Huber DR - Search Results

1

Genetic selection for and molecular dynamic modeling of a protein transmembrane domain multimerization motif from a random Escherichia coli genomic library.

Leeds JA, Boyd D, Huber DR, Sonoda GK, Luu HT, Engelman DM, Beckwith J. Leeds JA, et al. Among authors: huber dr. J Mol Biol. 2001 Oct 12;313(1):181-95. doi: 10.1006/jmbi.2001.5007. J Mol Biol. 2001. PMID: 11601855

2

The DsbA signal sequence directs efficient, cotranslational export of passenger proteins to the Escherichia coli periplasm via the signal recognition particle pathway.

Schierle CF, Berkmen M, Huber D, Kumamoto C, Boyd D, Beckwith J. Schierle CF, et al. J Bacteriol. 2003 Oct;185(19):5706-13. doi: 10.1128/JB.185.19.5706-5713.2003. J Bacteriol. 2003. PMID: 13129941 Free PMC article.

3

Use of thioredoxin as a reporter to identify a subset of Escherichia coli signal sequences that promote signal recognition particle-dependent translocation.

Huber D, Boyd D, Xia Y, Olma MH, Gerstein M, Beckwith J. Huber D, et al. J Bacteriol. 2005 May;187(9):2983-91. doi: 10.1128/JB.187.9.2983-2991.2005. J Bacteriol. 2005. PMID: 15838024 Free PMC article.

4

A selection for mutants that interfere with folding of Escherichia coli thioredoxin-1 in vivo.

Huber D, Cha MI, Debarbieux L, Planson AG, Cruz N, López G, Tasayco ML, Chaffotte A, Beckwith J. Huber D, et al. Proc Natl Acad Sci U S A. 2005 Dec 27;102(52):18872-7. doi: 10.1073/pnas.0509583102. Epub 2005 Dec 15. Proc Natl Acad Sci U S A. 2005. PMID: 16357193 Free PMC article.

5

Amino acid residues important for folding of thioredoxin are revealed only by study of the physiologically relevant reduced form of the protein.

Huber D, Chaffotte A, Eser M, Planson AG, Beckwith J. Huber D, et al. Biochemistry. 2010 Oct 19;49(41):8922-8. doi: 10.1021/bi100784h. Biochemistry. 2010. PMID: 20873718 Free PMC article.

6

Phage display extends its reach.

Huber D, Beckwith J. Huber D, et al. Nat Biotechnol. 2006 Jul;24(7):793-4. doi: 10.1038/nbt0706-793. Nat Biotechnol. 2006. PMID: 16841063 No abstract available.

7

SecA interacts with ribosomes in order to facilitate posttranslational translocation in bacteria.

Huber D, Rajagopalan N, Preissler S, Rocco MA, Merz F, Kramer G, Bukau B. Huber D, et al. Mol Cell. 2011 Feb 4;41(3):343-53. doi: 10.1016/j.molcel.2010.12.028. Mol Cell. 2011. PMID: 21292166 Free article.

8

SecA Cotranslationally Interacts with Nascent Substrate Proteins In Vivo.

Huber D, Jamshad M, Hanmer R, Schibich D, Döring K, Marcomini I, Kramer G, Bukau B. Huber D, et al. J Bacteriol. 2016 Dec 28;199(2):e00622-16. doi: 10.1128/JB.00622-16. Print 2017 Jan 15. J Bacteriol. 2016. PMID: 27795329 Free PMC article.

9

Selective ribosome profiling reveals the cotranslational chaperone action of trigger factor in vivo.

Oh E, Becker AH, Sandikci A, Huber D, Chaba R, Gloge F, Nichols RJ, Typas A, Gross CA, Kramer G, Weissman JS, Bukau B. Oh E, et al. Cell. 2011 Dec 9;147(6):1295-308. doi: 10.1016/j.cell.2011.10.044. Cell. 2011. PMID: 22153074 Free PMC article.

10

Integrating protein homeostasis strategies in prokaryotes.

Mogk A, Huber D, Bukau B. Mogk A, et al. Cold Spring Harb Perspect Biol. 2011 Apr 1;3(4):a004366. doi: 10.1101/cshperspect.a004366. Cold Spring Harb Perspect Biol. 2011. PMID: 21441580 Free PMC article. Review.

Save citations to file

Email citations

Send citations to clipboard

Add to Collections

Add to My Bibliography

Create a file for external citation management software

Your saved search

Your RSS Feed

My NCBI Filters

Text availability

Article attribute

Article type

Publication date

42 results

Search Page