Search results
From Proteopedia
You searched for Dsbd
There is no page with the exact title "Dsbd". The search results for "Dsbd" are displayed below. You can create a page titled Dsbd (by clicking on the red link).
For more information about searching Proteopedia, see Help.
Showing below up to 20 results starting with #1.
View (previous 20) (next 20) (20 | 50 | 100 | 250 | 500)
Article title matches
- Category:Dsbd (35 bytes)
1: List of pages with the keyword Dsbd - Category:Dsbd homolog (43 bytes)
1: List of pages with the keyword Dsbd homolog
Page text matches
- 2iy2 (4,596 bytes)
11: ...an DsbC. DsbG is maintained in a reduced state by DsbD. Displays chaperone activity in both redox states... - 1eej (4,361 bytes)
11: ... is reduced in the process. DsbC is reoxidized by DsbD.<ref>PMID:19965429</ref> - 1g0t (4,104 bytes)
11: ... is reduced in the process. DsbC is reoxidized by DsbD.<ref>PMID:19965429</ref> - 1jpe (4,292 bytes)
2: ...structure of DsbD-alpha; the N-terminal domain of DsbD==
10: [https://www.uniprot.org/uniprot/DSBD_ECOLI DSBD_ECOLI] Required to facilitate the formation of co...
23: ...ults explain how DsbC is selectively activated by DsbD using electrons derived from the cytoplasm.
25: ...iol oxidoreductase: crystal structure of the DsbC-DsbDalpha complex.,Haebel PW, Goldstone D, Katzen F, B... - 1jzd (4,334 bytes)
2: ==DsbC-DsbDalpha complex==
10: ... is reduced in the process. DsbC is reoxidized by DsbD.<ref>PMID:19965429</ref>
23: ...ults explain how DsbC is selectively activated by DsbD using electrons derived from the cytoplasm.
25: ...iol oxidoreductase: crystal structure of the DsbC-DsbDalpha complex.,Haebel PW, Goldstone D, Katzen F, B... - 1jzo (4,323 bytes)
10: ... is reduced in the process. DsbC is reoxidized by DsbD.<ref>PMID:19965429</ref>
23: ...ults explain how DsbC is selectively activated by DsbD using electrons derived from the cytoplasm.
25: ...iol oxidoreductase: crystal structure of the DsbC-DsbDalpha complex.,Haebel PW, Goldstone D, Katzen F, B... - 1l6p (4,606 bytes)
2: ==N-terminal of DsbD (residues 20-144) from E. coli.==
10: [https://www.uniprot.org/uniprot/DSBD_ECOLI DSBD_ECOLI] Required to facilitate the formation of co...
23: ...l is discussed whereby the immunoglobulin fold of DsbD(N) may provide for the discriminating interaction...
25: ...-like fold: structure of the N-terminal domain of DsbD.,Goulding CW, Sawaya MR, Parseghian A, Lim V, Eis... - 1tjd (4,467 bytes)
10: ... is reduced in the process. DsbC is reoxidized by DsbD.<ref>PMID:19965429</ref> - 1uc7 (4,177 bytes)
2: ==Crystal structure of DsbDgamma==
10: [https://www.uniprot.org/uniprot/DSBD_ECO57 DSBD_ECO57] Required to facilitate the formation of co...
23: ...a may be important in the specific recognition of DsbDalpha.
25: Crystal structure of DsbDgamma reveals the mechanism of redox potential shi... - 1v57 (3,055 bytes)
11: ...an DsbC. DsbG is maintained in a reduced state by DsbD. Displays chaperone activity in both redox states... - 1v58 (4,988 bytes)
11: ...an DsbC. DsbG is maintained in a reduced state by DsbD. Displays chaperone activity in both redox states... - 1vrs (4,850 bytes)
2: ...terminal domain of the electron transfer catalyst DsbD==
10: [https://www.uniprot.org/uniprot/DSBD_ECOLI DSBD_ECOLI] Required to facilitate the formation of co...
23: ...rface areas of nDsbD that interact with DsbC and cDsbD. In addition, we have measured the kinetics of al...
25: ...olecular disulfide exchange in the redox catalyst DsbD.,Rozhkova A, Stirnimann CU, Frei P, Grauschopf U,... - 1z5y (4,657 bytes)
2: ...Terminal Domain Of The Electron Transfer Catalyst DsbD and The Cytochrome c Biogenesis Protein CcmG==
11: [https://www.uniprot.org/uniprot/DSBD_ECOLI DSBD_ECOLI] Required to facilitate the formation of co...
24: ...ute the structural basis for the adaptability of nDsbD to different protein substrates.
26: Structural basis and kinetics of DsbD-dependent cytochrome c maturation.,Stirnimann CU,... - 2b1k (4,827 bytes)
10: ...e lyase. DsbE is maintained in a reduced state by DsbD.
23: ...141 undergoes conformational changes upon binding DsbD. A cis-proline located at the N-terminus of the f... - 2b1l (4,885 bytes)
10: ...e lyase. DsbE is maintained in a reduced state by DsbD.
23: ...141 undergoes conformational changes upon binding DsbD. A cis-proline located at the N-terminus of the f... - 2fwe (5,913 bytes)
2: ...terminal domain of the electron transfer catalyst DsbD (oxidized form)==
11: [https://www.uniprot.org/uniprot/DSBD_ECOLI DSBD_ECOLI] Required to facilitate the formation of co...
24: ...e domain and the N-terminal periplasmic domain of DsbD.
26: High-resolution structures of Escherichia coli cDsbD in different redox states: A combined crystallogr... - 2fwf (5,872 bytes)
2: ...terminal domain of the electron transfer catalyst DsbD (reduced form)==
11: [https://www.uniprot.org/uniprot/DSBD_ECOLI DSBD_ECOLI] Required to facilitate the formation of co...
24: ...e domain and the N-terminal periplasmic domain of DsbD.
26: High-resolution structures of Escherichia coli cDsbD in different redox states: A combined crystallogr... - 2fwg (5,660 bytes)
2: ...terminal domain of the electron transfer catalyst DsbD (photoreduced form)==
10: [https://www.uniprot.org/uniprot/DSBD_ECOLI DSBD_ECOLI] Required to facilitate the formation of co...
23: ...e domain and the N-terminal periplasmic domain of DsbD.
25: High-resolution structures of Escherichia coli cDsbD in different redox states: A combined crystallogr... - 2fwh (5,895 bytes)
2: ...terminal domain of the electron transfer catalyst DsbD (reduced form at pH7)==
11: [https://www.uniprot.org/uniprot/DSBD_ECOLI DSBD_ECOLI] Required to facilitate the formation of co...
24: ...e domain and the N-terminal periplasmic domain of DsbD.
26: High-resolution structures of Escherichia coli cDsbD in different redox states: A combined crystallogr... - 2g0f (4,842 bytes)
10: ...e lyase. DsbE is maintained in a reduced state by DsbD.
23: ...141 undergoes conformational changes upon binding DsbD. A cis-proline located at the N-terminus of the f...
View (previous 20) (next 20) (20 | 50 | 100 | 250 | 500)
