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Study of itaconic acid production by Aspergillus terrus MJL05 strain with different variable

Autor: Juy, M. I., Orejas, J. A., Lucca, M. E.

Publikováno v: Revista Colombiana de Biotecnología, Volume: 12, Issue: 2, Pages: 187-193, Published: DEC 2010

Itaconic acid (IA) production by Aspergillus terreus MJL05 strain was investigated in submerged batch fermentation in a stirred bioreactor to determine the effect of varying the nitrogen, phosphorous and carbon sources concentrations in the productio

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od_______618::96455ceac4b85fa875fe13932cab0e02
http://www.scielo.org.co/scielo.php?script=sci_arttext&pid=S0123-34752010000200015&lng=en&tlng=en

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Solid state NMR sequential resonance assignments and conformational analysis of the 2 x 10.4 kDa dimeric form of the Bacillus subtilis protein Crh

Autor: Boeckmann, A., Lange, A., Galinier, A., Luca, S., Giraud, N., Juy, M., Heise, H., Montserret, R., Penin, F., Baldus, M.

Publikováno v: Journal of Biomolecular NMR

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od______1874::677501658aa0332c0bc473c3f8c0944c
https://hdl.handle.net/11858/00-001M-0000-0028-DD2F-611858/00-001M-0000-0012-EF95-1

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Solid state NMR sequential resonance assignments and conformational analysis of the 2x10.4 kDa dimeric form of the Bacillus subtilis protein Crh

Autor: Anja Böckmann, Lange, A., Galinier, A., Luca, S., Giraud, N., Juy, M., Heise, H., Montserret, R., Penin, F., Baldus, M.

Publikováno v: J Biomol NMR
J Biomol NMR, 2003, 27, pp.323-339
HAL

International audience; Solid state NMR sample preparation and resonance assignments of the U-[13C,15N] 2x10.4 kDa dimeric form of the regulatory protein Crh in microcrystalline, PEG precipitated form are presented. Intra- and interresidue correlatio

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::1cb0583e39c4a0e3b20e2e138dc74142
https://hal.archives-ouvertes.fr/hal-00313695

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Type II protein secretion in gram-negative pathogenic bacteria: the study of the structure/secretion relationships of the cellulase cel5 (formerly EGZ) from Erwinia chrysanthemi

Autor: virginie chapon, Czjzek, M., Elhassouni, M., Py, B., Juy, M., Barras, F.

Publikováno v: Journal of Molecular Biology
Journal of Molecular Biology, 2001, 310 (5), pp.1055-1066. ⟨10.1006/jmbi.2001.4787⟩
Journal of Molecular Biology, Elsevier, 2001, 310 (5), pp.1055-1066. ⟨10.1006/jmbi.2001.4787⟩
Journal of Molecular Biology, Elsevier, 2001, 310, pp.1055-1066
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International audience; Erwinia chrysanthemi, a Gram-negative plant pathogen, secretes the cellulase Cel5 (formerly EGZ) via the type II secretion pathway (referred to as Out). Cel5 is composed of two domains, a large N-terminal catalytic domain (390

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::28182b56ce8de82fad5c983bc4963349
https://amu.hal.science/hal-01560909

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Amylose chain behavior in an interacting context II. Molecular modeling of a maltopentaose fragment in the barley alpha-amylase catalytic site

Autor: Andre, G., Buleon, A., Juy, M., Nushin Aghajari, Haser, R., Xxxx Tranv

Publikováno v: Biopolymers
Biopolymers, Wiley, 1999, 49, pp.107-119
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International audience; xxx

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::a57569fae5611cf48b1084f9dcd41d54
https://hal.archives-ouvertes.fr/hal-00314552

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Amylose chain behavior in an interacting context. 2- Molecular modeling of a maltopentaose fragment in the barley alpha-amylase catalytic site

Autor: André, G., Buléon, A., Juy, M., Aghajari, N., Haser, R., Tran, V.

Publikováno v: Biopolymers
Biopolymers, Wiley, 1999, 49, pp.107-119
Biopolymers (49), 107-119. (1999)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::e4d6478ca2097a35b51e8c2fba5651bf
https://hal.inrae.fr/hal-02695441

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Barley alpha-amylase bound to its endogenous protein inhibitor BASI: crystal structure of the complex at 1.9 A resolution

Autor: Vallee, F., Kadziola, A., Bourne, Yves, Juy, M., Rodenburg, Kw, Svensson, B., Haser, R.

Publikováno v: Structure
Structure, Elsevier (Cell Press), 1998, 6, pp.649-659

International audience; BACKGROUND: Barley alpha-amylase is a 45 kDa enzyme which is involved in starch degradation during barley seed germination. The released sugars provide the plant embryo with energy for growth. The major barley alpha-amylase is

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::2329710fde0575ac1cf5718e0127b6db
https://hal.archives-ouvertes.fr/hal-00313562

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Crystallization of the catalytic domain of Clostridium cellulolyticum CeLF cellulase in the presence of a newly synthesized cellulase inhibitor

Autor: Reverbel-Leroy, C., Parsiegla, G., Moreau, V., Juy, M., Tardif, C., Driguez, H., Belaich, J.P., Haser, R.

Publikováno v: Acta Crystallogr. Sect. D-Biol. Crystallogr.
Acta Crystallogr. Sect. D-Biol. Crystallogr., 1998, pp.114-118

The catalytic domain of the CeIF processive endocellulase, a family 48 glycosyl hydrolase from Clostridium cellulolyticum has been crystallized in the presence of a newly synthesized inhibitor (methyl 4-S-beta-cellobiosyl-4-thio-beta-cellobioside), b

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::b61c7d5fb3458fce4a7294bc68fc01a9
https://hal.archives-ouvertes.fr/hal-00313560

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