Crossref
journal-article
Elsevier BV
Journal of Molecular Biology (78)
References
41
Referenced
13
10.1002/prot.10398
/ Proteins: Struct. Funct. Genet. / CAPRI—critical assesemnt of predicted interaction by Janin (2003)10.1016/j.jmb.2003.10.069
/ J. Mol. Biol. / Identification of protein–protein interaction sites from docking energy landscapes by Fernandez-Recio (2004)10.1002/prot.10389
/ Proteins: Struct. Funct. Genet. / ZDOCK: an initial-stage protein-docking algorithm by Chen (2003)10.1128/MCB.13.4.2478
/ Mol. Cell. Biol. / Two cofactors and cytoplasmic chaperonin are required for the folding of alpha and beta tubulin by Gao (1993)10.1083/jcb.138.4.821
/ J. Cell Biol. / Tubulin subunits exist in an activated conformational state generated and maintained by protein cofactors by Tian (1997)10.1083/jcb.200208001
/ J. Cell Biol. / Missense mutation in the tubulin-specific chaperone E (Tbce) gene in the mouse mutant progressive motor neuronopathy, a model of human motoneuron disease by Bommel (2002)10.1105/tpc.003020
/ Plant Cell / The Arabidopsis tubulin-folding cofactor A gene is involved in the control of the alpha/beta-tubulin monomer balance by Kirik (2002)10.1016/0092-8674(95)90431-X
/ Cell / RbI2p, a yeast protein that binds to beta-tubulin and participates in microtubule function in vivo by Archer (1995)10.1083/jcb.144.1.113
/ J. Cell Biol. / Alf1p, a CLIP-170 domain-containing protein, is functionally and physically associated with alpha-tubulin by Feierbach (1999)10.1083/jcb.149.5.1087
/ J. Cell Biol. / ADP ribosylation factor-like protein 2 (Arl2) regulates the interaction of tubulin-folding cofactor D with native tubulin by Bhamidipati (2000)10.1093/genetics/124.2.251
/ Genetics / Yeast mutants sensitive to antimicrotubule drugs define three genes that affect microtubule function by Stearns (1990)10.1091/mbc.8.6.1035
/ Mol. Biol. Cell / Saccharomyces cerevisiae genes required in the absence of the CIN8-encoded spindle motor act in functionally diverse mitotic pathways by Geiser (1997)10.1128/MCB.18.3.1757
/ Mol. Cell. Biol. / Formation and function of the Rbl2p-beta-tubulin complex by Archer (1998)10.1091/mbc.11.5.1887
/ Mol. Biol. Cell / Structure–function relationships in yeast tubulins by Richards (2000)10.1038/14912
/ Nature Struct. Biol. / Crystal structure of the post-chaperonin beta-tubulin binding cofactor Rbl2p by Steinbacher (1999)10.1038/34465
/ Nature / Structure of the alpha beta tubulin dimer by electron crystallography by Nogales (1998)10.1073/pnas.95.19.11158
/ Proc. Natl Acad. Sci. USA / Clustering of low-energy conformations near the native structures of small proteins by Shortle (1998)10.1091/mbc.5.1.29
/ Mol. Biol. Cell / Systematic mutational analysis of the yeast β-tubulin gene by Reijo (1994)10.1091/mbc.01-09-0458
/ Mol. Biol. Cell / Stu1p is physically associated with beta-tubulin and is required for structural integrity of the mitotic spindle by Yin (2002)10.1016/S0014-5793(96)01198-2
/ FEBS Letters / The beta-tubulin monomer release factor (p14) has homology with a region of the DnaJ protein by Llosa (1996)10.1091/mbc.9.9.2349
/ Mol. Biol. Cell / An alpha-tubulin mutant destabilizes the heterodimer: phenotypic consequences and interactions with tubulin-binding proteins by Vega (1998)10.1002/prot.10092
/ Proteins: Struct. Funct. Genet. / Docking unbound proteins using shape complementarity, desolvation, and electrostatics by Chen (2002)10.1002/prot.10383
/ Proteins: Struct. Funct. Genet. / ICM-DISCO docking by global energy optimization with fully flexible side-chains by Fernandez-Recio (2003)10.1002/prot.10134
/ Proteins: Struct. Funct. Genet. / Model of the alphaLbeta2 integrin I-domain/ICAM-1 DI interface suggests that subtle changes in loop orientation determine ligand specificity by Legge (2002)10.1126/science.1061692
/ Science / Crystal structure of a neutralizing human IGG against HIV-1: a template for vaccine design by Saphire (2001)10.1002/jcc.20088
/ J. Comput. Chem. / Optimization and dynamics of protein–protein complexes using B-splines by Gillilan (2004)10.1093/protein/12.4.271
/ Protein Eng. / An analysis of conformational changes on protein–protein association: implications for predictive docking by Betts (1999)10.1016/S0092-8674(00)81806-1
/ Cell / Transcription activation at class II CAP-dependent promoters: two interactions between CAP and RNA polymerase by Niu (1996)10.1006/jmbi.1996.0052
/ J. Mol. Biol. / Functional significance of loops in the receptor binding domain of Bacillus thuringiensis CryIIIA delta-endotoxin by Wu (1996)10.1006/jmbi.1998.1748
/ J. Mol. Biol. / Ecotin: a serine protease inhibitor with two distinct and interacting binding sites by Yang (1998)10.1091/mbc.E01-10-0089
/ Mol. Biol. Cell / Dissociation of the tubulin dimer is extremely slow, thermodynamically very unfavorable, and reversible in the absence of an energy source by Caplow (2002)10.1016/S0022-2836(02)00185-7
/ J. Mol. Biol. / Three-dimensional structure of human tubulin chaperone cofactor A by Guasch (2002)10.1002/(SICI)1096-987X(199604)17:5/6<490::AID-JCC1>3.0.CO;2-P
/ J. Comput. Chem. / Merck molecular force field. I. Basis, form, scope, parameterization, and performance of MMFF94 by Halgren (1996){'key': '10.1016/j.jmb.2004.06.081_bib34', 'series-title': 'Cluster Dissection and Analysis Theory, FORTRAN Programs and Examples. FORTRAN Programs and Examples', 'author': 'Spath', 'year': '1985'}
/ Cluster Dissection and Analysis Theory, FORTRAN Programs and Examples. FORTRAN Programs and Examples by Spath (1985)10.1146/annurev.bb.06.060177.001055
/ Annu. Rev. Biophys. Bioeng. / Areas, volumes, packing and protein structure by Richards (1977)10.1109/38.310720
/ IEEE Comp. Graph. Appl. / Linearly scalable computation of smooth molecular surfaces by Varshney (1994){'key': '10.1016/j.jmb.2004.06.081_bib37', 'series-title': 'Data Visualization in Molecular Science', 'first-page': '61', 'article-title': 'Visualizing enzyme electrostatics with IBM visualization data explorer', 'author': 'Gillilan', 'year': '1995'}
/ Data Visualization in Molecular Science / Visualizing enzyme electrostatics with IBM visualization data explorer by Gillilan (1995)10.1016/0076-6879(91)94004-V
/ Methods Enzymol. / Getting started with yeast by Sherman (1991)10.1016/0378-1119(89)90358-2
/ Gene / Site-directed mutagenesis by overlap extension using the polymerase chain reaction by Ho (1989)10.1101/gad.7.4.555
/ Genes Dev. / The retinoblastoma protein associates with the protein phosphatase type 1 catalytic subunit by Durfee (1993)10.1007/s008940050010
/ J. Mol. Model / Molecular dynamics of the Ha-ras protein: nucelotide atom-centred within the AMBER force field by Worth (1995)
Dates
Type | When |
---|---|
Created | 20 years, 10 months ago (Oct. 21, 2004, 2:48 p.m.) |
Deposited | 4 years, 2 months ago (June 26, 2021, 3:55 p.m.) |
Indexed | 1 year, 5 months ago (March 14, 2024, 5:20 a.m.) |
Issued | 21 years ago (Aug. 1, 2004) |
Published | 21 years ago (Aug. 1, 2004) |
Published Print | 21 years ago (Aug. 1, 2004) |
@article{You_2004, title={Model for the Yeast Cofactor A–β-Tubulin Complex Based on Computational Docking and Mutagensis}, volume={341}, ISSN={0022-2836}, url={http://dx.doi.org/10.1016/j.jmb.2004.06.081}, DOI={10.1016/j.jmb.2004.06.081}, number={5}, journal={Journal of Molecular Biology}, publisher={Elsevier BV}, author={You, Liru and Gillilan, Richard and Huffaker, Tim C.}, year={2004}, month=aug, pages={1343–1354} }