Surin BP - Search Results

1

The symmetry of Escherichia coli cpn60 (GroEL) determined by X-ray crystallography.

Svensson LA, Surin BP, Dixon NE, Spangfort MD. Svensson LA, et al. Among authors: surin bp. J Mol Biol. 1994 Jan 7;235(1):47-52. doi: 10.1016/s0022-2836(05)80011-7. J Mol Biol. 1994. PMID: 7904652

2

Crystallization and preliminary X-ray investigation of the Escherichia coli molecular chaperone cpn60 (GroEL).

Spangfort MD, Surin BP, Oppentocht JE, Weibull C, Carlemalm E, Dixon NE, Svensson LA. Spangfort MD, et al. Among authors: surin bp. FEBS Lett. 1993 Apr 5;320(2):160-4. doi: 10.1016/0014-5793(93)80083-7. FEBS Lett. 1993. PMID: 8096194 Free article.

3

Internal symmetry of the molecular chaperone cpn60 (GroEL) determined by X-ray crystallography.

Spangfort MD, Surin BP, Dixon NE, Svensson LA. Spangfort MD, et al. Among authors: surin bp. Acta Crystallogr D Biol Crystallogr. 1994 Jul 1;50(Pt 4):591-5. doi: 10.1107/S0907444993014349. Acta Crystallogr D Biol Crystallogr. 1994. PMID: 15299422

4

Isolation and biochemical characterization of highly purified Escherichia coli molecular chaperone Cpn60 (GroEL) by affinity chromatography and urea-induced monomerization.

Blennow A, Surin BP, Ehring H, McLennan NF, Spangfort MD. Blennow A, et al. Among authors: surin bp. Biochim Biophys Acta. 1995 Sep 27;1252(1):69-78. doi: 10.1016/0167-4838(95)00111-7. Biochim Biophys Acta. 1995. PMID: 7548168

5

GroEL/ES-mediated refolding of human carbonic anhydrase II: role of N-terminal helices as recognition motifs for GroEL.

Persson M, Aronsson G, Bergenhem N, Freskgård PO, Jonsson BH, Surin BP, Spangfort MD, Carlsson U. Persson M, et al. Among authors: surin bp. Biochim Biophys Acta. 1995 Mar 15;1247(2):195-200. doi: 10.1016/0167-4838(94)00227-8. Biochim Biophys Acta. 1995. PMID: 7696308

6

Substoichiometric amounts of the molecular chaperones GroEL and GroES prevent thermal denaturation and aggregation of mammalian mitochondrial malate dehydrogenase in vitro.

Hartman DJ, Surin BP, Dixon NE, Hoogenraad NJ, Høj PB. Hartman DJ, et al. Among authors: surin bp. Proc Natl Acad Sci U S A. 1993 Mar 15;90(6):2276-80. doi: 10.1073/pnas.90.6.2276. Proc Natl Acad Sci U S A. 1993. PMID: 8096339 Free PMC article.

7

Purification of the phoU protein, a negative regulator of the pho regulon of Escherichia coli K-12.

Surin BP, Dixon NE, Rosenberg H. Surin BP, et al. J Bacteriol. 1986 Nov;168(2):631-5. doi: 10.1128/jb.168.2.631-635.1986. J Bacteriol. 1986. PMID: 3536855 Free PMC article.

8

Phosphate-specific transport system of Escherichia coli: nucleotide sequence and gene-polypeptide relationships.

Surin BP, Rosenberg H, Cox GB. Surin BP, et al. J Bacteriol. 1985 Jan;161(1):189-98. doi: 10.1128/jb.161.1.189-198.1985. J Bacteriol. 1985. PMID: 3881386 Free PMC article.

9

Structural gene for the phosphate-repressible phosphate-binding protein of Escherichia coli has its own promoter: complete nucleotide sequence of the phoS gene.

Surin BP, Jans DA, Fimmel AL, Shaw DC, Cox GB, Rosenberg H. Surin BP, et al. J Bacteriol. 1984 Mar;157(3):772-8. doi: 10.1128/jb.157.3.772-778.1984. J Bacteriol. 1984. PMID: 6321434 Free PMC article.

10

Translational coupling varying in efficiency between different pairs of genes in the central region of the atp operon of Escherichia coli.

Hellmuth K, Rex G, Surin B, Zinck R, McCarthy JE. Hellmuth K, et al. Mol Microbiol. 1991 Apr;5(4):813-24. doi: 10.1111/j.1365-2958.1991.tb00754.x. Mol Microbiol. 1991. PMID: 1830358

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