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11 results for uniprot:P38254 in Computationally mapped citations

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Functional analysis of 150 deletion mutants in Saccharomyces cerevisiae by a systematic approach.

Entian K.-D., Schuster T., Hegemann J.H., Becher D., Feldmann H., Gueldener U., Goetz R., Hansen M., Hollenberg C.P., Jansen G. et al.

Mol. Gen. Genet. 262:683-702(1999) SGD S000000298 · UniProtKB (10) · Mapped (130)
Strains/Constructs|Mutants/Phenotypes SGD S000000298

Systematic genetic analysis with ordered arrays of yeast deletion mutants.

Tong A.H., Evangelista M., Parsons A.B., Xu H., Bader G.D., Page N., Robinson M., Raghibizadeh S., Hogue C.W., Bussey H. et al.

Science 294:2364-2368(2001) SGD S000000298 · Mapped (197)
Genetic Interactions|Strains/Constructs SGD S000000298

Elg1 forms an alternative RFC complex important for DNA replication and genome integrity.

Bellaoui M., Chang M., Ou J., Xu H., Boone C., Brown G.W.

EMBO J. 22:4304-4313(2003) SGD S000000298 · UniProtKB (4) · Mapped (34)
Genetic Interactions|Strains/Constructs SGD S000000298

Global mapping of the yeast genetic interaction network.

Tong A.H., Lesage G., Bader G.D., Ding H., Xu H., Xin X., Young J., Berriz G.F., Brost R.L., Chang M. et al.

Science 303:808-813(2004) SGD S000000298 · Mapped (943)
Genetic Interactions|Strains/Constructs SGD S000000298

A biological network in Saccharomyces cerevisiae prevents the deleterious effects of endogenous oxidative DNA damage.

Huang M.E., Kolodner R.D.

Mol. Cell 17:709-720(2005) SGD S000000298 · Mapped (24)
Genetic Interactions|Strains/Constructs|Mutants/Phenotypes|Function/Process SGD S000000298

Ccr4 contributes to tolerance of replication stress through control of CRT1 mRNA poly(A) tail length.

Woolstencroft R.N., Beilharz T.H., Cook M.A., Preiss T., Durocher D., Tyers M.

J. Cell. Sci. 119:5178-5192(2006) SGD S000000298 · Mapped (61)
Strains/Constructs|Mutants/Phenotypes SGD S000000298

A comprehensive analysis of protein-protein interactions in Saccharomyces cerevisiae.

Uetz P., Giot L., Cagney G., Mansfield T.A., Judson R.S., Knight J.R., Lockshon D., Narayan V., Srinivasan M., Pochart P. et al.

Nature 403:623-627(2000) MINT MINT-409689 · UniProtKB (7) · Mapped (984)
MINT-5742. RPS28A (uniprotkb:Q3E7X9) physically interacts (MI:0915) with YBR0821 (uniprotkb:P38254) by two hybrid array (MI:0397). From mint MINT MINT-409689

A comprehensive two-hybrid analysis to explore the yeast protein interactome.

Ito T., Chiba T., Ozawa R., Yoshida M., Hattori M., Sakaki Y.

Proc. Natl. Acad. Sci. U.S.A. 98:4569-4574(2001) MINT MINT-409689 MINT MINT-409689 · UniProtKB (9) · Mapped (3,197)
MINT-351. YBR0821 (uniprotkb:P38254) physically interacts (MI:0915) with DCP1 (uniprotkb:Q12517) by two hybrid pooling approach (MI:0398). From mint MINT MINT-409689 MINT-4319. RPS28A (uniprotkb:Q3E7X9) physically interacts (MI:0915) with YBR0821 (uniprotkb:P38254) by two hybrid pooling approach (MI:0398). From mint MINT MINT-409689

Functional organization of the yeast proteome by systematic analysis of protein complexes.

Gavin A.-C., Boesche M., Krause R., Grandi P., Marzioch M., Bauer A., Schultz J., Rick J.M., Michon A.-M., Cruciat C.-M. et al.

Nature 415:141-147(2002) MINT MINT-409689 · UniProtKB (14) · Mapped (1,461)
MINT-9606. YBR0821 (uniprotkb:P38254) physically interacts (MI:0915) with YBR0821 (uniprotkb:P38254) by anti tag coimmunoprecipitation (MI:0007). From mint MINT MINT-409689

Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry.

Ho Y., Gruhler A., Heilbut A., Bader G.D., Moore L., Adams S.-L., Millar A., Taylor P., Bennett K., Boutilier K. et al.

Nature 415:180-183(2002) MINT MINT-409689 · UniProtKB (3) · Mapped (1,358)
MINT-12670. YBU4 (uniprotkb:P38254) physically interacts (MI:0915) with CSK22 (uniprotkb:P19454) by anti tag coimmunoprecipitation (MI:0007). From mint MINT MINT-409689

Global landscape of protein complexes in the yeast Saccharomyces cerevisiae.

Krogan N.J., Cagney G., Yu H., Zhong G., Guo X., Ignatchenko A., Li J., Pu S., Datta N., Tikuisis A.P. et al.

Nature 440:637-643(2006) MINT MINT-409689 MINT MINT-409689 MINT MINT-409689 MINT MINT-409689 MINT MINT-409689 MINT MINT-409689 MINT MINT-409689 MINT MINT-409689 MINT MINT-409689 MINT MINT-409689 · UniProtKB (1) · Mapped (2,675)
MINT-2109445. DCP1 (uniprotkb:Q12517) physically interacts (MI:0915) with YBR0821 (uniprotkb:P38254) by tandem affinity purification (MI:0676). From mint MINT MINT-409689 MINT-2109463. EDC3 (uniprotkb:P39998) physically interacts (MI:0915) with YBR0821 (uniprotkb:P38254) by tandem affinity purification (MI:0676). From mint MINT MINT-409689 MINT-2311288. YBR0821 (uniprotkb:P38254) physically interacts (MI:0915) with EDC3 (uniprotkb:P39998) by tandem affinity purification (MI:0676). From mint MINT MINT-409689 MINT-2311306. YBR0821 (uniprotkb:P38254) physically interacts (MI:0915) with EDC3 (uniprotkb:P39998) by tandem affinity purification (MI:0676). From mint MINT MINT-409689 MINT-2350583. DCP1 (uniprotkb:Q12517) physically interacts (MI:0915) with YBR0821 (uniprotkb:P38254) by tandem affinity purification (MI:0676). From mint MINT MINT-409689 MINT-2358243. FOX2 (uniprotkb:Q02207) physically interacts (MI:0915) with YBR0821 (uniprotkb:P38254) by tandem affinity purification (MI:0676). From mint MINT MINT-409689 MINT-2780990. YBR0821 (uniprotkb:P38254), DCP1 (uniprotkb:Q12517) physically interact (MI:0914) by experimental knowledge based (MI:0046). From mint MINT MINT-409689 MINT-2780990. YBR0821 (uniprotkb:P38254), DCP2 (uniprotkb:P53550) physically interact (MI:0914) by experimental knowledge based (MI:0046). From mint MINT MINT-409689 MINT-2780990. YBR0821 (uniprotkb:P38254), EDC2 (uniprotkb:P40023) physically interact (MI:0914) by experimental knowledge based (MI:0046). From mint MINT MINT-409689 MINT-2780990. YBR0821 (uniprotkb:P38254), EDC3 (uniprotkb:P39998) physically interact (MI:0914) by experimental knowledge based (MI:0046). From mint MINT MINT-409689

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