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  • 1
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    Sentencing in Time (2022)
    Amherst College Press | Amherst College Press
    Details
    Publication Date: 2024-02-28
    Description: Exactly how is it we think the ends of justice are accomplished by sentencing someone to a term in prison? How do we relate a quantitative measure of time—months and years—to the objectives of deterring crime, punishing wrongdoers, and accomplishing justice for those touched by a criminal act? Linda Ross Meyer investigates these questions, examining the disconnect between our two basic modes of thinking about time—chronologically (seconds, minutes, hours), or phenomenologically (observing, taking note of, or being aware of the passing of time). In Sentencing in Time, Meyer asks whether—in overlooking the irreconcilability of these two modes of thinking about time—we are failing to accomplish the ends we believe the criminal justice system is designed to serve. Drawing on work in philosophy, legal theory, jurisprudence, and the history of penology, Meyer explores how, rather than condemning prisoners to an experience of time bereft of meaning, we might instead make the experience of incarceration constructively meaningful—and thus better aligned with social objectives of deterring crime, reforming offenders, and restoring justice.
    Keywords: Sentences (Criminal procedure) -- United States. ; Prison sentences -- United States. ; Criminal justice, Administration of -- United States. ; bic Book Industry Communication::L Law::LA Jurisprudence & general issues ; bic Book Industry Communication::L Law::LN Laws of Specific jurisdictions::LNF Criminal law & procedure::LNFX Criminal procedure::LNFX1 Sentencing & punishment ; bic Book Industry Communication::L Law::LN Laws of Specific jurisdictions::LNF Criminal law & procedure::LNFX Criminal procedure
    Language: English
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  • 2
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    Sentencing in Time (2022)
    Amherst College Press
    Details
    Publication Date: 2022-07-15
    Description: Exactly how is it we think the ends of justice are accomplished by sentencing someone to a term in prison? How do we relate a quantitative measure of time—months and years—to the objectives of deterring crime, punishing wrongdoers, and accomplishing justice for those touched by a criminal act? Linda Ross Meyer investigates these questions, examining the disconnect between our two basic modes of thinking about time—chronologically (seconds, minutes, hours), or phenomenologically (observing, taking note of, or being aware of the passing of time). In Sentencing in Time, Meyer asks whether—in overlooking the irreconcilability of these two modes of thinking about time—we are failing to accomplish the ends we believe the criminal justice system is designed to serve. Drawing on work in philosophy, legal theory, jurisprudence, and the history of penology, Meyer explores how, rather than condemning prisoners to an experience of time bereft of meaning, we might instead make the experience of incarceration constructively meaningful—and thus better aligned with social objectives of deterring crime, reforming offenders, and restoring justice.
    Keywords: Jurisprudence & general issues ; bic Book Industry Communication::L Law::LA Jurisprudence & general issues
    Language: English
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    E-BOOK
  • 3
    Electronic Resource
    Electronic Resource
    Hydrothermal synthesis, structure, and sorption properties of the new microporous ferric molybdenum phosphates [(CH3)4N]2(NH4)2[Fe2Mo12O30(H2PO4)6(HPO4)2].nH2O and [(CH3)4N]2Na4[Fe3Mo12O30(HxPO4)8].nH2O (1993)
    s.l. : American Chemical Society
    Inorganic chemistry 32 (1993), S. 1579-1586 
    Details
    ISSN: 1520-510X
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/ic00061a011
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  • 4
    Electronic Resource
    Electronic Resource
    Hydrothermal Synthesis and Structural Characterization of the Two New Vanadium Arsenates H2NC4H8NH2[(VIVO)2(HAsO4)2(H2AsO4)2] and H3NCH2CH2NH3[VIII(HAsO4)2(H2AsO4)].cntdot.H2O (1994)
    s.l. : American Chemical Society
    Chemistry of materials 6 (1994), S. 1463-1464 
    Details
    ISSN: 1520-5002
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/cm00045a001
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  • 5
    Electronic Resource
    Electronic Resource
    The First Octahedral-Trigonal Bipyramidal-Tetrahedral Framework Oxide: Hydrothermal Synthesis and Structure of K[Ni(H2O)2Al2(PO4)3] (1994)
    s.l. : American Chemical Society
    Chemistry of materials 6 (1994), S. 349-350 
    Details
    ISSN: 1520-5002
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/cm00040a001
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  • 6
    Electronic Resource
    Electronic Resource
    Biochemical and genetic characterization of the acetaldehyde dehydrogenase complex from Acetobacter europaeus (1997)
    Springer
    Archives of microbiology 168 (1997), S. 81-91 
    Details
    ISSN: 1432-072X
    Keywords: Key wordsAcetobacter europaeus ; Aldehyde ; dehydrogenase complex ; Aldehyde dehydrogenase-encoding genes ; Promoter mapping
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The aldehyde dehydrogenase complex, which catalyzes the oxidation of acetaldehyde to acetic acid, was purified to apparent homogeneity from the membrane fraction of the industrial vinegar-producing strain Acetobacter europaeus. The determined K m for acetaldehyde was 2.1 mM. SDS-PAGE of the enzyme complex showed the presence of three different subunits with molecular masses of 79, 46, and 17 kDa, respectively. The two larger subunits contained heme. The difference spectrum indicated a cytochrome c, a heme B, and a [2Fe–2S] cluster. The nucleotide sequence of several cloned fragments of a 6-kb chromosomal DNA segment from A. europaeus was determined. It contains three consecutive open reading frames that correspond to proteins with calculated molecular masses of 84.1, 49.0, and 16.7 kDa; these were assigned to the purified proteins and named aldH, aldF, and aldG, respectively. The N-terminal sequence of the 79-kDa subunit was detected within the predicted amino acid sequence of AldH, which indicated the presence of a leader peptide. Cotranscription of the three genes was shown by Northern hybridization. Sequence analysis and experimental evidence allowed the assignment of the following cofactors to the respective subunits of the aldehyde dehydrogenase complex: heme C to AldF, [2Fe–2S] cluster to AldG, and heme B and a molybdopterin cofactor to AldH. Part of an open reading frame, gdhA, was detected upstream of the operon that showed high similarities to the C-terminal part of several pyrroloquinoline-chinone-dependent glucose dehydrogenases.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002030050473
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  • 7
    Electronic Resource
    Electronic Resource
    Crystallization and preliminary diffraction studies of native and selenomethionine CcmG (CycY, DsbE) (2001)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 57 (2001), S. 1293-1295 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Disulfide-bond (Dsb) proteins are a family of redox proteins containing a Cys-X-X-Cys motif. They are essential for disulfide-bond exchange in the bacterial periplasm and are necessary for the correct folding and function of many secreted proteins. CcmG (DsbE) is a reducing Dsb protein required for cytochrome c maturation. Crystals of Bradyrhizobium japonicum CcmG have been obtained that diffract X-rays to 1.14 Å resolution. The crystals are orthorhombic, space group P212121, with unit-cell parameters a = 35.1, b = 48.2, c = 90.2 Å. Selenomethionine CcmG was expressed without using a methionine auxotroph or methionine-pathway inhibition and was purified without reducing agents.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444901009982
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  • 8
    Electronic Resource
    Electronic Resource
    Periplasmic protein thiol:disulfide oxidoreductases of Escherichia coli (2000)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology reviews 24 (2000), S. 0 
    Details
    ISSN: 1574-6976
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Disulfide bond formation is part of the folding pathway for many periplasmic and outer membrane proteins that contain structural disulfide bonds. In Escherichia coli, a broad variety of periplasmic protein thiol:disulfide oxidoreductases have been identified in recent years, which substantially contribute to this pathway. Like the well-known cytoplasmic thioredoxins and glutaredoxins, these periplasmic protein thiol:disulfide oxidoreductases contain the conserved C-X-X-C motif in their active site. Most of them have a domain that displays the thioredoxin-like fold. In contrast to the cytoplasmic system, which consists exclusively of reducing proteins, the periplasmic oxidoreductases have either an oxidising, a reducing or an isomerisation activity. Apart from understanding their physiological role, it is of interest to learn how these proteins interact with their target molecules and how they are recycled as electron donors or acceptors. This review reflects the recently made efforts to elucidate the sources of oxidising and reducing power in the periplasm as well as the different properties of certain periplasmic protein thiol:disulfide oxidoreductases of E. coli.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6976.2000.tb00544.x
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  • 9
    Electronic Resource
    Electronic Resource
    New insights into the role of CcmC, CcmD and CcmE in the haem delivery pathway during cytochrome c maturation by a complete mutational analysis of the conserved tryptophan-rich motif of CcmC (2000)
    Oxford, UK : Blackwell Science Ltd
    Molecular microbiology 37 (2000), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Maturation of c-type cytochromes in Escherichia coli is a complex process requiring eight membrane proteins encoded by the ccmABCDEFGH operon. CcmE is a mediator of haem delivery. It binds haem transiently at a conserved histidine residue and releases it for directed transfer to apocytochrome c. CcmC, an integral membrane protein with six transmembrane helices, is necessary and sufficient to incorporate haem covalently into CcmE. CcmC contains a highly conserved tryptophan-rich motif, WGXXWXWD, in its second periplasmic loop. Here, we present the results of a systematic mutational analysis of this motif. Changes of the non-conserved T121 and W122 to A resulted in wild-type CcmC activity. Changes of the single amino acids W119A, G120A, W123A, W125I and D126A or of the spacing within the motif by deleting V124 (ΔV124) inhibited the covalent haem incorporation into CcmE. Enhanced expression of ccmD suppressed this mutant phenotype by increasing the amounts of CcmC and CcmE polypeptides in the membrane. The ΔV124 mutant showed the strongest defect of all single mutants. Mutants in which six residues of the tryptophan-rich motif were changed showed no residual CcmC activity. This phenotype was independent of the level of ccmD expression. Our results demonstrate the functional importance of the tryptophan-rich motif for haem transfer to CcmE. We propose that the three membrane proteins CcmC, CcmD and CcmE interact directly with each other, establishing a cytoplasm to periplasm haem delivery pathway for cytochrome c maturation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2958.2000.02083.x
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  • 10
    Electronic Resource
    Electronic Resource
    The ccoNOQP gene cluster codes for a cb-type cytochrome oxidase that functions in aerobic respiration of Rhodobacter capsulatus (1994)
    Oxford, UK : Blackwell Publishing Ltd
    Molecular microbiology 14 (1994), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: The genes for a new type of a haem-copper cytochrome oxidase were cloned from Rhodobacter capsulatus strain 37b4, using the Bradyrhizobium japonicum fixNOQP gene region as a hybridizing probe. Four genes, probably organized in an operon (ccoNOQP), were identified; their products share extensive amino acid sequence similarity with the FixN, O, Q and P proteins that have recently been shown to be the subunits of a cb-type oxidase. CcoN is a c-type cytochrome, CcoO and CcoP are membrane-bound mono- and dihaem c-type cytochromes and CcoQ is a small membrane protein of unknown function. Genes for a similar oxidase are also present in other non-rhizobial bacterial species such as Azoto-bacter vinelandii, Agrobacterium tumefaciens and Pseudomonas aeruginosa, as revealed by polymerase chain reaction analysis. A ccoN mutant was constructed whose phenotype, in combination with the structural information on the gene products, provides evidence that the CcoNOQP oxidase is a cytochrome c oxidase of the cb type, which supports aerobic respiration in R. capsulatus and which is probably identical to the cbb3-type oxidase that was recently purified from a different strain of the same species. Mutant analysis also showed that this oxidase has no influence on photosynthetic growth and nitrogen-fixation activity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2958.1994.tb01308.x
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