The DOI matches its Crossref record; 47 of the 47 references it cites were found in a registry or an index.
Mitochondrial protein import: Identification of processing peptidase and of PEP, a processing enhancing protein
Open accessAbstract
Transport of nuclear-encoded precursor proteins into mitochondria includes proteolytic cleavage of amino-terminal targeting sequences in the mitochondrial matrix. We have isolated the processing activity from Neurospora crassa. The final preparation (enriched ca. 10,000-fold over cell extracts) consists of two proteins, the matrix processing peptidase (MPP, 57 kd) and a processing enhancing protein (PEP, 52 kd). The two components were isolated as monomers. PEP is about 15-fold more abundant in mitochondria than MPP. It is partly associated with the inner membrane, while MPP is soluble in the matrix. MPP alone has a low processing activity whereas PEP alone has no apparent activity. Upon recombining both, full processing activity is restored. Our data indicate that MPP contains the catalytic site and that PEP has an enhancing function. The mitochondrial processing enzyme appears to represent a new type of "signal peptidase," different from the bacterial leader peptidase and the signal peptidase of the endoplasmic reticulum.
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Self-citationEmerging mechanisms for heavy metal transport in plants
Williams, L. E., Pittman, J. K., & Hall, J. L. (2000) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/s0005-2736(00)00133-4 · Cited by 629
Metadata
- Authors
- Hawlitschek, G., Schneider, H., Schmidt, B., Tropschug, M., Hartl, F.-U., & Neupert, W.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 1988-06
- Volume
- 53
- Issue
- 5
- Pages
- 795-806
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2067310224
- Cited by
- 395
- References
- 47
- FWCI
- 14.36
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Hawlitschek, G., Schneider, H., Schmidt, B., Tropschug, M., Hartl, F.-U., & Neupert, W. (1988). Mitochondrial protein import: Identification of processing peptidase and of PEP, a processing enhancing protein. Cell. https://doi.org/10.1016/0092-8674(88)90096-7
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.