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  1. Article: Bacterial chromosome segregation.

    Rothfield, L I

    Cell

    1994  Volume 77, Issue 7, Page(s) 963–966

    MeSH term(s) Bacteria/cytology ; Bacterial Proteins/physiology ; Cell Division ; Centromere ; Chromosomal Proteins, Non-Histone ; Chromosomes, Bacterial/physiology ; DNA Replication ; DNA, Bacterial/physiology ; DNA, Circular/physiology ; DNA-Binding Proteins/physiology ; Escherichia coli Proteins ; Plasmids
    Chemical Substances Bacterial Proteins ; Chromosomal Proteins, Non-Histone ; DNA, Bacterial ; DNA, Circular ; DNA-Binding Proteins ; Escherichia coli Proteins ; MukB protein, E coli ; chromosome partition proteins, bacterial
    Language English
    Publishing date 1994-07-01
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 187009-9
    ISSN 1097-4172 ; 0092-8674
    ISSN (online) 1097-4172
    ISSN 0092-8674
    DOI 10.1016/0092-8674(94)90435-9
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article: Nucleoid-independent identification of cell division sites in Escherichia coli.

    Cook, W R / Rothfield, L I

    Journal of bacteriology

    1999  Volume 181, Issue 6, Page(s) 1900–1905

    Abstract: The mechanism used by Escherichia coli to determine the correct site for cell division is unknown. In this report, we have attempted to distinguish between a model in which septal position is determined by the position of the nucleoids and a model in ... ...

    Abstract The mechanism used by Escherichia coli to determine the correct site for cell division is unknown. In this report, we have attempted to distinguish between a model in which septal position is determined by the position of the nucleoids and a model in which septal position is predetermined by a mechanism that does not involve nucleoid position. To do this, filaments with extended nucleoid-free regions adjacent to the cell poles were produced by simultaneous inactivation of cell division and DNA replication. The positions of septa that formed within the nucleoid-free zones after division was allowed to resume were then analyzed. The results showed that septa were formed at a uniform distance from cell poles when division was restored, with no relation to the distance from the nearest nucleoid. In some cells, septa were formed directly over nucleoids. These results are inconsistent with models that invoke nucleoid positioning as the mechanism for determining the site of division site formation.
    MeSH term(s) Bacterial Proteins/genetics ; Cell Division/genetics ; Cytoskeletal Proteins ; DNA Helicases/genetics ; DnaB Helicases ; Escherichia coli/cytology ; Escherichia coli/genetics ; Escherichia coli Proteins ; Fixatives ; Genes, Bacterial ; Models, Biological ; Mutation ; Osmium Tetroxide
    Chemical Substances Bacterial Proteins ; Cytoskeletal Proteins ; Escherichia coli Proteins ; Fixatives ; FtsZ protein, Bacteria ; sulA protein, E coli ; DNA Helicases (EC 3.6.4.-) ; DnaB Helicases (EC 3.6.4.12) ; Osmium Tetroxide (P40W033BGM)
    Language English
    Publishing date 1999-03
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
    ZDB-ID 2968-3
    ISSN 1098-5530 ; 0021-9193
    ISSN (online) 1098-5530
    ISSN 0021-9193
    DOI 10.1128/JB.181.6.1900-1905.1999
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  3. Article: Stability of the Escherichia coli division inhibitor protein MinC requires determinants in the carboxy-terminal region of the protein.

    Sen, M / Rothfield, L I

    Journal of bacteriology

    1998  Volume 180, Issue 1, Page(s) 175–177

    Abstract: Certain mutations in the C-terminal region of the Escherichia coli division inhibitor protein MinC cause loss of function of the division inhibitor by making MinC more sensitive to degradation by Lon protease, implying a possible role for the C-terminal ... ...

    Abstract Certain mutations in the C-terminal region of the Escherichia coli division inhibitor protein MinC cause loss of function of the division inhibitor by making MinC more sensitive to degradation by Lon protease, implying a possible role for the C-terminal region in regulating the stability and cellular concentration of MinC.
    MeSH term(s) ATP-Dependent Proteases ; Bacterial Proteins/analysis ; Bacterial Proteins/chemistry ; Bacterial Proteins/genetics ; Cell Division ; Escherichia coli/cytology ; Escherichia coli/genetics ; Escherichia coli Proteins ; Heat-Shock Proteins/metabolism ; Mutation ; Phenotype ; Protease La ; Serine Endopeptidases/metabolism
    Chemical Substances Bacterial Proteins ; Escherichia coli Proteins ; Heat-Shock Proteins ; MinC protein, Bacteria ; ATP-Dependent Proteases (EC 3.4.21.-) ; Serine Endopeptidases (EC 3.4.21.-) ; Lon protein, E coli (EC 3.4.21.53) ; Protease La (EC 3.4.21.53)
    Language English
    Publishing date 1998-01
    Publishing country United States
    Document type Journal Article ; Research Support, U.S. Gov't, P.H.S.
    ZDB-ID 2968-3
    ISSN 1098-5530 ; 0021-9193
    ISSN (online) 1098-5530
    ISSN 0021-9193
    DOI 10.1128/JB.180.1.175-177.1998
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  4. Article: On the relation of the hippocampal-fornix system to the control of rage responses in cats.

    ROTHFIELD, L / HARMAN, P J

    The Journal of comparative neurology

    2003  Volume 101, Issue 2, Page(s) 265–282

    MeSH term(s) Animals ; Brain/physiology ; Cats ; Emotions ; Fornix, Brain ; Hippocampus/physiology ; Rage
    Language English
    Publishing date 2003-08-13
    Publishing country United States
    Document type Journal Article
    ZDB-ID 3086-7
    ISSN 1096-9861 ; 0021-9967 ; 0092-7317
    ISSN (online) 1096-9861
    ISSN 0021-9967 ; 0092-7317
    DOI 10.1002/cne.901010203
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  5. Article: Bacterial cell division: the cycle of the ring.

    Rothfield, L I / Justice, S S

    Cell

    1997  Volume 88, Issue 5, Page(s) 581–584

    MeSH term(s) Bacteria/cytology ; Bacterial Physiological Phenomena ; Cell Division/physiology
    Language English
    Publishing date 1997-03-07
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 187009-9
    ISSN 1097-4172 ; 0092-8674
    ISSN (online) 1097-4172
    ISSN 0092-8674
    DOI 10.1016/s0092-8674(00)81899-1
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  6. Article: How do bacteria decide where to divide?

    Rothfield, L I / Zhao, C R

    Cell

    1996  Volume 84, Issue 2, Page(s) 183–186

    MeSH term(s) Bacillus subtilis/cytology ; Bacteria/cytology ; Bacterial Proteins/genetics ; Bacterial Proteins/physiology ; Cell Division/physiology ; Escherichia coli/cytology
    Chemical Substances Bacterial Proteins
    Language English
    Publishing date 1996-01-26
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 187009-9
    ISSN 1097-4172 ; 0092-8674
    ISSN (online) 1097-4172
    ISSN 0092-8674
    DOI 10.1016/s0092-8674(00)80971-x
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  7. Article: The MreB and Min cytoskeletal-like systems play independent roles in prokaryotic polar differentiation.

    Shih, Yu-Ling / Kawagishi, Ikuro / Rothfield, Lawrence

    Molecular microbiology

    2005  Volume 58, Issue 4, Page(s) 917–928

    Abstract: Establishment of an axis of cell polarity and differentiation of the cell poles are fundamental aspects of cellular development in many organisms. We compared the effects of two bacterial cytoskeletal-like systems, the MreB and MinCDE systems, on these ... ...

    Abstract Establishment of an axis of cell polarity and differentiation of the cell poles are fundamental aspects of cellular development in many organisms. We compared the effects of two bacterial cytoskeletal-like systems, the MreB and MinCDE systems, on these processes in Escherichia coli. We report that the Min proteins are capable of establishing an axis of oscillation that is the initial step in establishment of polarity in spherical cells, in a process that is independent of the MreB cytoskeleton. In contrast, the MreB system is required for establishment of the rod shape of the cell and for polar targeting of other polar constituents, such as the Shigella virulence factor IcsA and the aspartate chemoreceptor Tar, in a process that is independent of the Min system. Thus, the two bacterial cytoskeletal-like systems act independently on different aspects of cell polarization.
    MeSH term(s) Adenosine Triphosphatases/analysis ; Adenosine Triphosphatases/genetics ; Adenosine Triphosphatases/physiology ; Bacterial Proteins/metabolism ; Cell Cycle Proteins/analysis ; Cell Cycle Proteins/genetics ; Cell Cycle Proteins/physiology ; Chemoreceptor Cells ; DNA-Binding Proteins/metabolism ; Escherichia coli/chemistry ; Escherichia coli/cytology ; Escherichia coli/genetics ; Escherichia coli/physiology ; Escherichia coli Proteins/analysis ; Escherichia coli Proteins/genetics ; Escherichia coli Proteins/metabolism ; Escherichia coli Proteins/physiology ; Gene Deletion ; Green Fluorescent Proteins/analysis ; Green Fluorescent Proteins/genetics ; Membrane Proteins/analysis ; Membrane Proteins/genetics ; Membrane Proteins/physiology ; Microscopy, Fluorescence ; Models, Biological ; Mutagenesis, Insertional ; Receptors, Cell Surface/metabolism ; Shigella/cytology ; Shigella/genetics ; Shigella/physiology ; Staining and Labeling ; Transcription Factors/metabolism
    Chemical Substances Bacterial Proteins ; Cell Cycle Proteins ; DNA-Binding Proteins ; Escherichia coli Proteins ; Membrane Proteins ; MinC protein, E coli ; MinE protein, E coli ; Receptors, Cell Surface ; Tar protein, E coli ; Transcription Factors ; virG protein, Shigella flexneri ; Green Fluorescent Proteins (147336-22-9) ; MreB protein, E coli (149255-61-8) ; Adenosine Triphosphatases (EC 3.6.1.-) ; MinD protein, E coli (EC 3.6.1.-)
    Language English
    Publishing date 2005-11
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 619315-8
    ISSN 1365-2958 ; 0950-382X
    ISSN (online) 1365-2958
    ISSN 0950-382X
    DOI 10.1111/j.1365-2958.2005.04841.x
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  8. Article: The periseptal annulus: An organelle associated with cell division in Gram-negative bacteria.

    Macalister, T J / Macdonald, B / Rothfield, L I

    Proceedings of the National Academy of Sciences of the United States of America

    2002  Volume 80, Issue 5, Page(s) 1372–1376

    Abstract: Evidence is presented that the site of cell division in Salmonella typhimurium is flanked by two circumferential zones of cell envelope differentiation, the periseptal annuli, which separate the division site from the remainder of the cell envelope. Each ...

    Abstract Evidence is presented that the site of cell division in Salmonella typhimurium is flanked by two circumferential zones of cell envelope differentiation, the periseptal annuli, which separate the division site from the remainder of the cell envelope. Each annulus is composed of a continuous structure in which the membranous elements of the cell envelope are closely associated with the murein cytoskeleton. The paired annuli appear early in the division process and the region between them defines a new cellular domain, the periseptal compartment, within which the division septum is formed.
    Language English
    Publishing date 2002-09-13
    Publishing country United States
    Document type Journal Article
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.80.5.1372
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  9. Article: Polar explorers: membrane proteins that determine division site placement.

    Rothfield, L I / Shih, Y L / King, G

    Cell

    2001  Volume 106, Issue 1, Page(s) 13–16

    MeSH term(s) Adenosine Triphosphatases/physiology ; Bacterial Proteins/physiology ; Cell Cycle Proteins ; Cell Division/physiology ; Cell Polarity/physiology ; Escherichia coli/cytology ; Escherichia coli/physiology ; Escherichia coli Proteins ; Membrane Proteins/physiology ; Models, Biological
    Chemical Substances Bacterial Proteins ; Cell Cycle Proteins ; Escherichia coli Proteins ; Membrane Proteins ; MinC protein, Bacteria ; MinE protein, E coli ; Adenosine Triphosphatases (EC 3.6.1.-) ; MinD protein, E coli (EC 3.6.1.-)
    Language English
    Publishing date 2001-07-13
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 187009-9
    ISSN 1097-4172 ; 0092-8674
    ISSN (online) 1097-4172
    ISSN 0092-8674
    DOI 10.1016/s0092-8674(01)00432-9
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  10. Article: Relation of positive L.E.-cell preparations to activity of lupus erythematosus and corticosteroid therapy.

    ROTHFIELD, N F / PACE, N

    The New England journal of medicine

    1962  Volume 266, Page(s) 535–538

    MeSH term(s) Adrenal Cortex Hormones/therapy ; Humans ; Lupus Erythematosus, Systemic/therapy
    Chemical Substances Adrenal Cortex Hormones
    Language English
    Publishing date 1962-03-15
    Publishing country United States
    Document type Journal Article
    ZDB-ID 207154-x
    ISSN 1533-4406 ; 0028-4793
    ISSN (online) 1533-4406
    ISSN 0028-4793
    DOI 10.1056/NEJM196203152661103
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