-
1
-
-
0027377202
-
The X-Ray Structure of the GCN4 bZIP Bound to ATF/CREB Site DNA Shows the Complex Depends on DNA Flexibility
-
of outstanding interest, The crystal structure of GCN4 bound to the creb response element shows an unexpected distorsion of the DNA that permits the protein to contact the same bases as those contacted in the GCN4/AP-1 DNA complex.
-
(1993)
Journal of Molecular Biology
, vol.233
, pp. 139-154
-
-
Konig1
Richmond2
-
2
-
-
0027910469
-
Recognition by Max of its Cognate DNA Through a Dimeric b/HLH/Z Domain
-
of outstanding interest, The crystal structure of a basic region-helix loop helix domain bound to DNA is presented in this paper. The fold of the helix loop helix and the specific DNA contacts made by the Max homodimer are discussed as they relate to previous genetic and biochemical studies of this family of proteins.
-
(1993)
Nature
, vol.363
, pp. 38-45
-
-
Ferre-d'amare1
Prendergast2
Ziff3
Burley4
-
3
-
-
0027049805
-
The GCN4 Basic Region Leucine Zipper Binds DNA as a Dimer of Uninterrupted a-Helices: Crystal Structure of the ProteinDNA Complex
-
of outstanding interest, The crystal structure of the GCN4 bZIP domain on the AP-1 DNA site shows that the subunits of the dimer make nonequivalent contacts to the central base-pair of the binding site. The amino acids contacting DNA bases in the GCN4 complex are conserved among bZIP proteins having diverse DNA-binding specificities.
-
(1992)
Cell
, vol.71
, pp. 1223-1237
-
-
Ellenberger1
Brandl2
Struhl3
Harrison4
-
5
-
-
0025182484
-
Design of DNA binding peptides based on the Leucine Zipper motif
-
of special interest, The authors propose the ‘induced helical fork’ model for the basic region leucine zipper domain on the basis of the DNA binding activities of synthetic peptides containing a minimal number of GCN4 residues.
-
(1990)
Science
, vol.249
, pp. 774-778
-
-
O'Neil1
Hoess2
Degrado3
-
7
-
-
0025017975
-
Altered Protein Conformation on DNA Binding by Fos and Jun
-
(1990)
Nature
, vol.347
, pp. 572-574
-
-
Patel1
Abate2
Curran3
-
12
-
-
0027399193
-
High Affinity DNA-binding Myc Analogs: Recognition by an α-Helix
-
of special interest, An exhaustive mutational analysis of the TFEB and Myc bHLH-zipper domains showing the importance of residues that have subsequently been shown to contact the DNA of the Max/DNA complex.
-
(1993)
Cell
, vol.72
, pp. 467-476
-
-
Fisher1
Parent2
Sharp3
-
13
-
-
0025995844
-
A Structural Taxonomy of DNA-Binding Domains
-
(1991)
Nature
, vol.353
, pp. 715-719
-
-
Harrison1
-
14
-
-
0026682657
-
Transcription Factors: Structural Fami-lies and Principles of DNA Recognition
-
(1992)
Annu Rev Biochem
, vol.61
, pp. 1053-1095
-
-
Pabo1
Sauer2
-
15
-
-
0024990252
-
Mutations That Define the Optimal Half-site for Binding Yeast GCN4 Activator Pro tcin and Identify an ATF/CREB-like Repressor That Recognizes Similar DNA Sites
-
(1990)
Mol Cell Biol
, vol.10
, pp. 5077-5086
-
-
Sellers1
Vincent2
Struhl3
-
16
-
-
0024370748
-
Scissors-Grip Model for DNA Recognition by a Family of Leucine Zipper Proteins
-
of special interest, The authors propose the ‘scissors-grip’ model, which correctly predicted some of the essential features of the basic region leucine zipper structure.
-
(1989)
Science
, vol.246
, pp. 911-916
-
-
Vinson1
Sigler2
McKnight3
-
17
-
-
0026534215
-
Predicted Structural Similarities of the DNA Binding Domains of c-Myc and Endonuclease Eco RI
-
(1992)
Science
, vol.255
, pp. 464-466
-
-
Halazonetis1
Kandil2
-
18
-
-
0026842208
-
Molecular Model for DNA Recognition by the Family of Basic-Helix-Loop-Helix-Zipper Proteins
-
(1992)
The New Biologist
, vol.4
, pp. 39603
-
-
Vinson1
Garcia2
-
20
-
-
0026331267
-
X-ray Structure of the GCN4 Lcucinc Zipper, a Two-Strandcd, Parallel Coiled Coil
-
of outstanding interest, The authors determined the first and, to date, the only high resolution structure of a leucine zipper. The details of a-helical packing in the coiled-coil are presented.
-
(1991)
Science
, vol.254
, pp. 539-544
-
-
O'Shea1
Klemm2
Kim3
Alber4
-
21
-
-
0026845838
-
Structure of the Leucine Zipper
-
of special interest, An excellent review of the GCN4 leucine zipper structure.
-
(1992)
Curr Opin Genet Dev
, vol.2
, pp. 205-210
-
-
Alber1
-
23
-
-
0026463516
-
What is the Pitch of the a-helical Coiled Coil?
-
(1992)
Proteins
, vol.14
, pp. 425-429
-
-
Phillips1
-
25
-
-
0027176792
-
Dimcrization Specificity of the Leucine Zippcrcontaining bZIP Motif on DNA Binding: Prediction and Rational Design
-
of special interest, The authors develop an ‘i+5’ rule for interhelical salt bridges involving surface residues of the leucine zipper. The utility of the this rule is shown by the manipulation of C/EBP's dimerization specificity via changes in ‘i+5’ residue-pairs.
-
(1993)
Genes Dev
, vol.7
, pp. 1047-1058
-
-
Vinson1
Hai2
Boyd3
-
26
-
-
0027180729
-
The Role of Surface Contacts in Leucine Zipper Stability
-
of special interest, The contributions of surface residues ‘e’ and ‘g’ to the dimerization activity of the GCN4 leucine zipper were systematically examined by screening a library of mutants containing alanine, glutamic acid, lysine, or threonine at these positions of the leucine zipper.
-
(1993)
Protein Science
, vol.2
, pp. 1072-1084
-
-
Hu1
Newell2
Tidor3
Sauer4
-
27
-
-
0025598302
-
Sequence Requirements for Coilcdcoils: Analysis with Lambda RepressorGCN4 Leucine Zipper Fusions
-
of special interest, An extensive mutational analysis of the GCN4 leucine zipper was performed using a genetic screen for dimerization activity.
-
(1990)
Science
, vol.250
, pp. 1400-1403
-
-
Hu1
O'Shfa2
Kim3
Sauer4
-
28
-
-
0024370723
-
Leucine Zippers of fos, jun, and GCN4 Dictate Dimcrization Specificity and Thereby Control DNA Binding
-
(1989)
Nature
, vol.340
, pp. 568-571
-
-
Kouzarides1
Ziff2
-
30
-
-
0024535960
-
Leucine Repeats and an Adjacent DNA Binding Domain Mediate the Formation of Functional cFoscJun Heterodimers
-
(1989)
Science
, vol.243
, pp. 1689-1694
-
-
Turner1
Tjian2
-
32
-
-
0026073643
-
Non-leucine Residues in the Leucine Repeats of Fos and Jun Contribute to the Stability and Determine the Specificity of Dimerization
-
of special interest, Alternate hydrophobes at position ‘a’ of the leucine zipper, and charged surface residues ‘e’ and ‘g’ are shown to influence the dimerization specificties of Fos and Jun.
-
(1991)
Nuc Acids Res
, vol.19
, pp. 739-746
-
-
Schuermann1
Hunter2
Hennig3
Mueller4
-
33
-
-
0026571898
-
Mechanism of Specificity in the Fos-Jun Oncoprotein Heterodimer
-
of special interest, A thermodynamic analysis of Fos-Jun heterodimerization showing the importance of charged residues on the surface of their leucine zippers.
-
(1992)
Cell
, vol.68
, pp. 699-708
-
-
O'Shea1
Rutkowski2
Kim3
-
35
-
-
0024511105
-
Involvement of the Leucine Zipper Region in the Oligomerization and Transforming Activity of Human c-Myc Protein
-
(1989)
Nature
, vol.337
, pp. 664-666
-
-
Dang1
McGuire2
Buckmim3
Lee4
-
37
-
-
0025084602
-
The Adenovirus Major Late Transcription Factor USF is a Member of the Helix-Loop-Helix Group of Regulatory Proteins and Binds to DNA as a Dimer
-
(1990)
Genes Dev
, vol.4
, pp. 1730-1740
-
-
Gregor1
Sawadogo2
Roeder3
-
38
-
-
0025763419
-
Max A Helix-loop-Helix Zipper Protein That Forms a Sequence-Specific DNA-binding Complex With Myc
-
(1991)
Science
, vol.251
, pp. 1211-1217
-
-
Blackwood1
Eisenman2
-
40
-
-
0025821904
-
The Leucine Zipper of TFE3 Dictates Helix-loop-helix Dimerization Specificity
-
(1991)
Genes Dev.
, vol.5
, pp. 1057-1066
-
-
Beckmann1
Kadesch2
-
41
-
-
0025719216
-
TFEB Has DNA-binding and Oligomerization Properties of a Unique Helix-Loop-Helix/Leucine Zipper Family
-
(1991)
Genes Dev
, vol.5
, pp. 2342-2352
-
-
Fisher1
Carr2
Parent3
Sharp4
-
42
-
-
0027462748
-
Both the Helix-Loop-Helix and the Lcucine Zipper Motifs of c-Myc Contribute to Its Dimerization Specificity with Max
-
(1992)
Oncogene
, vol.7
, pp. 125-132
-
-
Davis1
Halazonetis2
-
45
-
-
0026798829
-
Helix-loop-helix Proteins in the Regulation of Immunogobulin Gene Transcription
-
(1992)
Immunology Today
, vol.33
, pp. 31-36
-
-
Kadesch1
-
48
-
-
0025829169
-
Association of Myn, the Murine Homolog of Max, With c-Myc Stimulates Methylation-sensitive DNA Binding and Ras Cotransforma-tion
-
(1991)
Cell
, vol.65
, pp. 395-407
-
-
Prendergast1
Lawe2
Ziff3
-
51
-
-
0026603423
-
Uracil Interference, a Rapid and General Method for Defining Protein-DNA Interactions Involving the 5-methyl Group of Thymincs: The GCN4-DNA Complex
-
(1992)
Nuc Acids Res
, vol.20
, pp. 771-775
-
-
Pu1
Struhl2
-
52
-
-
0026782249
-
Identification of an Amino Acid-Bast Contact in the GCN4-DNA Complex by Bromouracil-mediated Photocrosstinking
-
(1992)
Nature
, vol.359
, pp. 650-652
-
-
Blatter1
Ebright2
Ebright3
-
53
-
-
0025940099
-
Highly Conserved Residues in the bZIP Domain of Yeast GCN4 Are Not Essential for DNA Binding
-
(1991)
Mol Cell Biol
, vol.11
, pp. 4918-4926
-
-
Pu1
Strum2
-
55
-
-
0027479165
-
Identification of Three Residues in the Basic Regions of the bZIP Proteins GCN4, C/EBP and TAF-1 That Are Involved in Specific DNA Binding
-
of special interest, The DNA-binding specificity of GCN4 is converted to that of C/EBP following a limited number of amino acid replacements.
-
(1993)
EMBO J
, vol.12
, pp. 1193-1200
-
-
Suckow1
von Wilcken-Bergmann2
Moller-Hill3
-
59
-
-
0027339727
-
Altered Specificity of DNA-binding Proteins with Transition Metal Dimerization Domains
-
(1993)
Science
, vol.259
, pp. 510-513
-
-
Cuenoud1
Schepartz2
-
60
-
-
0027458868
-
Design of a Metallo-bZIP Protein That Discriminates Between CRE and API Target Sites: SeIcction Against API
-
2nd edition
-
(1993)
Proc Nail Acad Sci USA
, vol.90
, pp. 1154-1159
-
-
Cuenoud1
Schepartz2
-
61
-
-
0027327313
-
Binding of Myc Proteins to Canonical and Noncanonical DNA Sequences
-
of special interest, Selection of Myc-Max binding sites from pools of randomized sequences reveals atypical sites that are selectively bound by Myc-Max, but not bound by related bHLH proteins.
-
(1993)
Mol CeU Biol
, vol.13
, pp. 5216-5224
-
-
Blackwell1
Huang2
Ma3
Kretzner4
Alt5
Eisenman6
Weintraub7
-
63
-
-
0026670518
-
Single Amino Acid Substitutions Alter Helix-Loop-Helix Protein Specificity for Bases Flanking the Core CANNTG Motif
-
(1992)
EMBO J
, vol.11
, pp. 4103-4109
-
-
Fisher1
Goding2
-
65
-
-
0026546825
-
Discrimination Between Related DNA Sites by a Single Amino Acid Residue of Myc-related Basic-Helix-Loop-Helix Proteins
-
of special interest, 2nd edition, The authors classify bHLH proteins according to their binding site preferences and show that the binding preference of CBF1 primarily depends upon the identity of one residue within the basic region.
-
(1992)
Proc. Natl Acad Sci USA
, vol.89
, pp. 599-602
-
-
Dang1
Dolde2
Gillison3
Kato4
-
66
-
-
0026667715
-
A Point Mutation in the MyoD Basic Domain Imparts c-Myelike Properties
-
of special interest, 2nd edition, The DNA-binding specificity of MyoD is converted to that of Myc by mutating the same basic region residue that was identified in [63∗]. The identity of a second basic region residue influences discrimination against the MyoD binding site.
-
(1992)
Proc Natl Acad Sci USA
, vol.89
, pp. 9010-9014
-
-
van Antwerp1
Chen2
Chang3
Prochownik4
-
67
-
-
0025572707
-
Differences and Similarities in DNA-binding Preferences of MyoD and E2A PRotcin Complexes Revealed by Binding Site Selection
-
(1990)
Science
, vol.250
, pp. 1104-1110
-
-
Blackwell1
Weintraub2
-
70
-
-
0025902328
-
Fos-Jun Hctcrodimers and Jun Homodimcrs Bend DNA in Opposite Orientations: Implication for Transcription Factor Coopcrativity
-
(1991)
Cell
, vol.66
, pp. 317-326
-
-
Kerppola1
Curran2
-
71
-
-
0026315512
-
DNA Bending by Fos and Jun: The Flexible Hinge Model
-
(1991)
Science
, vol.254
, pp. 1210-1214
-
-
Kerppola1
Curran2
-
76
-
-
0025996912
-
Cooperative Interaction of an Initiator-binding Transcription Initiation Factor and the Helix-Loop-Helix Activator USF
-
(1991)
Nature
, vol.354
, pp. 245-248
-
-
Roy1
Meisterernst Pognonec2
Pogder3
-
78
-
-
0026680845
-
Interaction Cloning: Identification of a Helix-Loop-Helix Zipper Protein That Interacts With c-Fos
-
(1992)
Science
, vol.256
, pp. 1014-1018
-
-
Blanar1
Rutter2
-
79
-
-
0026766680
-
Acquisition of Myogenic Specificity by Replacement of Three Amino Acid Residues From MyoD Into E12
-
(1992)
Science
, vol.256
, pp. 1027-1030
-
-
Davis1
Weintraub2
-
80
-
-
0026606084
-
Fos and Jun Repress Transcriptional Activation by Myogenin and MyoD: the Amino Terminus of Jun Can Mediate Repression
-
(1992)
Genes Dev
, vol.6
, pp. 676-689
-
-
Li1
Chambard2
Karin3
Olson4
-
81
-
-
0026687925
-
Cyclic Amplification and Selection of Targets for Multicomponent Complexes: Myogenin Interacts With Factors Recognizing Binding Sites For Ba sic Helix-Loop-Helix, Nuclear Factor 1, Myocyte-specific Enhanccr-bindng Factor 2, and COMPI Factor
-
2nd edition
-
(1992)
Proc Natl Acad Sci USA
, vol.89
, pp. 9484-9488
-
-
Funk1
Wright2
|