Search Results - (Author, Cooperation:C. Lamb)
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1Staff View
Publication Date: 2018-01-06Publisher: Wiley-BlackwellPrint ISSN: 0265-9247Electronic ISSN: 1521-1878Topics: BiologyMedicinePublished by: -
2Anders Barth, Jelle Hendrix, Daniel Fried, Yoav Barak, Edward A. Bayer, Don C. Lamb
National Academy of Sciences
Published 2018Staff ViewPublication Date: 2018-11-28Publisher: National Academy of SciencesPrint ISSN: 0027-8424Electronic ISSN: 1091-6490Topics: BiologyMedicineNatural Sciences in GeneralPublished by: -
3J. Fan ; C. Crooks ; G. Creissen ; L. Hill ; S. Fairhurst ; P. Doerner ; C. Lamb
American Association for the Advancement of Science (AAAS)
Published 2011Staff ViewPublication Date: 2011-03-10Publisher: American Association for the Advancement of Science (AAAS)Print ISSN: 0036-8075Electronic ISSN: 1095-9203Topics: BiologyChemistry and PharmacologyComputer ScienceMedicineNatural Sciences in GeneralPhysicsKeywords: Arabidopsis/genetics/*metabolism/*microbiology ; Bacterial Proteins/genetics/metabolism ; Escherichia coli/drug effects/genetics/growth & development ; *Genes, Bacterial ; Glucosinolates/metabolism ; *Host-Pathogen Interactions ; Isothiocyanates/metabolism/pharmacology ; Operon ; Plant Diseases/microbiology ; Plant Extracts/pharmacology ; Plants, Genetically Modified ; Pseudomonas syringae/drug effects/*genetics/growth & development/pathogenicity ; Thiocyanates/isolation & purification/*metabolism/*pharmacologyPublished by: -
4Lamb, C. T., Festa-Bianchet, M., Boyce, M. S.
American Association for the Advancement of Science (AAAS)
Published 2018Staff ViewPublication Date: 2018-03-06Publisher: American Association for the Advancement of Science (AAAS)Print ISSN: 0036-8075Electronic ISSN: 1095-9203Topics: BiologyChemistry and PharmacologyGeosciencesComputer ScienceMedicineNatural Sciences in GeneralPhysicsPublished by: -
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ISSN: 1365-3040Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: BiologyNotes: Abstract. Plants respond actively to infection and other environmental stresses by synthesizing phytoalexins and defence-related proteins. This response can be induced in plant cell suspension cultures with compounds known as elicitors. These are often carbohydrates of fungal origin. In bean, transcriptional activation of the defence genes commences less than five minutes after elicitor addition, thus it is clearly a very rapid response implying few biochemical steps exist between elicitor interaction and the initiation of defence gene transcription. The induction of phytoalexin biosynthesis during incompatible interactions of bean with Colletotrichum lindemuthianum occurs rapidly during the initial contact between the host and pathogen. This appears to be a direct response to molecular recognition of the pathogen. In compatible interactions however, the pathogen grows biotrophically and phytoalexin biosynthesis is not triggered until lesions begin to form. Thus this may be a response to tissue damage rather than direct molecular recognition. Many bean defence genes, including those regulating key points in the phytoalexin biosynthetic pathway, exist in the genome as small multigene families. In some cases there is differential regulation within a family in response to developmental and environmental signals. The analysis of the cis-acting sequences involved in the regulation of chalcone synthase has been facilitated by the use of electroporated protoplasts as a transient assay system. This work and the use of DNA footprinting and gel-retardation assays will help identify the corresponding trans-acting factors involved in the regulation of these genes. While progress is being made in understanding the mechanisms of transcriptional activation of defence genes little is known of how plants recognize pathogens and elicitors or how this signal is transduced to the nucleus.Type of Medium: Electronic ResourceURL: -
6SAUER, N. ; CORBIN, D. R. ; KELLER, B. ; LAMB, C. J.
Oxford, UK : Blackwell Publishing Ltd
Published 1990Staff ViewISSN: 1365-3040Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: BiologyNotes: Abstract. We have isolated a cDNA clone whose corresponding transcript encodes an apoprotein of a hydroxyproline-rich glycoprotein. Both infection of plants with fungal spores and treatment of suspension-cultured bean cells with a fungal elicitor preparation cause a rapid decrease of the level of this mRNA. Wounding of bean tissue, however, leads to a very rapid, transient induction of this transcript. In contrast, all bean hydroxyproline-rich glycoproteins described previously are induced both after infection with fungal spores and after mechanical damage. The protein encoded by this new clone contains a proline-rich domain of about 30 kilodaltons. Most of these proline residues are part of the characteristic peptides Ser-Pro4, Scr-Pro5 and Ser-Pro6, which are often tandemly repeated. These tandem-repeats are not found in any of the other bean hydroxyproline-rich glycoproteins, where almost all of the Ser-Pro4 units are integrated into higher order repetitive units of 16 amino acids. The gene is present at a single or low copy number in the haploid genome and exhibits an unusual codon usage bias for the amino acids proline and serine.Type of Medium: Electronic ResourceURL: -
7Staff View
ISSN: 1365-3040Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: BiologyNotes: Abstract The accumulation of chlorogenic acid in illuminated discs of Solanum tuberosum tuber tissue is accompanied by rapid but transient increases in the activity levels of the biosynthetic enzymes phenylalanine ammonia-lyase, cinnamic acid 4-hydroxylase and hydroxycinnamoyl-CoA : quinate hydroxycinna-moyl transferase. Exogenous D-phenylalanine and L-α-aminooxy-β-phenylpropionic acid, competitive inhibitors of phenylalanine ammonia-lyase, inhibit the accumulation of chlorogenic acid and presumably reduce the endogenous pools of pathway intermediates such as cinnamic acid. These treatments prolong the phase of increase in phenylalanine ammonia-lyase and cinnamic acid 4-hydroxylase activities and indicate that product feedback modulation is important in maintaining the interrelationship between the levels of these two enzymes during the later stages of induction. In contrast,L-α-aminooxy-β-phenylpropionic acid inhibits the development of hydroxycinnamoyl transferase in illuminated discs supporting the idea that the light-stimulated increase in phenylalanine ammonia-lyase activity causes an increase in cinnamic acid production which mediates the light-stimulated increase in hydroxycinnamoyl transferase activity.Type of Medium: Electronic ResourceURL: -
8Staff View
ISSN: 1365-246XSource: Blackwell Publishing Journal Backfiles 1879-2005Topics: GeosciencesNotes: The stability of a toroidal magnetic field B=B(s*)Iφ (where (s*, φ, z*) are cylindrical polar coordinates), in a rapidly rotating cylindrical annulus with finitely conducting boundaries is investigated. In particular we examine the effect of a conducting layer of thickness ɛ at the base of an insulating mantle. The ratio of magnetic diffusivity in the layer to that of the outer core is denoted by νm: νm→ 0 corresponding to a perfectly conducting layer and νm→∞ to an insulating one. The inner core/outer core diffusivity ratio, νi, is in most cases taken to be νi= 1. Checks were made on the results by comparisons with results of Lamb (1994), and good agreement was found in the limit νm→∞ with his insulating boundary result. Lowering νm to more realistic values and increasing the thickness of the layer were both found to be destabilizing effects. An unexpected result was the continued existence of the Roberts-Loper exceptional mode, not found in the presence of perfectly conducting boundaries, in the limit νi, νm→ 0 and, with νi, νm≲ 1, when E and Eν (non-dimensional measures of viscous and inertial effects) → 0.Type of Medium: Electronic ResourceURL: -
9Staff View
ISSN: 1476-4687Source: Nature Archives 1869 - 2009Topics: BiologyChemistry and PharmacologyMedicineNatural Sciences in GeneralPhysicsNotes: [Auszug] THE existence of plant growth regulators such as auxins and cytokinins has been known for some time and a plethora of physiological responses to each class of hormone have been described. However, little is known of the biochemical basis of plant hormone action. By analogy with animal hormones one ...Type of Medium: Electronic ResourceURL: -
10Staff View
ISSN: 1476-4687Source: Nature Archives 1869 - 2009Topics: BiologyChemistry and PharmacologyMedicineNatural Sciences in GeneralPhysicsNotes: [Auszug] IT has been said in these columns that 'Plant molecular biology is not dead, but is merely awaiting the attention of competent and dedicated biochemists', (News and Views 254, 13; 1975). A recent illustration of the potential con tribution that biochemical studies can make to the understanding of ...Type of Medium: Electronic ResourceURL: -
11Staff View
ISSN: 0968-0004Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002Topics: BiologyChemistry and PharmacologyMedicineType of Medium: Electronic ResourceURL: -
12Staff View
ISSN: 1749-6632Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: Natural Sciences in GeneralType of Medium: Electronic ResourceURL: -
13Segmentation and Market Structure When Both Consumer and Situational Characteristics Are ExplanatoryStaff View
ISSN: 0742-6046Topics: PsychologyEconomicsURL: -
14Staff View
ISSN: 0160-9327Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002Topics: Natural Sciences in GeneralType of Medium: Electronic ResourceURL: -
15Lamb, C. Sue ; Jackson, Lee A. ; Cassiday, Patricia B. ; Priest, Doris J.
New York, N.Y. : Periodicals Archive Online (PAO)
Published 1993Staff ViewISSN: 0360-0025Topics: ArchaeologyURL: -
16Staff View
ISSN: 0307-1847Topics: Political ScienceURL: -
17LAMB, C. B. 〈Lieutenant-Commander, DSO, DSC〉
London : Periodicals Archive Online (PAO)
Published 1948Staff ViewISSN: 0307-1847Topics: Political ScienceURL: -
18Cerundolo, V. ; Alexander, J. ; Anderson, K. ; Lamb, C. ; Cresswell, P. ; McMichael, A. ; Gotch, F. ; Townsend, A.
[s.l.] : Nature Publishing Group
Published 1990Staff ViewISSN: 1476-4687Source: Nature Archives 1869 - 2009Topics: BiologyChemistry and PharmacologyMedicineNatural Sciences in GeneralPhysicsNotes: [Auszug] The human mutant cell line LBL 721.174 (0.174) was selected from the B-cell line LBL 721 by exposure to gamma rays and sequential treatments with monoclonal antibodies against class I and class II molecules and complement1. It has a defect in assembly and transport of class I molecules that has ...Type of Medium: Electronic ResourceURL: -
19Staff View
ISSN: 1432-2048Keywords: Cell culture ; Phaseolus (enzyme turnover) ; Phenylalanine ammonia-lyase ; Phenylpropanoid biosynthesisSource: Springer Online Journal Archives 1860-2000Topics: BiologyNotes: Abstract The extractable activity ofl-phenylalanine ammonia-lyase (PAL; EC 4.3.1.5) in cell suspension cultures of bean (Phaseolus vulgaris) is greatly induced following exposure to an elicitor preparation from the cell walls of the phytopathogenic fungusColletotrichum lindemuthianum. Following exogenous application oftrans-cinnamic acid (the product of the PAL reaction) to elicitor-induced cells, the activity of the enzyme rapidly declines. Loss of enzyme activity is accompanied by inhibition of the rate of synthesis of PAL subunits, as determined by [35S]methionine pulse-labelling followed by specific immunoprecipitation; this is insufficient to account for the rapid loss of PAL enzyme activity. Pulse-chase and immune blotting experiments indicate that cinnamic acid does not affect the rate of degradation of enzyme subunits, but rather mediates inactivation of the enzyme. A non-dialysable factor from cinnamicacid-treated bean cells stimulates removal of PAL activity from enzyme extracts in vitro; this effect is dependent on the presence of cinnamic acid. Such loss of enzyme activity in vitro is accompanied by an apparent loss or reduction of the dehydroalanine residue of the enzyme's active site, as detected by active-site-specific tritiation, although levels of immunoprecipitable enzyme subunits do not decrease. Furthermore, cinnamic-acid-mediated loss of enzyme activity in vivo is accompanied, in pulse-chase experiments, by a greater relative loss of35S-labelled enzyme subunits precipitated by an immobilised active-site affinity ligand than of subunits precipitated with anti-immunoglobulin G. It is therefore suggested that a possible mechanism for cinnamic-acid-mediated removal of PAL activity may involve modification of the dehydroalanine residue of the enzyme's active site.Type of Medium: Electronic ResourceURL: -
20Staff View
ISSN: 1432-2048Source: Springer Online Journal Archives 1860-2000Topics: BiologyNotes: Summary Exogenous supplies of phenylalanne, cinnamic acid and p-coumaric acid can inhibit the appearance of phenylalanine ammonia-lyase (PAL, E.C. 4.3.1.5) activity in potato tuber discs, and exogenous supplies of cinnamic acid and p-coumaric acid can inhibit the appearance of cinnamic acid 4-hydroxylase (CA4H, E.C. 1.14.13.11) activity. The time-courses of the inhibitory effects of (a) exogenous phenylalanine on the appearance of PAL activity and (b) exogenous cinnamic acid on the appearance of CA4H activity suggest that the respective substrates of the two enzymes have no inhibitory effects per se, but rather that metabolic derivatives are the active agents. Accordingly, cinnamic acid and p-coumaric acid, but not phenylalanine can inhibit the initial appearance of PAL activity. Similarly, p-coumaric acid but not cinnamic acid can inhibit the initial appearance of CA4H activity. The inhibitory effects of exogenous cinnamic acid and p-coumaric acid on the initial appearance of PAL activity are independent. These findings are discussed in relation to the control in vivo of the levels of activity of PAL and CA4H.Type of Medium: Electronic ResourceURL: