2024-03-29T08:29:29Zhttp://repository.helmholtz-hzi.de/oai/requestoai:repository.helmholtz-hzi.de:10033/85992019-08-30T11:24:25Zcom_10033_6835com_10033_6832col_10033_6836
Li, Zu-Yi
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2007-02-20T12:51:47Z
1984-09
Applied and Environmental Microbiology 1984 48(3):610-617
0099-2240
1098-5336
http://hdl.handle.net/10033/8599
16346628
en_US
Copyright © 1984, American Society for Microbiology
Formation and Identification of Interfacial-Active Glycolipids from Resting Microbial Cells
YES
2018-06-13T19:43:34Z
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Helmholtz Zentrum für Infektionsforschung Repository
hzi@openrepository.com
oai:repository.helmholtz-hzi.de:10033/86902019-08-30T11:25:07Zcom_10033_6835com_10033_6832col_10033_6836
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2007-02-21T08:28:25Z
1987-03
Plant Physiology 1987 83(3):475-478
0032-0889
1532-2548
http://hdl.handle.net/10033/8690
1056389
en_US
Enzymic Synthesis of Caffeoylglucaric Acid from Chlorogenic Acid and Glucaric Acid by a Protein Preparation from Tomato Cotyledons 1
YES
2018-06-13T00:27:52Z
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Helmholtz Zentrum für Infektionsforschung Repository
hzi@openrepository.com
oai:repository.helmholtz-hzi.de:10033/185922019-08-30T11:32:37Zcom_10033_6835com_10033_6832col_10033_6836
Gutzeit, D.
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Jerz, Gerold
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2008-02-18T09:58:22Z
2008-02-18T09:58:22Z
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(2007) Chromatographia 65 (1-2); pp. 1-7
00095893
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10.1365/s10337-006-0105-6
http://hdl.handle.net/10033/18592
Chromatographia 65 (1-2); pp. 1-7
null
Springer Science Business Media
Preparative Isolation and Purification of Flavonoids and Protocatechuic Acid from Sea Buckthorn Juice Concentrate (Hippophae rhamnoides) by High-Speed Counter-Current Chromatography
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Helmholtz Zentrum für Infektionsforschung Repository
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oai:repository.helmholtz-hzi.de:10033/229332019-08-30T11:37:23Zcom_10033_6835com_10033_6832col_10033_6836
Scheibner, M
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Hülsdau, B
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Zelena, K
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Nimtz, M
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de Boer, L
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Berger, RG
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Zorn, H
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Zentrum Angewandte Chemie, Institut für Lebensmittelchemie der Universität Hannover, Wunstorfer Straße 14, 30453, Hannover, Germany.
2008-04-10T14:42:13Z
2008-04-10T14:42:13Z
2008-01
Novel peroxidases of Marasmius scorodonius degrade beta-carotene. 2008, 77 (6):1241-1250 Appl. Microbiol. Biotechnol.
0175-7598
18038130
10.1007/s00253-007-1261-9
http://hdl.handle.net/10033/22933
Applied microbiology and biotechnology
Two extracellular enzymes (MsP1 and MsP2) capable of efficient beta-carotene degradation were purified from culture supernatants of the basidiomycete Marasmius scorodonius (garlic mushroom). Under native conditions, the enzymes exhibited molecular masses of ~150 and ~120 kDa, respectively. SDS-PAGE and mass spectrometric data suggested a composition of two identical subunits for both enzymes. Biochemical characterisation of the purified proteins showed isoelectric points of 3.7 and 3.5, and the presence of heme groups in the active enzymes. Partial amino acid sequences were derived from N-terminal Edman degradation and from mass spectrometric ab initio sequencing of internal peptides. cDNAs of 1,604 to 1,923 bp, containing open reading frames (ORF) of 508 to 513 amino acids, respectively, were cloned from a cDNA library of M. scorodonius. These data suggest glycosylation degrees of ~23% for MsP1 and 8% for MsP2. Databank homology searches revealed sequence homologies of MsP1 and MsP2 to unusual peroxidases of the fungi Thanatephorus cucumeris (DyP) and Termitomyces albuminosus (TAP).
ENG
Novel peroxidases of Marasmius scorodonius degrade beta-carotene.
Article
2018-06-13T19:31:11Z
Two extracellular enzymes (MsP1 and MsP2) capable of efficient beta-carotene degradation were purified from culture supernatants of the basidiomycete Marasmius scorodonius (garlic mushroom). Under native conditions, the enzymes exhibited molecular masses of ~150 and ~120 kDa, respectively. SDS-PAGE and mass spectrometric data suggested a composition of two identical subunits for both enzymes. Biochemical characterisation of the purified proteins showed isoelectric points of 3.7 and 3.5, and the presence of heme groups in the active enzymes. Partial amino acid sequences were derived from N-terminal Edman degradation and from mass spectrometric ab initio sequencing of internal peptides. cDNAs of 1,604 to 1,923 bp, containing open reading frames (ORF) of 508 to 513 amino acids, respectively, were cloned from a cDNA library of M. scorodonius. These data suggest glycosylation degrees of ~23% for MsP1 and 8% for MsP2. Databank homology searches revealed sequence homologies of MsP1 and MsP2 to unusual peroxidases of the fungi Thanatephorus cucumeris (DyP) and Termitomyces albuminosus (TAP).
CC-LICENSE
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Generated Thumbnail
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Generated Thumbnail
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false
Figure3.jpg.jpg
Figure3.jpg.jpg
Generated Thumbnail
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MD5
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false
Figure5.jpg.jpg
Figure5.jpg.jpg
Generated Thumbnail
image/jpeg
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https://hzi.openrepository.com/bitstream/10033/22933/34/Figure5.jpg.jpg
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MD5
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false
Scheibner_final.pdf.jpg
Scheibner_final.pdf.jpg
Generated Thumbnail
image/jpeg
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MD5
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false
figure4.pdf.jpg
figure4.pdf.jpg
Generated Thumbnail
image/jpeg
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https://hzi.openrepository.com/bitstream/10033/22933/38/figure4.pdf.jpg
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MD5
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false
TEXT
Scheibner_final.pdf.txt
Scheibner_final.pdf.txt
Extracted Text
text/plain
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https://hzi.openrepository.com/bitstream/10033/22933/25/Scheibner_final.pdf.txt
cdf798a5c410cef1691613501417b97a
MD5
25
false
figure4.pdf.txt
figure4.pdf.txt
Extracted Text
text/plain
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https://hzi.openrepository.com/bitstream/10033/22933/26/figure4.pdf.txt
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MD5
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false
Table 1_new.doc.txt
Table 1_new.doc.txt
Extracted text
text/plain
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https://hzi.openrepository.com/bitstream/10033/22933/27/Table%201_new.doc.txt
c9a6532b4bfe79ca5f83ae1ae1cea97e
MD5
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false
Table 2_new.doc.txt
Table 2_new.doc.txt
Extracted text
text/plain
275
https://hzi.openrepository.com/bitstream/10033/22933/28/Table%202_new.doc.txt
3f20191178c4331a4a89c533b32664f6
MD5
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false
CONVERTED2_44257
CONVERTED2_44258
10033/22933
oai:hzi.openrepository.com:10033/22933
2019-08-30 11:37:23.969
Helmholtz Zentrum für Infektionsforschung Repository
hzi@openrepository.com
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oai:repository.helmholtz-hzi.de:10033/2394712019-08-30T11:26:13Zcom_10033_6835com_10033_6832col_10033_6836
Ebrahim, Weaam
65767e64e0482b6442dca1ce6d2da72a
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Kjer, Julia
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El Amrani, Mustapha
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Wray, Victor
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500
Lin, Wenhan
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500
Ebel, Rainer
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500
Lai, Daowan
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Proksch, Peter
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Institute of Pharmaceutical Biology and Biotechnology, Heinrich-Heine University, Universitaetsstrasse 1, D-40225 Duesseldorf, Germany; Email: weel-001@uni-duesseldorf.de or weaamnabil@mans.edu.eg (W.E.); jacob.julia@web.de (J.K.); mustapha.elamrani@uni-duesseldorf.de (M.E.A.).
2012-08-22T13:01:10Z
2012-08-22T13:01:10Z
2012-05
Pullularins E and F, Two New Peptides from the Endophytic Fungus Bionectria ochroleuca Isolated from the Mangrove Plant Sonneratia caseolaris. 2012, 10 (5):1081-91 Mar Drugs
1660-3397
22822358
10.3390/md10051081
http://hdl.handle.net/10033/239471
Marine drugs
Chemical investigation of the EtOAc extract of the endophytic fungus Bionectria ochroleuca, isolated from the inner leaf tissues of the plant Sonneratia caseolaris (Sonneratiaceae) from Hainan island (China), yielded two new peptides, pullularins E and F (1 and 2) together with three known compounds (3-5). The structures of the new compounds were unambiguously determined on the basis of one- and two-dimensional NMR spectroscopy as well as by high-resolution mass spectrometry. The absolute configurations of amino acids were determined by HPLC analysis of acid hydrolysates using Marfey's method. The isolated compounds exhibited pronounced to moderate cytotoxic activity against the mouse lymphoma cells (L5178Y) with EC(50) values ranging between 0.1 and 6.7 µg/mL.
en
Archived with thanks to Marine drugs
Pullularins E and F, Two New Peptides from the Endophytic Fungus Bionectria ochroleuca Isolated from the Mangrove Plant Sonneratia caseolaris.
Article
2018-06-13T15:56:03Z
Chemical investigation of the EtOAc extract of the endophytic fungus Bionectria ochroleuca, isolated from the inner leaf tissues of the plant Sonneratia caseolaris (Sonneratiaceae) from Hainan island (China), yielded two new peptides, pullularins E and F (1 and 2) together with three known compounds (3-5). The structures of the new compounds were unambiguously determined on the basis of one- and two-dimensional NMR spectroscopy as well as by high-resolution mass spectrometry. The absolute configurations of amino acids were determined by HPLC analysis of acid hydrolysates using Marfey's method. The isolated compounds exhibited pronounced to moderate cytotoxic activity against the mouse lymphoma cells (L5178Y) with EC(50) values ranging between 0.1 and 6.7 µg/mL.
ORIGINAL
Ebrahim et al_final.pdf
Ebrahim et al_final.pdf
allowed publisher's PDF
application/pdf
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https://hzi.openrepository.com/bitstream/10033/239471/1/Ebrahim%20et%20al_final.pdf
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MD5
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true
CC-LICENSE
license_url
license_url
text/plain
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https://hzi.openrepository.com/bitstream/10033/239471/2/license_url
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false
license_text
license_text
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license_rdf
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https://hzi.openrepository.com/bitstream/10033/239471/4/license_rdf
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LICENSE
license.txt
license.txt
text/plain
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https://hzi.openrepository.com/bitstream/10033/239471/5/license.txt
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MD5
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false
TEXT
Ebrahim et al_final.pdf.txt
Ebrahim et al_final.pdf.txt
Extracted Text
text/plain
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https://hzi.openrepository.com/bitstream/10033/239471/8/Ebrahim%20et%20al_final.pdf.txt
6e19f971da3fb499616d37aa3b7a0d92
MD5
8
false
THUMBNAIL
Ebrahim et al_final.pdf.jpg
Ebrahim et al_final.pdf.jpg
Generated Thumbnail
image/jpeg
33420
https://hzi.openrepository.com/bitstream/10033/239471/9/Ebrahim%20et%20al_final.pdf.jpg
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MD5
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false
10033/239471
oai:hzi.openrepository.com:10033/239471
2019-08-30 11:26:13.066
Helmholtz Zentrum für Infektionsforschung Repository
hzi@openrepository.com
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oai:repository.helmholtz-hzi.de:10033/2938552019-08-30T11:28:45Zcom_10033_6835com_10033_6832col_10033_6836
Ibrahim, Sabrin R. M.
a16a7da30547b93f43ad70d33d038788
500
Edrada-Ebel, RuAngelie
f5c0f333e6b2fd0c8e494d50ede38ecc
500
Mohamed,Gamal A.
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500
Youssef, Diaa T. A
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500
Wray, Victor
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Proksch, Peter
a6d8b7364b40f5f2490c9c05bc0e2e9a
500
Helmholz Centre for Infection research, D-38124 Braunschweig, Germany
2013-06-12T08:37:36Z
2013-06-12T08:37:36Z
2008-04-16
2008-01
Callyaerin G, a new cytotoxic cyclic peptide from the marine sponge Callyspongia aerizusa 2008, 2008 (12):164 Arkivoc
1551-7012
1551-7012
10.3998/ark.5550190.0009.c18
http://hdl.handle.net/10033/293855
Arkivoc
Arkat
http://hdl.handle.net/2027/spo.5550190.0009.c18
Archived with thanks to Arkivoc
Callyaerin G, a new cytotoxic cyclic peptide from the marine sponge Callyspongia aerizusa
Article
2018-06-13T14:11:34Z
LICENSE
license.txt
license.txt
text/plain
1685
https://hzi.openrepository.com/bitstream/10033/293855/5/license.txt
cb598eeb10bfed09d26fd8d285172ad4
MD5
5
false
ORIGINAL
Ibrahim et al_final.pdf
Ibrahim et al_final.pdf
Open Access publication
application/pdf
203171
https://hzi.openrepository.com/bitstream/10033/293855/1/Ibrahim%20et%20al_final.pdf
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MD5
1
true
CC-LICENSE
license_text
license_text
application/octet-stream
0
https://hzi.openrepository.com/bitstream/10033/293855/3/license_text
d41d8cd98f00b204e9800998ecf8427e
MD5
3
false
license_url
license_url
text/plain
49
https://hzi.openrepository.com/bitstream/10033/293855/2/license_url
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MD5
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false
license_rdf
license_rdf
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https://hzi.openrepository.com/bitstream/10033/293855/4/license_rdf
306824103cdab5a2460a7737d9c97e69
MD5
4
false
TEXT
Ibrahim et al_final.pdf.txt
Ibrahim et al_final.pdf.txt
Extracted Text
text/plain
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https://hzi.openrepository.com/bitstream/10033/293855/8/Ibrahim%20et%20al_final.pdf.txt
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MD5
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THUMBNAIL
Ibrahim et al_final.pdf.jpg
Ibrahim et al_final.pdf.jpg
Generated Thumbnail
image/jpeg
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https://hzi.openrepository.com/bitstream/10033/293855/9/Ibrahim%20et%20al_final.pdf.jpg
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MD5
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10033/293855
oai:hzi.openrepository.com:10033/293855
2019-08-30 11:28:45.284
Helmholtz Zentrum für Infektionsforschung Repository
hzi@openrepository.com
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oai:repository.helmholtz-hzi.de:10033/3025902019-08-30T11:33:55Zcom_10033_6835com_10033_6832col_10033_6836
Wang, Jian-ping
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Lin, Wenhan
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Wray, Victor
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Lai, Daowan
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Proksch, Peter
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2013-10-01T14:53:25Z
2013-10-01T14:53:25Z
2013-10-01
Induced production of depsipeptides by co-culturing Fusarium tricinctum and Fusarium begoniae 2013, 54 (20):2492 Tetrahedron Letters
00404039
10.1016/j.tetlet.2013.03.005
http://hdl.handle.net/10033/302590
Tetrahedron Letters
http://linkinghub.elsevier.com/retrieve/pii/S0040403913003869
Archived with thanks to Tetrahedron Letters
Induced production of depsipeptides by co-culturing Fusarium tricinctum and Fusarium begoniae
Article
2018-06-13T15:12:11Z
ORIGINAL
Wang et al_final.pdf
Wang et al_final.pdf
original manuscript
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TEXT
Wang et al_final.pdf.txt
Wang et al_final.pdf.txt
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THUMBNAIL
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2019-08-30 11:33:55.066
Helmholtz Zentrum für Infektionsforschung Repository
hzi@openrepository.com
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oai:repository.helmholtz-hzi.de:10033/5612262019-08-30T11:28:23Zcom_10033_6835com_10033_6832col_10033_6836
Stoppok, W
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Rapp, P
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Wagner, F
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Gesellschaft fur Biotechnologische Forschung mbH, D-38124 Braunschweig, Germany.
2015-07-30T09:13:38Z
2015-07-30T09:13:38Z
1982-07
Formation, Location, and Regulation of Endo-1,4-beta-Glucanases and beta-Glucosidases from Cellulomonas uda. 1982, 44 (1):44-53 Appl. Environ. Microbiol.
0099-2240
16346067
http://hdl.handle.net/10033/561226
Applied and environmental microbiology
The formation and location of endo-1,4-beta-glucanases and beta-glucosidases were studied in cultures of Cellulomonas uda grown on microcrystalline cellulose, carboxymethyl cellulose, printed newspaper, and some mono- or disaccharides. Endo-1,4-Glucanases were found to be extracellular, but a very small amount of cell-bound endo-1,4-beta-glucanase was considered to be the basal endoglucanase level of the cells. The formation of extracellular endo-1,4-beta-glucanases was induced by cellobiose and repressed by glucose. Extracellular endoglucanase activity was inhibited by cellobiose but not by glucose. beta-Glucosidases, on the other hand, were formed constitutively and found to be cell bound. beta-Glucosidase activity was inhibited noncompetitively by glucose. Some characteristics such as the optimal pH for and the thermostability of the endoglucanases and beta-glucosidases and the end products of cellulose degradation were determined.
en
Formation, Location, and Regulation of Endo-1,4-beta-Glucanases and beta-Glucosidases from Cellulomonas uda.
Article
2018-06-13T15:12:46Z
The formation and location of endo-1,4-beta-glucanases and beta-glucosidases were studied in cultures of Cellulomonas uda grown on microcrystalline cellulose, carboxymethyl cellulose, printed newspaper, and some mono- or disaccharides. Endo-1,4-Glucanases were found to be extracellular, but a very small amount of cell-bound endo-1,4-beta-glucanase was considered to be the basal endoglucanase level of the cells. The formation of extracellular endo-1,4-beta-glucanases was induced by cellobiose and repressed by glucose. Extracellular endoglucanase activity was inhibited by cellobiose but not by glucose. beta-Glucosidases, on the other hand, were formed constitutively and found to be cell bound. beta-Glucosidase activity was inhibited noncompetitively by glucose. Some characteristics such as the optimal pH for and the thermostability of the endoglucanases and beta-glucosidases and the end products of cellulose degradation were determined.
ORIGINAL
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TEXT
Stoppok et al_final.pdf.txt
Stoppok et al_final.pdf.txt
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THUMBNAIL
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Generated Thumbnail
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2019-08-30 11:28:23.895
Helmholtz Zentrum für Infektionsforschung Repository
hzi@openrepository.com
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oai:repository.helmholtz-hzi.de:10033/6206962019-08-30T11:26:13Zcom_10033_6835com_10033_6832col_10033_6836
Sharma, Alok
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500
Bruns, Karsten
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Röder, René
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Henklein, Peter
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Votteler, Jörg
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Wray, Victor
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Schubert, Ulrich
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2017-01-13T09:49:46Z
2017-01-13T09:49:46Z
2009-12-17
2015-09-04T08:31:10Z
BMC Structural Biology. 2009 Dec 17;9(1):74
http://dx.doi.org/10.1186/1472-6807-9-74
http://hdl.handle.net/10033/620696
Abstract Background The equine infection anemia virus (EIAV) p9 Gag protein contains the late (L-) domain required for efficient virus release of nascent virions from the cell membrane of infected cell. Results In the present study the p9 protein and N- and C-terminal fragments (residues 1-21 and 22-51, respectively) were chemically synthesized and used for structural analyses. Circular dichroism and 1H-NMR spectroscopy provide the first molecular insight into the secondary structure and folding of this 51-amino acid protein under different solution conditions. Qualitative 1H-chemical shift and NOE data indicate that in a pure aqueous environment p9 favors an unstructured state. In its most structured state under hydrophobic conditions, p9 adopts a stable helical structure within the C-terminus. Quantitative NOE data further revealed that this α-helix extends from Ser-27 to Ser-48, while the N-terminal residues remain unstructured. The structural elements identified for p9 differ substantially from that of the functional homologous HIV-1 p6 protein. Conclusions These structural differences are discussed in the context of the different types of L-domains regulating distinct cellular pathways in virus budding. EIAV p9 mediates virus release by recruiting the ALG2-interacting protein X (ALIX) via the YPDL-motif to the site of virus budding, the counterpart of the YPXnL-motif found in p6. However, p6 contains an additional PTAP L-domain that promotes HIV-1 release by binding to the tumor susceptibility gene 101 (Tsg101). The notion that structures found in p9 differ form that of p6 further support the idea that different mechanisms regulate binding of ALIX to primary versus secondary L-domains types.
Solution structure of the Equine Infectious Anemia Virus p9 protein: a rationalization of its different ALIX binding requirements compared to the analogous HIV-p6 protein
Journal Article
en
Sharma et al.
2018-06-13T00:56:30Z
Abstract
Background
The equine infection anemia virus (EIAV) p9 Gag protein contains the late (L-) domain required for efficient virus release of nascent virions from the cell membrane of infected cell.
Results
In the present study the p9 protein and N- and C-terminal fragments (residues 1-21 and 22-51, respectively) were chemically synthesized and used for structural analyses. Circular dichroism and 1H-NMR spectroscopy provide the first molecular insight into the secondary structure and folding of this 51-amino acid protein under different solution conditions. Qualitative 1H-chemical shift and NOE data indicate that in a pure aqueous environment p9 favors an unstructured state. In its most structured state under hydrophobic conditions, p9 adopts a stable helical structure within the C-terminus. Quantitative NOE data further revealed that this α-helix extends from Ser-27 to Ser-48, while the N-terminal residues remain unstructured. The structural elements identified for p9 differ substantially from that of the functional homologous HIV-1 p6 protein.
Conclusions
These structural differences are discussed in the context of the different types of L-domains regulating distinct cellular pathways in virus budding. EIAV p9 mediates virus release by recruiting the ALG2-interacting protein X (ALIX) via the YPDL-motif to the site of virus budding, the counterpart of the YPXnL-motif found in p6. However, p6 contains an additional PTAP L-domain that promotes HIV-1 release by binding to the tumor susceptibility gene 101 (Tsg101). The notion that structures found in p9 differ form that of p6 further support the idea that different mechanisms regulate binding of ALIX to primary versus secondary L-domains types.
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Helmholtz Zentrum für Infektionsforschung Repository
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