Journal Issue - Volume 11 Issue 5 (May 2002)
Timing and structural consideration for the processing of mitochondrial matrix space proteins by the mitochondrial processing peptidase (MPP)
- Abhijit Mukhopadhyay, Philip Hammen, Mary Waltner‐Law, Henry Weiner
- Published in Wiley Interscience on Jan 01, 2009
- DOI: 10.1110/ps.3760102 (p 1026-1035)
Abstract Most mitochondrial matrix space proteins are synthesized as a precursor protein, and the N‐terminal extension of amino acids that served as the leader sequence is removed after import by the action of a metalloprotease called mitochondrial processing peptidase (MPP). The crystal structure of MPP has been solved very recently, and it has been shown that synthetic leader peptides bind with MPP in an extended conformation....
Exploring protein aggregation and self‐propagation using lattice models: Phase diagram and kinetics
- R.I. Dima, D. Thirumalai
- Published in Wiley Interscience on Jan 01, 2009
- DOI: 10.1110/ps.4220102 (p 1036-1049)
Abstract Many seemingly unrelated neurodegenerative disorders, such as amyloid and prion diseases, are associated with propagating fibrils whose structures are dramatically different from the native states of the corresponding monomers. This observation, along with the experimental demonstration that any protein can aggregate to form either fibrils or amorphous structures (inclusion bodies) under appropriate external conditions,...
Assessment of the ability to model proteins with leucine‐rich repeats in light of the latest structural information
- Andrey V. Kajava, Bostjan Kobe
- Published in Wiley Interscience on Jan 01, 2009
- DOI: 10.1110/ps.4010102 (p 1082-1090)
Abstract The three‐dimensional structures of leucine‐rich repeat (LRR)‐containing proteins from five different families were previously predicted based on the crystal structure of the ribonuclease inhibitor, using an approach that combined homology‐based modeling, structure‐based sequence alignment of LRRs, and several rational assumptions. The structural models have been produced based on very limited sequence similarity, which, in...
Stability and interactions of the amino‐terminal domain of ClpB from Escherichia coli
- Vekalet Tek, Michal Zolkiewski
- Published in Wiley Interscience on Jan 01, 2009
- DOI: 10.1110/ps.4860102 (p 1192-1198)
Abstract ClpB is a member of a multichaperone system in Escherichia coli (with DnaK, DnaJ, and GrpE) that reactivates aggregated proteins. The sequence of ClpB contains two ATP‐binding regions that are enclosed between the N‐ and C‐terminal extensions. Whereas it has been found that the N‐terminal region of ClpB is essential for the chaperone activity, the structure of this region is not known, and its biochemical properties have not been...
Development of a cytokine analog with enhanced stability using computational ultrahigh throughput screening
- Peizhi Luo, Robert J. Hayes, Cheryl Chan, Diane M. Stark, Marian Y. Hwang, Jonathan M. Jacinto, Padmaja Juvvadi, Helen S. Chung, Anirban Kundu, Marie L. Ary, Bassil I. Dahiyat
- Published in Wiley Interscience on Jan 01, 2009
- DOI: 10.1110/ps.4580102 (p 1218-1226)
Abstract Granulocyte‐colony stimulating factor (G‐CSF) is used worldwide to prevent neutropenia caused by high‐dose chemotherapy. It has limited stability, strict formulation and storage requirements, and because of poor oral absorption must be administered by injection (typically daily). Thus, there is significant interest in developing analogs with improved pharmacological properties. We used our ultrahigh throughput computational...
A model of the replication fork blocking protein Fob1p based on the catalytic core domain of retroviral integrases
- Mensur Dlakić
- Published in Wiley Interscience on Jan 01, 2009
- DOI: 10.1110/ps.4470102 (p 1274-1277)
Abstract The replication fork blocks are common in both prokaryotes and eukaryotes. In most cases, these blocks are associated with increased levels of mitotic recombination. One of the best‐characterized replication fork blocks in eukaryotes is found in ribosomal DNA (rDNA) repeats of Saccharomyces cerevisiae. It has been shown that the replication fork blocking protein Fob1p regulates the recombination rate and the number of rDNA ...




