Neil Crickmore

Dr. Neil Crickmore

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Research Focus & Metrics

Academic Career Length

41Years (1986-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

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1 September 1998 in Microbiology and Molecular Biology Reviews
Verified
Journal Article
Closed access
PDF file
ESE. Schnepf
E. Schnepf
NCNeil Crickmore
Neil Crickmore
JRJ. Van Rie
J. Van Rie
DLD. Lereclus
D. Lereclus
JBJ. Baum
J. Baum
DDD. H. Dean
D. H. Dean
SUMMARY: During the past decade the pesticidal bacterium Bacillus thuringiensis has been the subject of intensive research. These efforts have yielded considerable data about the complex relationships between the structure, mechanism of action, and genetics of the organism’s pesticidal crystal proteins, and a coherent picture of these relationships is beginning to emerge. Other studies have focused on the ecological role of the B. thuringiensis crystal proteins, their performance in agricultural and other natural settings, and the evolution of resistance mechanisms in target pests. Armed with this knowledge base and with the tools of modern biotechnology, researchers are now reporting promising results in engineering more-useful toxins and formulations, in creating transgenic plants that express pesticidal activity, and in constructing integrated management strategies to insure that these products are utilized with maximum efficiency and benefit.

1 September 1998 in Microbiology and Molecular Biology Reviews
Verified
Journal Article
Closed access
PDF file
NCNeil Crickmore
Neil Crickmore
DZD. R. Zeigler
D. R. Zeigler
JFJ. Feitelson
J. Feitelson
ESE. Schnepf
E. Schnepf
JRJ. Van Rie
J. Van Rie
DDD. H. Dean
D. H. Dean
SUMMARY: The crystal proteins of Bacillus thuringiensis have been extensively studied because of their pesticidal properties and their high natural levels of production. The increasingly rapid characterization of new crystal protein genes, triggered by an effort to discover proteins with new pesticidal properties, has resulted in a variety of sequences and activities that no longer fit the original nomenclature system proposed in 1989. Bacillus thuringiensis pesticidal crystal protein (Cry and Cyt) nomenclature was initially based on insecticidal activity for the primary ranking criterion. Many exceptions to this systematic arrangement have become apparent, however, making the nomenclature system inconsistent. Additionally, the original nomenclature, with four activity-based primary ranks for 13 genes, did not anticipate the current 73 holotype sequences that form many more than the original four subgroups. A new nomenclature, based on hierarchical clustering using amino acid sequence identity, is proposed. Roman numerals have been exchanged for Arabic numerals in the primary rank (e.g., Cry1Aa) to better accommodate the large number of expected new sequences. In this proposal, 133 crystal proteins comprising 24 primary ranks are systematically arranged.

19 January 2015 in Nature Biotechnology
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Journal Article
Closed access
YCYves Carrière
Yves Carrière
NCNeil Crickmore
Neil Crickmore
BTBruce E Tabashnik
Bruce E Tabashnik

1 November 2021 in Journal of Invertebrate Pathology
Verified
Journal Article
Open access
NCNeil Crickmore
Neil Crickmore
CBColin Berry
Colin Berry
SKSuresh Kannan
Suresh Kannan
RMRuchir Mishra
Ruchir Mishra
TCThomas R. Connor
Thomas R. Connor
BBBryony C. Bonning
Bryony C. Bonning
In 1998 a nomenclature for the growing list of pesticidal proteins from Bacillus thuringiensis (Bt) was derived based solely on protein sequence comparisons. This nomenclature was widely adopted and provided a robust framework for the naming and classification of the proteins. The success of these proteins in integrated pest management schemes prompted an increased effort to find others with improved or more diverse activities. These discovery activities led to the characterization of proteins from a wider range of bacteria and with a variety of different protein folds. Since most of these new proteins were grouped together as Cry proteins it became apparent that the existing nomenclature had limitations in representing the diverse range of proteins that had been identified. This revised nomenclature retains the basic principles of the 1998 version but provides specific mnemonics to represent different structural groups. For the purposes of consistency, the vast majority of the proteins have either retained their name or have a new name that clearly references the previous one. Other pesticidal proteins not previously included in the nomenclature have been incorporated into this version.

1 May 2010 in Trends in Microbiology
Verified
Journal Article
Closed access
BRBen Raymond
Ben Raymond
PJPaul R. Johnston
Paul R. Johnston
CNChristina Nielsen-LeRoux
Christina Nielsen-LeRoux
DLDidier Lereclus
Didier Lereclus
NCNeil Crickmore
Neil Crickmore

1 February 1994 in Molecular Microbiology
Verified
Journal Article
Closed access
PDF file
PKPeter J. K. Knight
Peter J. K. Knight
NCNeil Crickmore
Neil Crickmore
DEDavid J. Ellar
David J. Ellar