Joanna Hansen

University of Utah

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Ellie Ehrenfeld

National Institute of Allergy and Infectious Diseases

D Etchison

University of Kansas Medical Center

John W.B. Hershey

University of California, Davis

J P Kushner

Children's Oncology Group

Thomas F. McCutchan

National Institute of Allergy and Infectious Diseases

Ching‐Juh Lai

National Institutes of Health

Michael C. Schotz

University of California, Los Angeles

Kenji Sekikawa

Cancer Research Institute of the Slovak Academy of Sciences

Thomas T. Yoshikawa

Charles R. Drew University of Medicine and Science

Lewis Markoff

Center for Biologics Evaluation and Research

Cooperative Institutions

University of Utah

National Institutes of Health

National Institute of Allergy and Infectious Diseases

University of California, Los Angeles

University of Alabama at Birmingham

Huntsman Cancer Institute

Medical Research Council

Icahn School of Medicine at Mount Sinai

United States Department of Veterans Affairs

University of Alberta

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The HLA class I locus: analysis of RFLPs in hereditary hemochromatosis

Cytogenetic and Genome Research (1989)

Joanna Hansen J P Kushner

The gene for hereditary hemochromatosis is linked to the HLA locus on chromosome 6. Four cloned DNA probes originating from the HLA class I region were used to detect seven restriction fragment length polymorphisms (RFLPs). Allele frequencies and segregation of each RFLP was determined. Analysis of RFLPs in 38 unrelated homozygotes with hemochromatosis revealed differences in allele frequencies between the control and the hemochromatotic groups but these differences did not reach statistical significance. Some differences persisted, however, even when only controls with the A3 antigen were compared with A3 hemochromatotics. Since both control and hemochromatotic groups were small, further studies will be necessary to ascertain whether these RFLPs could serve to locate the gene responsible for hereditary hemochromatosis.

Hereditary hemochromatosis

10.1159/000132763

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Citations (8)

Choosing the Right Picture for the Right Place

The Iowa Homemaker (1921)

Joanna Hansen

New Right

Right of way

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Demonstration in vitro that eucaryotic initiation factor 3 is active but that a cap-binding protein complex is inactive in poliovirus-infected HeLa cells

Journal of Virology (1984)

D Etchison Joanna Hansen Ellie Ehrenfeld Isaac Edery Nahum Sonenberg

Protein synthesis initiation factor preparations from poliovirus-infected HeLa cells have reduced ability to initiate translation on capped mRNA. The defect in initiation factors has been variously attributed to inactivation of eucaryotic initiation factor 3 (eIF3), eIF4B, or a cap-binding protein (CBP) complex. We have developed a series of in vitro protein synthesis assays to show that eIF3 is active but a CBP complex activity is inactivated after poliovirus infection. eIF3 activity, when determined in the presence of purified CBP complex, is present in sucrose gradients of factors from both infected and uninfected cells. CBP complex activity, determined in the presence of eIF3 from poliovirus-infected cells, is present in uninfected cells only and comigrates on sucrose gradient with an activity which restores the ability of crude initiation factors from infected cells to translate capped globin mRNA. This is the first demonstration by a fractionated translation system that an activity which is attributable to CBP complex is inactivated in poliovirus-infected cells. The results also indicate that eIF3 is undetectable or has greatly reduced activity in the absence of CBP complex.

Initiation factor

HeLa

Eukaryotic initiation factor

10.1128/jvi.51.3.832-837.1984

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Citations (86)

Cyclic GMP phosphodiesterase from bovine retina. Evidence for interspecies conservation

Biochemical Journal (1984)

L. Takemoto Joanna Hansen Debora B. Farber Diego P. Souza D.J. Takemoto

A light-activated phosphodiesterase (PDE) from retinal rod outer segments (ROS) has been strongly implicated as a possible mediator in the propagation of the visual response. In view of the probable importance of this enzyme in the visual system, a comparison of the PDE proteins from ROS of different evolutionary species was made. Partial purification of the PDE, as measured by enzymic activity, followed by resolution of the protein components on sodium dodecyl sulphate/polyacrylamide-gel electrophoresis, indicated that the major Coomassie Blue-staining species in the ROS of all species studied is a doublet of 84000-88000 Da. After radioiodination, this doublet was converted in all but the frog proteins into a single band of 85000 Da. Two-dimensional tryptic peptide mapping of the radioiodinated peptides indicated that at least six major peptides of the putative PDE have been conserved in all of the species studies. If this protein is indeed associated with PDE activity, such conserved peptides may play an important role in the catalytic and/or regulatory functions of the enzyme.

Conserved sequence

10.1042/bj2170129

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Specificity of initiation factor preparations from poliovirus-infected cells

Journal of Virology (1980)

David W. Brown Joanna Hansen Ellie Ehrenfeld

Crude initiation factor preparations from poliovirus-infected cells stimulated the translation of poliovirus RNA in vitro, but were inactive for the translation of host cell or vesicular stomatitis virus mRNA's. In contrast, similar preparations from either uninfected or vesicular stomatitis virus-infected cells supported the initiation of translation of host cell mRNA's and both viral mRNA's. These results reflect a specific alteration of some components(s) of the initiation factor preparation from poliovirus-infected cells which is consistent with the ability of the virus to inhibit the translation of host cell and vesicular stomatitis virus-directed protein synthesis.

Initiation factor

10.1128/jvi.34.2.573-575.1980

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Citations (13)

Zero emission neighbourhoods – encouraging sustainable communities

Joanna Hansen Win Laing

Zero emission

Zero (linguistics)

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Steady-state levels of uroporphyrinogen decarboxylase mRNA in lymphoblastoid cell lines from patients with familial porphyria cutanea tarda and their relatives.

PubMed (1988)

Joanna Hansen Marsha Pryor J B Kennedy J P Kushner

Uroporphyrinogen III decarboxylase

Lymphoblast

Northern blot

Porphyria cutanea tarda

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Citations (10)

Presence of the cap-binding protein in initiation factor preparations from poliovirus-infected HeLa cells

Journal of Virology (1981)

Joanna Hansen Ellie Ehrenfeld

Crude preparations of initiation factors from mock-infected and poliovirus-infected HeLa cells were analyzed for the presence of proteins which could be cross-linked to the 5' cap group of mRNA. A protein having an apparent molecular weight of 26,000, similar to the cap-binding protein in rabbit reticulocytes described by Sonenberg and Shatkin (Proc. Natl. Acad. Sci. U.S.A. 75:4843-4847, 1978), was found in the ribosomal salt wash from both uninfected and infected cells. Cross-linking of this polypeptide was inhibited by the cap analog m7GMP. In addition, cross-linking of a protein having an approximate molecular weight of 60,000 was similarly inhibited by cap analog. The smaller cap-binding protein fractionated in a 0 to 40% ammonium sulfate precipitate of ribosomal salt wash; the larger protein was found in the 40 to 70% ammonium sulfate fraction. Although the cap-binding proteins were present in both mock-infected and poliovirus-infected ribosomal salt wash, only preparations from uninfected HeLa cells were able to restore translation of capped vesicular stomatitis virus mRNA by extracts prepared from poliovirus-infected cells.

HeLa

Ribosomal protein

10.1128/jvi.38.2.438-445.1981

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Citations (44)

Isolation of a gene segment expressed by mature schizonts of Plasmodium knowlesi

Molecular and Biochemical Parasitology (1986)

Joanna Hansen Thomas F. McCutchan

Schizogony

Plasmodium knowlesi

Insert (composites)

Nuclease