CoChat
Sign Up
Cited by 169

The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.

Protein prenylation: more than just glue?

Cox, Adrienne D., Der, Channing J.·1992·Current Opinion in Cell Biology
DOI 10.1016/0955-0674(92)90133-w
Open this paper in CoChat — free account

Abstract

As with other lipid modifications of proteins, prenylation now appears to be critically important in the regulation of protein function. Recent research has led to an explosion of information concerning prenylation signals, prenyl transferase enzymes and the role of prenylation in protein-membrane interactions. Experiments have examined the role of prenylation in protein function and the results suggest that protein prenylation may be involved in facilitating proper subcellular localization, promoting protein-protein and protein-membrane interactions and regulating protein function.

Overview

Integrity signals

Registry

Crossref · 10.1016/0955-0674(92)90133-w

Cites

2 of 2 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Verification

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Citations

Cites

Research works printed but not linked: 44

  1. Maltese, 1990, Posttranslational Modification of Proteins by Isoprenoids in Mammalian Cells, FASEB J, 4, 3319, 10.1096/fasebj.4.15.2123808 · DOI
  2. Glomset, 1990, Prenyl Proteins in Eukaryotic Cells: a New Type of Membrane Anchor, Trends Biochern Sci, 15, 139, 10.1016/0968-0004(90)90213-U · DOI
  3. Clarke, 1992, Protein Isoprenylation and Methylation at Carboxyl-terminal Cysteine Residues, Annu Rev Biochem, 61, 355, 10.1146/annurev.bi.61.070192.002035 · DOI
  4. Chow, 1992, Structure and Biological Effects of Lipid Modifications on Proteins, Curr Opin Cell Biol, 4, 629, 10.1016/0955-0674(92)90082-N · DOI
  5. Cox, 1992, The Ras/Cholesterol Connection: Implications for Ras Oncogenicity, Crit Rev Oncogenesis, 3, 365
  6. Khosravi-Far, 1992, Protein Prenylation: Key to Ras Function and Cancer Intervention?, Cell Growth Diff, 3, 461
  7. Hancock, 1991, Methylation and Proteolysis Are Essential for Efficient Membrane Binding of Prenylated p21K-ras(B), EMBO J, 10, 641, 10.1002/j.1460-2075.1991.tb07992.x · DOI
  8. Hancock, 1991, A CAAX or a CAAL Motif and a Second Signal Are Sufficient for Plasma Membrane Targeting of Ras Proteins, EMBO J, 10, 4033, 10.1002/j.1460-2075.1991.tb04979.x · DOI
  9. Gutierrez, 1991, Characterization of an Acyltransferase Acting on p21N-ras Protein in a Cell-free System, Biochim Biophys Acta, 1078, 147, 10.1016/0167-4838(91)99003-B · DOI
  10. Moores, 1991, Sequence Dependence of Protein Isoprenylation, J Biol Chem, 266, 14603, 10.1016/S0021-9258(18)98729-6 · DOI
  11. Seabra, 1991, Protein Famesyltransferase and Geranylgeranyltransferase Share a Common a Subunit, Cell, 65, 429, 10.1016/0092-8674(91)90460-G · DOI
  12. Cox, 1992, Specific Isoprenoid Modification is Required for Function of Normal, but not Oncogenic, Ras Protein, Mol Cell Biol, 12, 2606
  13. Goldstein, 1991, Nonfarnesylated Tetrapeptide Inhibitors of Protein Famesyltransferase, J Biol Chem, 266, 15575, 10.1016/S0021-9258(18)98441-3 · DOI
  14. Adamson, 1992, Post-translational Modifications of p21rho Proteins, J Biol Chem, 267, 20033, 10.1016/S0021-9258(19)88661-1 · DOI · Paper page
  15. Kinsella, 1992, Rab GTP-binding Proteins with Three Different Carboxyl-terminal Cysteine Motifs are Modified in Vivo by 20-carbon Isoprenoids, J Biol Chem, 267, 3940, 10.1016/S0021-9258(19)50616-0 · DOI
  16. Khosravi-Far, 1992, Ras (CXXX) and Rab (CC/CXC) Prenylation Signal Sequences Are Unique and Functionally Distinct, J Biol Chem, 10.1016/S0021-9258(18)35774-0 · DOI
  17. Morimoto, 1991, Molecular Cloning of a Member of a New Class of Low-molecular-weight GTP-binding Proteins, Genes Dev, 5, 2386, 10.1101/gad.5.12b.2386 · DOI
  18. Reiss, 1992, Divalent Cation and Prenyl Pyrophosphate Specificities of the Protein Farnesyltransferase from Rat Brain, a Zinc Metalloenzyme, J Biol Chem, 267, 6403, 10.1016/S0021-9258(18)42709-3 · DOI
  19. Reiss, 1991, Nonidentical Subunits of p21H-ras Farnesyltransferase, J Biol Chem, 266, 10672, 10.1016/S0021-9258(18)99276-8 · DOI
  20. Gomez, 1992, Purified Yeast Protein Farnesyltransferase is Structurally and Functionally Similar to Its Mammalian Counterpart, Biochem J
  21. Horiuchi, 1991, A Novel Prenyltransferase for a Small GTP-binding Protein Having a C-terminal Cys-Ala-Cys Structure, J Biol Chem, 266, 16981, 10.1016/S0021-9258(19)47327-4 · DOI
  22. Seabra, 1992, Rab Geranylgeranyl Transferase: a Multisubunit Enzyme that Prenylates GTP-binding Proteins Terminating in Cys-X-Cys or CysCys, J Biol Chem, 267, 14497, 10.1016/S0021-9258(19)49740-8 · DOI
  23. Moomaw, 1992, Mammalian Protein Geranylgeranyltransferase, J Biol Chem, 267, 17438, 10.1016/S0021-9258(18)41945-X · DOI
  24. Seabra, 1992, Purification of Component A of Rab Geranylgeranyltransferase: Possible Identity with the Choroideremia Gene Product, Cell, 70, 1049, 10.1016/0092-8674(92)90253-9 · DOI · Paper page
  25. Boguski, 1992, Novel Repetitive Sequence Motifs in the a and β Subunits of Prenyl-protein Transferases and Homology of the a Subunit to the MAD2 Gene Product of Yeast, N Biol, 4, 408
  26. Fodor, 1991, Analysis of Choroideraemia Gene, Nature, 351, 614, 10.1038/351614b0 · DOI
  27. Takai, 1992, Small GTP-binding Proteins, Int Rev Cytol, 133, 187, 10.1016/S0074-7696(08)61861-6 · DOI
  28. Ridley, 1992, The Small GTP-binding Protein Rho Regulates the Assembly of Focal Adhesions and Actin Stress Fibers in Response to Growth Factors, Cell, 70, 389, 10.1016/0092-8674(92)90163-7 · DOI
  29. Ridley, 1992, The Small GTP-binding Protein Rac Regulates Growth Factor-induced Membrane Ruffling, Cell, 70, 401, 10.1016/0092-8674(92)90164-8 · DOI
  30. Abo, 1991, Activation of the NADPH Oxidase Involves the Small GTPbinding Protein p21rac-1, Nature, 353, 668, 10.1038/353668a0 · DOI
  31. Knaus, 1991, Regulation of Phagocyte Oxygen Radical Production by the GTP-binding Protein Rac 2, Science, 254, 1512, 10.1126/science.1660188 · DOI · Paper page
  32. Ohguro, 1991, Carboxyl Methylation and Famesylation of Transducin γ-subunit Synergistically Enhance Its Coupling with Metarhodopsin II, EMBO J, 10, 3669, 10.1002/j.1460-2075.1991.tb04934.x · DOI
  33. Ingiese, 1992, Isoprenylation of a Protein Kinase, J Biol Chem, 267, 1422
  34. Anant, 1992, In Vivo Differential Prenylation of Retinal Cyclic GMP Phosphodiesterase Catalytic Subunits, J Biol Chem, 267, 687, 10.1016/S0021-9258(18)48336-6 · DOI
  35. Bokoch, 1992, Isoprenoid Metabolism is Required for Stimulation of the Respiratory Burst Oxidase of HL-60 Cells, J Clin Invest, 89, 402, 10.1172/JCI115599 · DOI
  36. Law, 1992, Lipopolysaccharide-induced NFxB Activation in Mouse 70Z/3 Pre-B Lymphocytes is Inhibited by Mevinolin and 5′-methylthioadenosine: Roles of Protein Prenylation and Carboxyl Methylation Reactions, Mol Cell Biol, 12, 103
  37. Glenn, 1992, Identification of a Prenylation Site in Delta Virus Large Antigen, Science, 256, 1331, 10.1126/science.1598578 · DOI
  38. Caplan, 1992, Famesylation of YDJ1p is Required for Function at Elevated Growth Temperatures in Saccbaromyces cerevisiae, J Biol Chem, 267, 18890, 10.1016/S0021-9258(19)37044-9 · DOI
  39. Gibbs, 1991, Ras C-terminal Processing Enzymes — New Drug Targets?, Cell, 65, 1, 10.1016/0092-8674(91)90352-Y · DOI
  40. Hrycyna, 1991, The Saccbaromyces cerevisiae STE14 Gene Encodes a Methyltransferase that Mediates C-terminal Methylation of a-factor and RAS Proteins, EMBO J, 10, 1699, 10.1002/j.1460-2075.1991.tb07694.x · DOI
  41. Musha, 1992, The Geranylgeranyl Moiety but not the Methyl Moiety of the Smg25A/Rab3A Protein is Essential for the Interactions with Membrane and Its Inhibitory GDP/GTP Exchange Protein, J Biol Chem, 267, 9821, 10.1016/S0021-9258(19)50167-3 · DOI
  42. Marcus, 1991, Significance of C-terminal Cysteine Modifications to the Biological Activity of the Saccbaromyces cerevisiae a-factor Mating Pheromone, Mol Cell Biol, 11, 3603
  43. Marshal, 1991, Identification of Amino Acid Residues Required for Ras p21 Target Activation, Mol Cell Biol, 11, 3997
  44. Koch, 1992, Posttranslational Isoprenylation of Rho Proteins is a Prerequisite for Its Interaction with Mastoparan and other Amphiphilic Agents, Biochem Biophys Res Commun, 186, 448, 10.1016/S0006-291X(05)80828-9 · DOI

Cited by

See all 169

Metadata

Authors
Cox, A. D., & Der, C. J.
Venue
Current Opinion in Cell Biology
Publisher
Elsevier BV
Published
1992-12
Volume
4
Issue
6
Pages
1008-1016
ISSN
0955-0674
DOI
10.1016/0955-0674(92)90133-w
Cited by
169
References
2
Language
en
Licence

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review