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Did you mean C. borhani (50 results)?
Optimised amylases extraction from oat seeds and its impact on bread properties.
Ben Halima N, Borchani M, Fendri I, Khemakhem B, Gosset D, Baril P, Pichon C, Ayadi MA, Abdelkafi S. Ben Halima N, et al. Int J Biol Macromol. 2015 Jan;72:1213-21. doi: 10.1016/j.ijbiomac.2014.10.018. Epub 2014 Oct 22. Int J Biol Macromol. 2015. PMID: 25453287
The application of the response surface methodology allows us to determine a set of optimal conditions (ratio seed weight/buffer volume 0.1, germination days 10 days, temperature 20 C and pH 5.6). Experiments carried out under these conditions led to amylase production yie …
The application of the response surface methodology allows us to determine a set of optimal conditions (ratio seed weight/buffer volume 0.1, …
BotIT6: a potent depressant insect toxin from Buthus occitanus tunetanus venom.
Mejri T, Borchani L, Srairi-Abid N, Benkhalifa R, Cestele S, Regaya I, Karoui H, Pelhate M, Rochat H, El Ayeb M. Mejri T, et al. Toxicon. 2003 Feb;41(2):163-71. doi: 10.1016/s0041-0101(02)00246-5. Toxicon. 2003. PMID: 12565735
When compared to other insect toxin sequences, BotIT6 present high similarities with depressant insect toxins with an additional arginine residue at the C-terminus and a methionine at position 27. The calculated net charge of BotIT6 is positive (+3) whereas it is negative …
When compared to other insect toxin sequences, BotIT6 present high similarities with depressant insect toxins with an additional arginine re …
Structural, magnetic and electrical properties of a new double-perovskite LaNaMnMoO6 material.
Borchani SM, Koubaa WC, Megdiche M. Borchani SM, et al. R Soc Open Sci. 2017 Nov 8;4(11):170920. doi: 10.1098/rsos.170920. eCollection 2017 Nov. R Soc Open Sci. 2017. PMID: 29291087 Free PMC article.
Magnetization versus temperature in a magnetic applied field of 0.05 T shows that our sample exhibits a paramagnetic-ferromagnetic transition with decreasing temperature. The Curie temperature T(C) is found to be 320 K. Arrott plots show that all our double-perovskite oxid …
Magnetization versus temperature in a magnetic applied field of 0.05 T shows that our sample exhibits a paramagnetic-ferromagnetic transitio …
Histopathological changes induced by Hemiscorpius lepturus scorpion venom in mice.
Heidarpour M, Ennaifer E, Ahari H, Srairi-Abid N, Borchani L, Khalili G, Amini H, Anvar AA, Boubaker S, El-Ayeb M, Shahbazzadeh D. Heidarpour M, et al. Toxicon. 2012 Mar 1;59(3):373-8. doi: 10.1016/j.toxicon.2011.12.011. Epub 2011 Dec 31. Toxicon. 2012. PMID: 22230352
In this work the LD50 of H. lepturus venom were determined by subcutaneous (SC) injection in white Balb/c mice (5 mg/kg). Histopathological alterations in organs such as kidney, heart, liver, lungs, stomach and intestine were determined in 3, 6, 12 and 24 h following exper …
In this work the LD50 of H. lepturus venom were determined by subcutaneous (SC) injection in white Balb/c mice (5 mg/kg). Histopathol …
Caulobacter crescentus synthesizes an S-layer-editing metalloprotease possessing a domain sharing sequence similarity with its paracrystalline S-layer protein.
Umelo-Njaka E, Bingle WH, Borchani F, Le KD, Awram P, Blake T, Nomellini JF, Smit J. Umelo-Njaka E, et al. J Bacteriol. 2002 May;184(10):2709-18. doi: 10.1128/JB.184.10.2709-2718.2002. J Bacteriol. 2002. PMID: 11976300 Free PMC article.
The S-layer protein (RsaA) is secreted by a type I mechanism (relying on a C-terminal signal) and is unusual among type I secreted proteins because high levels of protein are produced continuously. ...The N-terminal half of Sap possessed significant similarity to other typ …
The S-layer protein (RsaA) is secreted by a type I mechanism (relying on a C-terminal signal) and is unusual among type I secreted pr …
A new scorpion venom toxin paralytic to insects that affects Na+ channel activation. Purification, structure, antigenicity and mode of action.
Borchani L, Mansuelle P, Stankiewicz M, Grolleau F, Cestèle S, Karoui H, Lapied B, Rochat H, Pelhate M, el Ayeb M. Borchani L, et al. Eur J Biochem. 1996 Oct 15;241(2):525-32. doi: 10.1111/j.1432-1033.1996.00525.x. Eur J Biochem. 1996. PMID: 8917451 Free article.
This indicates that the binding site for BotIT2 is identical, contiguous or in allosteric interaction with that of AaHIT and depressant toxins. (c) The BotIT2 amino acid sequence shows strong similarity to depressant toxins. ...
This indicates that the binding site for BotIT2 is identical, contiguous or in allosteric interaction with that of AaHIT and depressant toxi …