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Cited by 287

The DOI matches its Crossref record; 26 of the 26 references it cites were found in a registry or an index.

Regulation by Heme of Mitochondrial Protein Transport Through a Conserved Amino Acid Motif

Lathrop, Julia Tait, Timko, Michael P.·1993·Science
DOI 10.1126/science.8424176
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Abstract

A conserved motif, termed the heme regulatory motif (HRM), was identified in the presequences of the erythroid δ-aminolevulinate synthase precursors and was shown to be involved in hemin inhibition of transport of these proteins into mouse mitochondria in vitro. When the HRM was inserted into the presequence of the ornithine transcarbamoylase precursor, a normally unregulated mitochondrial protein, it conferred hemin inhibition on the transport of the chimeric protein. The conserved cysteine within the HRM was shown by site-directed mutagenesis to be required for hemin inhibition.

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Cites

Show all 26 references

Research works printed but not linked: 12

  1. CHEN, J.J., DISULFIDE BOND FORMATION IN THE REGULATION OF EIF-2-ALPHA-KINASE BY HEME, JOURNAL OF BIOLOGICAL CHEMISTRY 264: 9559 (1989). · doi:10.1016/s0021-9258(18)60568-x
  2. CHEN, W.J., THE ROLE OF PROTEIN-STRUCTURE IN THE MITOCHONDRIAL IMPORT PATHWAY - UNFOLDING OF MITOCHONDRIALLY BOUND PRECURSORS IS REQUIRED FOR MEMBRANE TRANSLOCATION, JOURNAL OF BIOLOGICAL CHEMISTRY 262: 15605 (1987). · doi:10.1016/s0021-9258(18)47769-1
  3. CONBOY, J.G., POSTTRANSLATIONAL UPTAKE AND PROCESSING OF INVITRO SYNTHESIZED ORNITHINE TRANSCARBAMOYLASE PRECURSOR BY ISOLATED RAT-LIVER MITOCHONDRIA, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA-BIOLOGICAL SCIENCES 78: 3073 (1981).
  4. EILERS, M, UNFOLDING AND REFOLDING OF A PURIFIED PRECURSOR PROTEIN DURING IMPORT INTO ISOLATED-MITOCHONDRIA, EMBO JOURNAL 7: 1139 (1988). · doi:10.1002/j.1460-2075.1988.tb02923.x
  5. GRAYZEL, A.I., STIMULATION OF GLOBIN SYNTHESIS BY HEME, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 55: 650 (1966).
  6. KENG, T, THE 9 AMINO-TERMINAL RESIDUES OF DELTA-AMINOLEVULINATE SYNTHASE DIRECT BETA-GALACTOSIDASE INTO THE MITOCHONDRIAL MATRIX, MOLECULAR AND CELLULAR BIOLOGY 6: 355 (1986).
  7. LATHROP J.T. THESIS U VIRGINIA (1992).
  8. MURAKAMI, K, RECONSTITUTION OF MITOCHONDRIAL PROTEIN-TRANSPORT WITH PURIFIED ORNITHINE CARBAMOYLTRANSFERASE PRECURSOR EXPRESSED IN ESCHERICHIA-COLI, JOURNAL OF BIOLOGICAL CHEMISTRY 263: 18437 (1988). · doi:10.1016/s0021-9258(19)81377-7
  9. RANU, R.S., METHODS IN ENZYMOLOGY 60: 459 (1979). · doi:10.1016/s0076-6879(79)60045-9
  10. SRIVASTAVA, G, HEMIN INHIBITS TRANSFER OF PRE-DELTA-AMINOLEVULINATE SYNTHASE INTO CHICK-EMBRYO LIVER-MITOCHONDRIA, BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS 117: 344 (1983). · doi:10.1016/0006-291x(83)91582-6
  11. TANAKA, Y, SITE-DIRECTEDLY MUTATED HUMAN CYTOCHROME-C WHICH RETAINS HEME-C VIA ONLY ONE THIOETHER BOND, JOURNAL OF BIOCHEMISTRY 108: 7 (1990). · doi:10.1093/oxfordjournals.jbchem.a123165
  12. YOUNG E.G. THESIS U VIRGINIA (1990).

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Metadata

Authors
Lathrop, J. T., & Timko, M. P.
Venue
Science
Publisher
American Association for the Advancement of Science (AAAS)
Published
1993-01-22
Volume
259
Issue
5094
Pages
522-525
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
DOI
10.1126/science.8424176
OpenAlex
W2053114862
Cited by
287
References
26
FWCI
3.25
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Regulation by Heme of Mitochondrial Protein Transport Through a Conserved Amino Acid Motif. https://app.cochat.ai/papers/10.1126/science.8424176
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Lathrop, J. T., & Timko, M. P. (1993). Regulation by Heme of Mitochondrial Protein Transport Through a Conserved Amino Acid Motif. Science. https://doi.org/10.1126/science.8424176

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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