. The results suggested that the disease process in dystrophic muscle may be due to oxidation of the essential sulfhydryl groups of proteins. Penicillamine may produce therapeutic effects by altering the intracellular redox status, thereby promoting better regulation of enzymatic activity, membrane stability, and improved muscle function.

Animals↗
PubMed1976

Enzymological studies on hereditary avian muscular dystrophy.

White and red muscles of normal and genetically dystrophic chickens were compared with regards to activity levels of three soluble enzymes, glyceraldehyde-3-phosphate dehydrogenase, creatine phosphokinase, and acetyl phosphatase. In dystrophic white muscle (pectoral), activity of the two sulfhydryl enzymes, glyceraldehyde-3-phosphate dehydrogenase and creatine phosphokinase, was preferentially lost from the sarcoplasm resulting in decreased specific activities. By contrast, acetyl phosphatase was preferentially retained and showed increased specific activity. Dystrophic white muscle had decreased sulfhydryl content in the soluble proteins, severe reduction in muscle mass, fatty infiltration, and fragmentation of fibers. Red dystrophic muscles (thigh) were minimally involved in accordance with the known sparing of red fibers. Enzyme activities were correlated with histological observations. The results suggested that the disease process in dystrophic white muscle may be related to alterations in the sulfhydryl groups of proteins. The data are correlated with the beneficial effects of our treatment of hereditary avian dystrophy with the sulfhydryl compound, penicillamine (Chou, T.H., Hill, E.J., Bartle, E., Woolley, K., LeQuire, V., Olson, W., Roelofs, R., and Park, J.H. (1975) J. Clin. Invest. 56, 842-849).

Animals↗
PubMed1975

Covalent binding of 3-pyridinealdehyde nicotinamide adenine dinucleotide and substrate to glyceraldehyde 3-phosphate dehydrogenase.

Glyceraldehyde 3-phosphate dehydrogenase (D-glyceraldehyde-3-phoshate:nicotinamide adenine dinucleotide oxidoreductase (phosphorylating), EC 1.2.1.12) forms a complex with 3-pyridinealdehyde-NAD which survives precipitation with 7% perchloric acid. The molar ratio bound 3-pyridinealdehyde-NAD to the enzyme is 2.5 to 2.9. Lactate, malate, and alcohol dehydrogenases do not form acid-precipitable complexes with 3-pyridinealdehyde-NAD. 3-Pyridinealdehyde-deamino-NAD or glyceraldehyde 3-phosphate also forms an acid-stable complex with glyceraldehyde 3-phosphate dehydrogenase; however, NAD, 3-acetylpyridine-NAD, or thionicotinamide-NAD does not produce an acid-stable complex. Incubation of the glyceraldehyde 3-phosphate dehydrogenase with glyceraldehyde 3-phosphate, acetyl phosphate, iodoacetic acid, or iodosobenzoate inhibits the formation of the acid-stable complex with 3-pyridinealdehyde-NAD. Glyceraldehyde 3-phosphate or 3-pyridinealdehyde-NAD also prevents carboxymethylation of the active site cysteine-149 by[14-C]iodoacetic acid. These studies indicate that the aldehyde group of 3-pyridinealdehyde-NAD forms a thiohemiacetal linkage with cysteine-149 which is the substrate binding site for the dehydrogenase reaction. These findings may account for the fact that 3-pyridinealdehyde-NAD strongly inhibits the dehydrogenase and esterase activities of 3-pyridinealdehyde-NAD forms a thiohemiacetal linkage with cysteine-149 which is the substrate binding site for the dehydrogenase reaction. These findings may account for the fact that 3-pyridinealdehyde-NAD strongly inhibits the dehydrogenase and esterase activities of glyceraldehyde 3-phosphate dehydrogenase which require reduced cysteine-149. However, the analogue does not inhibit the acetyl phosphates activity of the enzyme for which the active site sulfhydryl residues must be oxidized.

Aldehydes↗