scholarly journals Studies on structural elements contributing to the appearance of pheromone activity in the male eri-silk moth, Samia cynthia ricini. Part I. Synthesis of(6Z,10Z,12E)-6,10,12-hexadecatrienal, a compound with a similar structure to the eri-silk moth pheromone.

1991 ◽  
Vol 55 (4) ◽  
pp. 1131-1132 ◽  
Author(s):  
Ichiro TOMIDA ◽  
Taiki MATSUNAGA
Keyword(s):  
Structural Elements ◽  
Silk Moth ◽  
Pheromone Activity ◽  
Eri Silk

scholarly journals EFFECT OF MATING DURATION ON FECUNDITY (REPRODUCTIVE PARAMETER) OF ERI SILK MOTH PHILOSAMIA RICINI IN DIFFERENT SEASONS

2015 ◽  
Vol 3 (9SE) ◽  
pp. 1-3
Author(s):  
Rajkumari Batham ◽  
Ulka Yadav
Keyword(s):  
Reproductive Parameter ◽  
Philosamia Ricini ◽  
Mating Duration ◽  
Fecundity Rate ◽  
Silk Moth ◽  
Different Seasons ◽  
Eri Silk

Production of viable eggs in the Eri silkworm, Philosamiaricini is influenced by the mating activity.The effect of coupling duration on the fecundity of Eri silkworm, Philosamiaricini during different seasons was studied. Fecundity rate inEri silkworm, PhilosamiaRicinidoes notsignificant variation with increase in mating duration were observed different season.

scholarly journals Composition and Diversity of Gut Bacteria Associated with the Eri Silk Moth, Samia ricini, (Lepidoptera: Saturniidae) as Revealed by Culture-Dependent and Metagenomics Analysis

2020 ◽  
Vol 30 (9) ◽  
pp. 1367-1378
Author(s):  
Kondwani MsangoSoko ◽  
Sakshi Gandotra ◽  
Rahul Kumar Chandel ◽  
Kirti Sharma ◽  
Balasubramanian Ramakrishinan ◽  
...  
Keyword(s):  
Gut Bacteria ◽  
Silk Moth ◽  
Eri Silk ◽  
Metagenomics Analysis ◽  
Culture Dependent

Structural phenomena in the growth of carbon nanotubes

1993 ◽  
Vol 51 ◽  
pp. 750-751
Author(s):  
Jun Jiao
Keyword(s):  
Carbon Nanotubes ◽  
Growth Mechanism ◽  
Carbonaceous Material ◽  
Cluster Growth ◽  
Structural Elements ◽  
Rich Variety ◽  
Different Shapes ◽  
Point To Point

HREM studies of the carbonaceous material deposited on the cathode of a Huffman-Krätschmer arc reactor have shown a rich variety of multiple-walled nano-clusters of different shapes and forms. The preparation of the samples, as well as the variety of cluster shapes, including triangular, rhombohedral and pentagonal projections, are described elsewhere.The close registry imposed on the nanotubes, focuses attention on the cluster growth mechanism. The strict parallelism in the graphitic separation of the tube walls is maintained through changes of form and size, often leading to 180° turns, and accommodating neighboring clusters and defects. Iijima et. al. have proposed a growth scheme in terms of pentagonal and heptagonal defects and their combinations in a hexagonal graphitic matrix, the first bending the surface inward, and the second outward. We report here HREM observations that support Iijima’s suggestions, and add some new features that refine the interpretation of the growth mechanism. The structural elements of our observations are briefly summarized in the following four micrographs, taken in a Hitachi H-8100 TEM operating at an accelerating voltage of 200 kV and with a point-to-point resolution of 0.20 nm.

Designing TIMP (tissue inhibitor of metalloproteinases) variants that are selective metalloproteinase inhibitors

2003 ◽  
Vol 70 ◽  
pp. 201-212 ◽  
Author(s):  
Hideaki Nagase ◽  
Keith Brew
Keyword(s):  
Three Dimensional ◽  
Therapeutic Interventions ◽  
Tissue Inhibitors Of Metalloproteinases ◽  
Structural Basis ◽  
Structural Elements ◽  
Ridge Structure ◽  
Extracellular Matrix Components ◽  
Metalloproteinase Inhibitors ◽  
The Matrix ◽  
A Disintegrin And Metalloproteinase

The tissue inhibitors of metalloproteinases (TIMPs) are endogenous inhibitors of the matrix metalloproteinases (MMPs), enzymes that play central roles in the degradation of extracellular matrix components. The balance between MMPs and TIMPs is important in the maintenance of tissues, and its disruption affects tissue homoeostasis. Four related TIMPs (TIMP-1 to TIMP-4) can each form a complex with MMPs in a 1:1 stoichiometry with high affinity, but their inhibitory activities towards different MMPs are not particularly selective. The three-dimensional structures of TIMP-MMP complexes reveal that TIMPs have an extended ridge structure that slots into the active site of MMPs. Mutation of three separate residues in the ridge, at positions 2, 4 and 68 in the amino acid sequence of the N-terminal inhibitory domain of TIMP-1 (N-TIMP-1), separately and in combination has produced N-TIMP-1 variants with higher binding affinity and specificity for individual MMPs. TIMP-3 is unique in that it inhibits not only MMPs, but also several ADAM (a disintegrin and metalloproteinase) and ADAMTS (ADAM with thrombospondin motifs) metalloproteinases. Inhibition of the latter groups of metalloproteinases, as exemplified with ADAMTS-4 (aggrecanase 1), requires additional structural elements in TIMP-3 that have not yet been identified. Knowledge of the structural basis of the inhibitory action of TIMPs will facilitate the design of selective TIMP variants for investigating the biological roles of specific MMPs and for developing therapeutic interventions for MMP-associated diseases.

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