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  • 1
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    Call number: ERW
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  • 2
    Keywords: Medicine ; Medical genetics ; Biochemistry ; Biomedicine ; Gene Function ; Protein Science ; Biomedicine general ; Springer eBooks
    Description / Table of Contents: Preface. Part I℗ Introduction -- Overview of the Carbonic Anhydrase Field -- Part II Carbonic Anhydrases: Ancient but Relevant. Physiological Functions of the Alpha Class of Carbonic Anhydrases -- Catalytic Mechanism of Îł-Class Carbonic Anhydrases: CO2 Hydration and Proton Transfer -- Structure and Catalytic Mechanism of b-Carbonic Anhydrases -- Prokaryotic Carbonic Anhydrases of Earth́€™s Environment -- Carboxysomal Carbonic Anhydrases -- Carbonic Anhydrases and their Interplay with Acid/base-coupled Membrane Transporters -- Carbonic Anhydrase Related Proteins: Molecular Biology and Evolution -- Membrane Associated Carbonic Anhydrase IV (CA IV): A Personal and Historical Perspective.-℗ Carbonic Anhydrase Expression in Kidney and Renal Cancer: Implications for Diagnosis and Treatment -- Carbonic Anhydrase IX: Regulation and Role in Cancer.-℗ Carbonic Anhydrase IX as an Imaging and Therapeutic Target for Tumors and Metastases -- Carbonic Anhydrase IX (CAIX) as a Mediator of Hypoxia-induced Stress Response in Cancer Cells -- Carbonic Anhydrases and Brain pH in the Control of Neruronal Excitability -- Carbonic Anhydrase Inhibitors: Drug Design -- Natural Products that Inhibit Carbonic Anhydrases -- Glaucoma and the Application of Carbonic Anhydrase Inhibitors -- Carbonic Anhydrase Inhibitors and High Altitude Illnesses -- Thermal-Stable Carbonic Anhydrases: A Structural Overview -- Carbonic Anhydrases in Industrial Applications. Index
    Abstract: ℗ The study of carbonic anhydrase has spanned multiple generations of scientists.℗ Carbonic anhydrase was first discovered in 1932 by Meldrum and Roughton.℗ Inhibition by sulfanilamide was shown in 1940 by Mann and Keilin.℗ Even Hans Krebs contributed to early studies with a paper in 1948 showing the relationship of 25 different sulfonamides to CA inhibition. It was he who pointed out the importance of both the charged and uncharged character of these compounds for physiological experiments. ℗ ℗ ℗ ℗ ℗ ℗ ℗ ℗ ℗ ℗ ℗ The field of study that focuses on carbonic anhydrase (CA) has exploded in recent years with the identification of new families and isoforms.℗ The CAs are metalloenzymes which are comprised of 5 structurally different families: the alpha, beta, gamma, and delta, and epsilon classes.℗ The alpha class is found primarily in animals with several isoforms℗ associated with human disease.℗ The beta CAs are expressed primarily in plants and are the most divergent.℗ The gamma CAs are the most ancient. These are structurally related to the beta CAs, but have a mechanism more similar to the alpha CAs.℗ ℗ The delta CAs are found in marine algae and diflagellates.℗ The epsilon class is found in prokaryotes in which it is part of the carboxysome shell perhaps supplying RuBisCO with CO2 for carbon fixation.℗ ℗ ℗ ℗ ℗ ℗ ℗ ℗ ℗ ℗ ℗ ℗ ℗ With the excitement surrounding the discovery of disease-related CAs, scientists have redoubled their efforts to better understand structure-function relationships, to design high affinity, isotype-specific inhibitors, and to delineate signaling systems that play regulatory roles over expression and activity.℗ We have designed the book to cover basic information of mechanism, structure, and function of the CA families.℗ The authors included in this book bring to light the newest data with regard to the role of CA in physiology and pathology, across phylums, and in unique environmental niches
    Pages: IX, 430 p. 75 illus., 37 illus. in color. : online resource.
    ISBN: 9789400773592
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  • 3
    Call number: QZ241:10/24
    Keywords: Bone Marrow Neoplasms / pathology
    Pages: xviii, 817 pages : illustrations.
    ISBN: 9781933477350
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  • 4
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    New York : The Oncology Group
    Call number: QZ365WF658:158
    Keywords: Lung Neoplasms ; Carcinoma, Non-Small-Cell Lung ; Mesothelioma ; Thymoma
    Notes: A selected chapter from: 7th ed. Cancer management: a multidisciplinary approach : medical, surgical, & radiation oncology, edited by Richard Pazdur ...
    Pages: 43 p.
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  • 5
    Keywords: IN-VIVO ; RESOLUTION ; MICE ; PARTICLES ; MINUTE VIRUS ; CANINE PARVOVIRUS ; REGRESSION ; FUNCTIONAL IMPLICATIONS ; ROTATION FUNCTION ; RAT MODELS
    Abstract: Crystals of H-1 Parvovirus (H-1PV), an antitumor gene-delivery vector, were obtained for DNA-containing capsids and diffracted X-rays to 2.7 A resolution using synchrotron radiation. The crystals belonged to the monoclinic space group P2(1), with unit-cell parameters a = 255.4, b = 350.4, c = 271.6 A, beta = 90.34 degrees . The unit cell contained two capsids, with one capsid per crystallographic asymmetric unit. The H-1PV structure has been determined by molecular replacement and is currently being refined.
    Type of Publication: Journal article published
    PubMed ID: 23192051
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  • 6
  • 7
    Keywords: NUCLEIC-ACID ; MINUTE VIRUS ; HUMAN TUMOR-CELLS ; CANINE PARVOVIRUS ; FUNCTIONAL IMPLICATIONS ; ONCOLYTIC PARVOVIRUS ; AMINO-ACID-RESIDUES ; HOST-RANGE ; COAT PROTEIN ; REPLICATING PARVOVIRUSES
    Abstract: The structure of single-stranded DNA (ssDNA) packaging H-1 parvovirus (H-1PV), which is being developed as an antitumor gene delivery vector, has been determined for wild-type (wt) virions and noninfectious (empty) capsids to 2.7- and 3.2-A resolution, respectively, using X-ray crystallography. The capsid viral protein (VP) structure consists of an alpha-helix and an eight-stranded anti-parallel beta-barrel with large loop regions between the strands. The beta-barrel and loops form the capsid core and surface, respectively. In the wt structure, 600 nucleotides are ordered in an interior DNA binding pocket of the capsid. This accounts for approximately 12% of the H-1PV genome. The wt structure is identical to the empty capsid structure, except for side chain conformation variations at the nucleotide binding pocket. Comparison of the H-1PV nucleotides to those observed in canine parvovirus and minute virus of mice, two members of the genus Parvovirus, showed both similarity in structure and analogous interactions. This observation suggests a functional role, such as in capsid stability and/or ssDNA genome recognition for encapsulation. The VP structure differs from those of other parvoviruses in surface loop regions that control receptor binding, tissue tropism, pathogenicity, and antibody recognition, including VP sequences reported to determine tumor cell tropism for oncotropic rodent parvoviruses. These structures of H-1PV provide insight into structural features that dictate capsid stabilization following genome packaging and three-dimensional information applicable for rational design of tumor-targeted recombinant gene delivery vectors.
    Type of Publication: Journal article published
    PubMed ID: 23449783
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  • 8
    Keywords: VIRAL VECTORS ; CANINE PARVOVIRUS ; CRYOELECTRON MICROSCOPY ; HEPARAN-SULFATE PROTEOGLYCAN ; EFFICIENT TRANSDUCTION ; GENE-THERAPY VECTOR ; LEBERS CONGENITAL AMAUROSIS ; NEUTRALIZING MONOCLONAL-ANTIBODY ; MINK DISEASE PARVOVIRUS ; DIRECTED EVOLUTION
    Abstract: The clinical utility of the adeno-associated virus (AAV) gene delivery system has been validated by the regulatory approval of an AAV serotype 1 (AAV1) vector for the treatment of lipoprotein lipase deficiency. However, neutralization from preexisting antibodies is detrimental to AAV transduction efficiency. Hence, mapping of AAV antigenic sites and engineering of neutralization-escaping vectors are important for improving clinical efficacy. We report the structures of four AAV-monoclonal antibody fragment complexes, AAV1-ADK1a, AAV1-ADK1b, AAV5-ADK5a, and AAV5-ADK5b, determined by cryo-electron microscopy and image reconstruction to a resolution of approximately 11 to 12 A. Pseudoatomic modeling mapped the ADK1a epitope to the protrusions surrounding the icosahedral 3-fold axis and the ADK1b and ADK5a epitopes, which overlap, to the wall between depressions at the 2- and 5-fold axes (2/5-fold wall), and the ADK5b epitope spans both the 5-fold axis-facing wall of the 3-fold protrusion and portions of the 2/5-fold wall of the capsid. Combined with the six antigenic sites previously elucidated for different AAV serotypes through structural approaches, including AAV1 and AAV5, this study identified two common AAV epitopes: one on the 3-fold protrusions and one on the 2/5-fold wall. These epitopes coincide with regions with the highest sequence and structure diversity between AAV serotypes and correspond to regions determining receptor recognition and transduction phenotypes. Significantly, these locations overlap the two dominant epitopes reported for autonomous parvoviruses. Thus, rather than the amino acid sequence alone, the antigenic sites of parvoviruses appear to be dictated by structural features evolved to enable specific infectious functions. IMPORTANCE: The adeno-associated viruses (AAVs) are promising vectors for in vivo therapeutic gene delivery, with more than 20 years of intense research now realized in a number of successful human clinical trials that report therapeutic efficacy. However, a large percentage of the population has preexisting AAV capsid antibodies and therefore must be excluded from clinical trials or vector readministration. This report represents our continuing efforts to understand the antigenic structure of the AAVs, specifically, to obtain a picture of "polyclonal" reactivity as is the situation in humans. It describes the structures of four AAV-antibody complexes determined by cryo-electron microscopy and image reconstruction, increasing the number of mapped epitopes to four and three, respectively, for AAV1 and AAV5, two vectors currently in clinical trials. The results presented provide information essential for generating antigenic escape vectors to overcome a critical challenge remaining in the optimization of this highly promising vector delivery system.
    Type of Publication: Journal article published
    PubMed ID: 25410874
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  • 9
    Keywords: EXPRESSION ; MONOCLONAL-ANTIBODIES ; AAV VECTORS ; RHESUS-MONKEYS ; VIRAL-VECTORS ; LIVER TRANSDUCTION ; TYPE-2 CAPSIDS ; GENE-THERAPY VECTOR ; PHOSPHOLIPASE-A2 ACTIVITY ; PREEXISTING IMMUNITY
    Abstract: Adeno-associated viruses (AAVs) are small single-stranded DNA viruses that can package and deliver nongenomic DNA for therapeutic gene delivery. AAV8, a liver-tropic vector, has shown great promise for the treatment of hemophilia A and B. However, as with other AAV vectors, host anti-capsid immune responses are a deterrent to therapeutic success. To characterize the antigenic structure of this vector, cryo-electron microscopy and image reconstruction (cryo-reconstruction) combined with molecular genetics, biochemistry, and in vivo approaches were used to define an antigenic epitope on the AAV8 capsid surface for a neutralizing monoclonal antibody, ADK8. Docking of the crystal structures of AAV8 and a generic Fab into the cryo-reconstruction for the AAV8-ADK8 complex identified a footprint on the prominent protrusions that flank the 3-fold axes of the icosahedrally symmetric capsid. Mutagenesis and cell-binding studies, along with in vitro and in vivo transduction assays, showed that the major ADK8 epitope is formed by an AAV variable region, VRVIII (amino acids 586 to 591 [AAV8 VP1 numbering]), which lies on the surface of the protrusions facing the 3-fold axis. This region plays a role in AAV2 and AAV8 cellular transduction. Coincidently, cell binding and trafficking assays indicate that ADK8 affects a postentry step required for successful virus trafficking to the nucleus, suggesting a probable mechanism of neutralization. This structure-directed strategy for characterizing the antigenic regions of AAVs can thus generate useful information to help re-engineer vectors that escape host neutralization and are hence more efficacious.
    Type of Publication: Journal article published
    PubMed ID: 22593150
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  • 10
    ISSN: 1520-5126
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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