Format
Items per page
Sort by

Send to:

Choose Destination

Results: 1 to 20 of 124

Similar articles for PubMed (Select 12381839)

1.

Structural and nucleotide-binding properties of YajQ and YnaF, two Escherichia coli proteins of unknown function.

Saveanu C, Miron S, Borza T, Craescu CT, Labesse G, Gagyi C, Popescu A, Schaeffer F, Namane A, Laurent-Winter C, Bârzu O, Gilles AM.

Protein Sci. 2002 Nov;11(11):2551-60.

2.

Structure of the universal stress protein of Haemophilus influenzae.

Sousa MC, McKay DB.

Structure. 2001 Dec;9(12):1135-41.

3.

The solution structure of YbcJ from Escherichia coli reveals a recently discovered alphaL motif involved in RNA binding.

Volpon L, Lievre C, Osborne MJ, Gandhi S, Iannuzzi P, Larocque R, Cygler M, Gehring K, Ekiel I.

J Bacteriol. 2003 Jul;185(14):4204-10.

4.

Crystal structure of the YajQ protein from Haemophilus influenzae reveals a tandem of RNP-like domains.

Teplyakov A, Obmolova G, Bir N, Reddy P, Howard AJ, Gilliland GL.

J Struct Funct Genomics. 2003;4(1):1-9.

PMID:
12943362
5.

Solution structure and NH exchange studies of the MutT pyrophosphohydrolase complexed with Mg(2+) and 8-oxo-dGMP, a tightly bound product.

Massiah MA, Saraswat V, Azurmendi HF, Mildvan AS.

Biochemistry. 2003 Sep 2;42(34):10140-54.

PMID:
12939141
6.

Solution structure of the carbon storage regulator protein CsrA from Escherichia coli.

Gutiérrez P, Li Y, Osborne MJ, Pomerantseva E, Liu Q, Gehring K.

J Bacteriol. 2005 May;187(10):3496-501.

7.

Periplasmic loop P2 of the MalF subunit of the maltose ATP binding cassette transporter is sufficient to bind the maltose binding protein MalE.

Jacso T, Grote M, Daus ML, Schmieder P, Keller S, Schneider E, Reif B.

Biochemistry. 2009 Mar 17;48(10):2216-25. doi: 10.1021/bi801376m.

PMID:
19159328
8.

Solution structure of the ribosome-associated cold shock response protein Yfia of Escherichia coli.

Rak A, Kalinin A, Shcherbakov D, Bayer P.

Biochem Biophys Res Commun. 2002 Dec 20;299(5):710-4.

PMID:
12470636
9.

ATP binding properties of the soluble part of the KdpC subunit from the Escherichia coli K(+)-transporting KdpFABC P-type ATPase.

Ahnert F, Schmid R, Altendorf K, Greie JC.

Biochemistry. 2006 Sep 12;45(36):11038-46.

PMID:
16953591
10.

Structure of dimeric SecA, the Escherichia coli preprotein translocase motor.

Papanikolau Y, Papadovasilaki M, Ravelli RB, McCarthy AA, Cusack S, Economou A, Petratos K.

J Mol Biol. 2007 Mar 9;366(5):1545-57. Epub 2006 Dec 23.

PMID:
17229438
11.
12.

Structure-based assignment of the biochemical function of a hypothetical protein: a test case of structural genomics.

Zarembinski TI, Hung LW, Mueller-Dieckmann HJ, Kim KK, Yokota H, Kim R, Kim SH.

Proc Natl Acad Sci U S A. 1998 Dec 22;95(26):15189-93.

13.

Ribosome-associated factor Y adopts a fold resembling a double-stranded RNA binding domain scaffold.

Ye K, Serganov A, Hu W, Garber M, Patel DJ.

Eur J Biochem. 2002 Nov;269(21):5182-91.

14.

Solution structure of the Escherichia coli protein ydhR: a putative mono-oxygenase.

Revington M, Semesi A, Yee A, Shaw GS.

Protein Sci. 2005 Dec;14(12):3115-20. Epub 2005 Oct 31.

15.

RNA sequence and secondary structure participate in high-affinity CsrA-RNA interaction.

Dubey AK, Baker CS, Romeo T, Babitzke P.

RNA. 2005 Oct;11(10):1579-87. Epub 2005 Aug 30.

16.

Characterization of the low pH solution structure and dynamics of the region 4 of Escherichia coli RNA polymerase sigma70 subunit.

Poznański J, Bolewska K, Zhukov I, Wierzchowski KL.

Biochemistry. 2003 Nov 25;42(46):13438-48.

PMID:
14621989
17.

Solution NMR structure of ribosome-binding factor A (RbfA), a cold-shock adaptation protein from Escherichia coli.

Huang YJ, Swapna GV, Rajan PK, Ke H, Xia B, Shukla K, Inouye M, Montelione GT.

J Mol Biol. 2003 Mar 21;327(2):521-36.

PMID:
12628255
18.
19.
20.

Functional modules of KdpB, the catalytic subunit of the Kdp-ATPase from Escherichia coli.

Bramkamp M, Altendorf K.

Biochemistry. 2004 Sep 28;43(38):12289-96.

PMID:
15379567
Format
Items per page
Sort by

Send to:

Choose Destination

Supplemental Content

Write to the Help Desk