Teschke CM - Search Results

1

A second-site suppressor of a folding defect functions via interactions with a chaperone network to improve folding and assembly in vivo.

Parent KN, Ranaghan MJ, Teschke CM. Parent KN, et al. Among authors: teschke cm. Mol Microbiol. 2004 Nov;54(4):1036-50. doi: 10.1111/j.1365-2958.2004.04326.x. Mol Microbiol. 2004. PMID: 15522085 Free article.

2

Templated trimerization of the phage L decoration protein on capsids.

Woodbury BM, Newcomer RL, Alexandrescu AT, Teschke CM. Woodbury BM, et al. Among authors: teschke cm. bioRxiv [Preprint]. 2024 Sep 8:2024.09.08.611893. doi: 10.1101/2024.09.08.611893. bioRxiv. 2024. PMID: 39282432 Free PMC article. Preprint.

3

Interactions between coat and scaffolding proteins of phage P22 are altered in vitro by amino acid substitutions in coat protein that cause a cold-sensitive phenotype.

Teschke CM, Fong DG. Teschke CM, et al. Biochemistry. 1996 Nov 26;35(47):14831-40. doi: 10.1021/bi960860l. Biochemistry. 1996. PMID: 8942646

4

The folded conformation of phage P22 coat protein is affected by amino acid substitutions that lead to a cold-sensitive phenotype.

Fong DG, Doyle SM, Teschke CM. Fong DG, et al. Among authors: teschke cm. Biochemistry. 1997 Apr 1;36(13):3971-80. doi: 10.1021/bi962188y. Biochemistry. 1997. PMID: 9092827

5

GroEL and GroES control of substrate flux in the in vivo folding pathway of phage P22 coat protein.

Nakonechny WS, Teschke CM. Nakonechny WS, et al. Among authors: teschke cm. J Biol Chem. 1998 Oct 16;273(42):27236-44. doi: 10.1074/jbc.273.42.27236. J Biol Chem. 1998. PMID: 9765246 Free article.

6

Aggregation and assembly of phage P22 temperature-sensitive coat protein mutants in vitro mimic the in vivo phenotype.

Teschke CM. Teschke CM. Biochemistry. 1999 Mar 9;38(10):2873-81. doi: 10.1021/bi982739f. Biochemistry. 1999. PMID: 10074339

7

Single amino acid substitutions globally suppress the folding defects of temperature-sensitive folding mutants of phage P22 coat protein.

Aramli LA, Teschke CM. Aramli LA, et al. Among authors: teschke cm. J Biol Chem. 1999 Aug 6;274(32):22217-24. doi: 10.1074/jbc.274.32.22217. J Biol Chem. 1999. PMID: 10428787 Free article.

8

Folding defects caused by single amino acid substitutions in a subunit are not alleviated by assembly.

Capen CM, Teschke CM. Capen CM, et al. Among authors: teschke cm. Biochemistry. 2000 Feb 8;39(5):1142-51. doi: 10.1021/bi991956t. Biochemistry. 2000. PMID: 10653661

9

GroEL binds a late folding intermediate of phage P22 coat protein.

de Beus MD, Doyle SM, Teschke CM. de Beus MD, et al. Among authors: teschke cm. Cell Stress Chaperones. 2000 Jul;5(3):163-72. doi: 10.1379/1466-1268(2000)005<0163:gbalfi>2.0.co;2. Cell Stress Chaperones. 2000. PMID: 11005374 Free PMC article.

10

Alleviation of a defect in protein folding by increasing the rate of subunit assembly.

Aramli LA, Teschke CM. Aramli LA, et al. Among authors: teschke cm. J Biol Chem. 2001 Jul 6;276(27):25372-7. doi: 10.1074/jbc.M101759200. Epub 2001 Apr 13. J Biol Chem. 2001. PMID: 11304542 Free article.

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