Holger Patzelt
Overview
Explore the profile of Holger Patzelt including associated specialties, affiliations and a list of published articles.
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7
Citations
531
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Recent Articles
1.
Ferbitz L, Maier T, Patzelt H, Bukau B, Deuerling E, Ban N
Nature
. 2004 Aug;
431(7008):590-6.
PMID: 15334087
During protein biosynthesis, nascent polypeptide chains that emerge from the ribosomal exit tunnel encounter ribosome-associated chaperones, which assist their folding to the native state. Here we present a 2.7 A...
2.
Schlieker C, Weibezahn J, Patzelt H, Tessarz P, Strub C, Zeth K, et al.
Nat Struct Mol Biol
. 2004 Jun;
11(7):607-15.
PMID: 15208691
The AAA+ protein ClpB cooperates with the DnaK chaperone system to solubilize and refold proteins from an aggregated state. The substrate-binding site of ClpB and the mechanism of ClpB-dependent protein...
3.
Kramer G, Patzelt H, Rauch T, Kurz T, Vorderwulbecke S, Bukau B, et al.
J Biol Chem
. 2004 Jan;
279(14):14165-70.
PMID: 14729669
The ribosome-associated Trigger Factor (TF) cooperates with the DnaK system to assist the folding of newly synthesized polypeptides in Escherichia coli. TF unifies two functions in one to promote proper...
4.
Deuerling E, Patzelt H, Vorderwulbecke S, Rauch T, Kramer G, Schaffitzel E, et al.
Mol Microbiol
. 2003 Feb;
47(5):1317-28.
PMID: 12603737
Ribosome-associated Trigger Factor (TF) and the DnaK chaperone system assist the folding of newly synthesized proteins in Escherichia coli. Here, we show that DnaK and TF share a common substrate...
5.
Patzelt H, Kramer G, Rauch T, Schonfeld H, Bukau B, Deuerling E
Biol Chem
. 2002 Nov;
383(10):1611-9.
PMID: 12452438
Trigger Factor (TF) is the first chaperone that interacts with nascent chains of cytosolic proteins in Escherichia coli. Although its chaperone activity requires association with ribosomes, TF is present in...
6.
Kramer G, Rauch T, Rist W, Vorderwulbecke S, Patzelt H, Schulze-Specking A, et al.
Nature
. 2002 Sep;
419(6903):171-4.
PMID: 12226666
During translation, the first encounter of nascent polypeptides is with the ribosome-associated chaperones that assist the folding process--a principle that seems to be conserved in evolution. In Escherichia coli, the...
7.
Kluck C, Patzelt H, Genevaux P, Brehmer D, Rist W, Schneider-Mergener J, et al.
J Biol Chem
. 2002 Aug;
277(43):41060-9.
PMID: 12183460
Hsp70 chaperones assist protein folding processes through nucleotide-controlled cycles of substrate binding and release. In our effort to understand the structure-function relationship within the Hsp70 family of proteins, we characterized...