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Items: 13

1.

Novel Role for PilNO in Type IV Pilus Retraction Revealed by Alignment Subcomplex Mutations.

Leighton TL, Dayalani N, Sampaleanu LM, Howell PL, Burrows LL.

J Bacteriol. 2015 Jul;197(13):2229-2238. doi: 10.1128/JB.00220-15. Epub 2015 Apr 27.

2.

PilMNOPQ from the Pseudomonas aeruginosa type IV pilus system form a transenvelope protein interaction network that interacts with PilA.

Tammam S, Sampaleanu LM, Koo J, Manoharan K, Daubaras M, Burrows LL, Howell PL.

J Bacteriol. 2013 May;195(10):2126-35. doi: 10.1128/JB.00032-13. Epub 2013 Mar 1.

3.

Characterization of the PilN, PilO and PilP type IVa pilus subcomplex.

Tammam S, Sampaleanu LM, Koo J, Sundaram P, Ayers M, Chong PA, Forman-Kay JD, Burrows LL, Howell PL.

Mol Microbiol. 2011 Dec;82(6):1496-514. doi: 10.1111/j.1365-2958.2011.07903.x. Epub 2011 Nov 18.

4.

Periplasmic domains of Pseudomonas aeruginosa PilN and PilO form a stable heterodimeric complex.

Sampaleanu LM, Bonanno JB, Ayers M, Koo J, Tammam S, Burley SK, Almo SC, Burrows LL, Howell PL.

J Mol Biol. 2009 Nov 20;394(1):143-59. doi: 10.1016/j.jmb.2009.09.037.

PMID:
19857646
5.

PilM/N/O/P proteins form an inner membrane complex that affects the stability of the Pseudomonas aeruginosa type IV pilus secretin.

Ayers M, Sampaleanu LM, Tammam S, Koo J, Harvey H, Howell PL, Burrows LL.

J Mol Biol. 2009 Nov 20;394(1):128-42. doi: 10.1016/j.jmb.2009.09.034.

PMID:
19857645
6.

PilF is an outer membrane lipoprotein required for multimerization and localization of the Pseudomonas aeruginosa Type IV pilus secretin.

Koo J, Tammam S, Ku SY, Sampaleanu LM, Burrows LL, Howell PL.

J Bacteriol. 2008 Nov;190(21):6961-9. doi: 10.1128/JB.00996-08. Epub 2008 Sep 5.

7.

Functional role of conserved residues in the characteristic secretion NTPase motifs of the Pseudomonas aeruginosa type IV pilus motor proteins PilB, PilT and PilU.

Chiang P, Sampaleanu LM, Ayers M, Pahuta M, Howell PL, Burrows LL.

Microbiology. 2008 Jan;154(Pt 1):114-26. doi: 10.1099/mic.0.2007/011320-0.

PMID:
18174131
8.

A duck delta1 crystallin double loop mutant provides insight into residues important for argininosuccinate lyase activity.

Tsai M, Sampaleanu LM, Greene C, Creagh L, Haynes C, Howell PL.

Biochemistry. 2004 Sep 21;43(37):11672-82.

PMID:
15362851
9.

Structural studies of duck delta2 crystallin mutants provide insight into the role of Thr161 and the 280s loop in catalysis.

Sampaleanu LM, Codding PW, Lobsanov YD, Tsai M, Smith GD, Horvatin C, Howell PL.

Biochem J. 2004 Dec 1;384(Pt 2):437-47.

10.

Three-dimensional structure of the argininosuccinate lyase frequently complementing allele Q286R.

Sampaleanu LM, Vallée F, Thompson GD, Howell PL.

Biochemistry. 2001 Dec 25;40(51):15570-80.

PMID:
11747432
12.

Structural studies of duck delta 1 and delta 2 crystallin suggest conformational changes occur during catalysis.

Sampaleanu LM, Vallée F, Slingsby C, Howell PL.

Biochemistry. 2001 Mar 6;40(9):2732-42.

PMID:
11258884
13.

Domain exchange experiments in duck delta-crystallins: functional and evolutionary implications.

Sampaleanu LM, Davidson AR, Graham C, Wistow GJ, Howell PL.

Protein Sci. 1999 Mar;8(3):529-37.

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