Structure-function relationships in yeast tubulins. - Wikidata - awgldk - TriplyDB

Structure-function relationships in yeast tubulins.

Structure-function relationships in yeast tubulins.

http://www.wikidata.org/entity/Q34718050

about

Evolution of the cytoskeleton EBs Recognize a Nucleotide-Dependent Structural Cap at Growing Microtubule Ends Genome-wide fitness test and mechanism-of-action studies of inhibitory compounds in Candida albicans Dominant-lethal alpha-tubulin mutants defective in microtubule depolymerization in yeast An inherited TUBB2B mutation alters a kinesin-binding site and causes polymicrogyria, CFEOM and axon dysinnervation.The V260I mutation in fission yeast alpha-tubulin Atb2 affects microtubule dynamics and EB1-Mal3 localization and activates the Bub1 branch of the spindle checkpoint.Mal3, the Schizosaccharomyces pombe homolog of EB1, changes the microtubule lattice Mutations in a beta-tubulin disrupt spindle orientation and microtubule dynamics in the early Caenorhabditis elegans embryo CetZ tubulin-like proteins control archaeal cell shape Alanine-scanning mutagenesis of Aspergillus gamma-tubulin yields diverse and novel phenotypes Molecular basis for fungal selectivity of novel antimitotic compounds.Molecular cloning and characterization of Hymenolepis diminuta alpha-tubulin gene.Genome-wide analysis reveals novel and discrete functions for tubulin carboxy-terminal tails Stu1p is physically associated with beta-tubulin and is required for structural integrity of the mitotic spindle.Single site alpha-tubulin mutation affects astral microtubules and nuclear positioning during anaphase in Saccharomyces cerevisiae: possible role for palmitoylation of alpha-tubulin Microtubule assembly dynamics: an attractive target for anticancer drugs.Relating molecular flexibility to function: a case study of tubulin.α-Tubulin mutations alter oryzalin affinity and microtubule assembly properties to confer dinitroaniline resistance.Genome-wide synthetic lethal screens identify an interaction between the nuclear envelope protein, Apq12p, and the kinetochore in Saccharomyces cerevisiae.Replication-coupled chromatin assembly generates a neuronal bilateral asymmetry in C. elegans Dynamic microtubules are essential for efficient chromosome capture and biorientation in S. cerevisiae Mutations in alpha-tubulin confer dinitroaniline resistance at a cost to microtubule function.In vitro assembly and GTP hydrolysis by bacterial tubulins BtubA and BtubB.Differentiating between models of epothilone binding to microtubules using tubulin mutagenesis, cytotoxicity, and molecular modeling Conformational analysis of the carboxy-terminal tails of human beta-tubulin isotypes.An electron microscopy journey in the study of microtubule structure and dynamics.Meiosis-specific failure of cell cycle progression in fission yeast by mutation of a conserved beta-tubulin residue Secondary mutations correct fitness defects in Toxoplasma gondii with dinitroaniline resistance mutations ε-tubulin is essential in Tetrahymena thermophila for the assembly and stability of basal bodies.Carbendazim inhibits cancer cell proliferation by suppressing microtubule dynamics Porphyrins affect the self-assembly of tubulin in solution.Higher-order septin assembly is driven by GTP-promoted conformational changes: evidence from unbiased mutational analysis in Saccharomyces cerevisiae Microtubules as antifungal and antiparasitic drug targets.Mutations in genes of Saccharomyces cerevisiae encoding pre-mRNA splicing factors cause cell cycle arrest through activation of the spindle checkpoint.In silico design of tubulin-targeted antimitotic peptides.Interaction between a G-patch protein and a spliceosomal DEXD/H-box ATPase that is critical for splicing.Molecular analysis reveals localization of Saccharomyces cerevisiae protein kinase C to sites of polarized growth and Pkc1p targeting to the nucleus and mitotic spindle Structural differences between yeast and mammalian microtubules revealed by cryo-EM.Mutants of FtsZ targeting the protofilament interface: effects on cell division and GTPase activity Structure-function analysis of yeast tubulin.

P2860

Q24645360-FE89B328-4980-4CB3-BFDB-D15EC75D58D9 Q27678506-03919B71-B785-42C8-8BB7-66E1E69137C0 Q28469241-9776009A-B8A5-470E-84EE-E445B43EF9BE Q28775688-5727824A-0224-4E0E-B41B-1AC12953913D Q29143441-872B0A1B-EC8E-44E5-AF13-A141A4331566 Q30476871-A54BB5AF-8718-4D07-9D1B-35849422B0BB Q30484323-4AFA7B6A-CC31-4F00-B239-9424382F4242 Q30487651-849B7C8B-6CC4-4FFF-8DB1-5CC4622820B6 Q30630847-491CA327-EA41-41BD-8926-92CF11A53166 Q30856871-F6A72537-6D4B-4AA1-A657-C2B1866B5822 Q30951417-50728627-CB1B-4AA4-8365-38EB4F754FCB Q33278971-DF8DF5AA-04F2-48D0-808B-076A08806A14 Q33804686-AD77E5C4-80E7-4FD0-954E-2AB3D8301AD0 Q33898838-098420CF-8B12-487A-950E-E10689FEEF1E Q33946692-301CBBC0-03C5-4C6A-A192-93BC8B4CAF8E Q34010820-88488D0C-2422-48DB-8B37-ECCC52A4B06F Q34178409-27A9652B-304A-49AA-BFE6-D51693224C80 Q34432289-ACFC5659-7199-4D5B-BDB4-A66DB0FF1D96 Q34589608-F96C71FD-6A3A-4DAF-A90B-74D8F73FCBC8 Q35791458-54DF2CB5-884F-4D27-88A4-EB1319B6CA78 Q36118907-1BA1BB09-1D94-4A15-8376-0F5032A85FA2 Q36173890-22A9AD08-C788-4EB1-BB59-15CC590126A8 Q36321571-F5C93EDD-8B2B-4AC9-B5EB-44573978F443 Q36452372-D76CE7F6-F19A-425B-A0B6-D4B27E5BC15C Q36481467-AC1B7D1C-030F-4943-B72E-67DB1C44539D Q36749266-F833C3A5-AF0B-440B-8CBE-F5B1F61F67D7 Q36779921-7869B66F-16CB-4C1C-8C16-9A487F47448C Q36936842-8D5B6500-0CE3-4A76-8380-7A9BE73D3BC5 Q37061538-DE54968E-10E7-4870-8BB2-0D5349913E18 Q37192735-2CEFA626-8063-471C-A3FB-C9681EA618E4 Q37439896-FC5019D5-97DE-4E4C-BCE4-2BBE5FA30B71 Q37628781-67AE0041-47B5-4239-B931-E4CCFA848473 Q37825895-F08245DC-8EC9-4587-8A79-0111EEA64D0D Q39687193-1A293156-4E90-434E-8F29-C065929D687B Q39781566-A2907B52-95D1-42D3-834A-62E8F926D8C3 Q40419046-5FC6DF2E-33E1-45D4-877D-9F178D9D2877 Q40895683-FF492F9C-6883-4C87-8D49-FF468566E2F0 Q41597403-419F99A8-CEB3-4502-8F4D-0B6F8F0E5780 Q41762400-2262FF2E-9BE9-4B05-A90F-3306046916E4 Q42723218-0A4824F4-E48A-433B-9463-61951474AA35

P2860

Structure-function relationships in yeast tubulins.

http://www.wikidata.org/entity/Q34718050

description

2000 nî lūn-bûn

@nan

2000 թուականի Մայիսին հրատարակուած գիտական յօդուած

@hyw

2000 թվականի մայիսին հրատարակված գիտական հոդված

@hy

2000年の論文

@ja

2000年論文

@yue

2000年論文

@zh-hant

2000年論文

@zh-hk

2000年論文

@zh-mo

2000年論文

@zh-tw

2000年论文

@wuu

name

Structure-function relationships in yeast tubulins.

@ast

Structure-function relationships in yeast tubulins.

@en

Structure-function relationships in yeast tubulins.

@nl

type

label

Structure-function relationships in yeast tubulins.

@ast

Structure-function relationships in yeast tubulins.

@en

Structure-function relationships in yeast tubulins.

@nl

prefLabel

Structure-function relationships in yeast tubulins.

@ast

Structure-function relationships in yeast tubulins.

@en

Structure-function relationships in yeast tubulins.

@nl

P1433

Q34718050-31EAB94A-B381-40C7-BEAE-13F76B367285

P1476

Q34718050-0B3A97EA-2195-4C62-983C-566789D66573

P2093

Q34718050-7F81ADA9-D0C9-4E4D-AAC8-0B0F9127CA82

Q34718050-81D4A73E-AF28-48E5-B7FD-E86C3E36BB7E

Q34718050-A69B348E-3390-459B-91A1-31385E89C94D

Q34718050-B74E4109-DDB6-4081-97E4-5DEC404725F1

Q34718050-ED85739D-D051-4F2C-995A-D30FA84B238E

P2860

Q34718050-00FB0BA8-3C8C-4E34-B491-AC21C091C40A

Q34718050-0538BEC3-21D8-4505-88B3-A6AA2BE5E223

Q34718050-0980568F-9810-44B0-BBB0-BD04B333EE30

Q34718050-0A6D517F-2A5C-4ADA-86E2-76FC457F7C8D

Q34718050-0A9A6AC0-214D-494F-B452-26DCA17BE161

Q34718050-0B260E2B-47A2-4E51-8F68-0E0C540B0671

Q34718050-14A07033-043B-4C57-AAF0-E8DDC8173549

Q34718050-15F07C6A-0EF1-48D3-886C-22EDFDEB36F8

Q34718050-1739CED1-515F-416D-9B29-EF44EB488837

Q34718050-1C5DDD6C-F32E-419C-B0E8-33108C417CB5

P304

Q34718050-3A152D2B-D205-4415-AD0E-32B7A007A17B

P31

Q34718050-9151AEA0-0A7C-4C56-9429-5D2C9E83BF7E

P356

Q34718050-A52FC1B6-9519-4250-B7AA-E7F876ED4E14

P433

Q34718050-D943145D-6ADE-4E16-A9C3-02BD25361227

P478

Q34718050-A95165EA-63E1-4E0F-8BB4-00F1B83263F8

P50

Q34718050-423B8B21-0B7D-4AA2-AD1F-3217965D0E20

P577

Q34718050-606654AB-890C-4615-9304-F14F4C2264B0

P5875

Q34718050-E906C380-56E8-4BAB-BC86-14FED4CB72F7

P698

Q34718050-5B27C883-3563-4AAE-9163-8360B3E7D006

P932

Q34718050-D0B83DAF-2C81-4496-907D-0317C901657C

P356

P1433

Molecular Biology of the Cell

P1476

Structure-function relationships in yeast tubulins.

@en

P2093

E Nogales

http://www.w3.org/2001/XMLSchema#string

K H Downing

http://www.w3.org/2001/XMLSchema#string

K L Richards

http://www.w3.org/2001/XMLSchema#string

K R Anders

http://www.w3.org/2001/XMLSchema#string

K Schwartz

http://www.w3.org/2001/XMLSchema#string

P2860

Alf1p, a CLIP-170 domain-containing protein, is functionally and physically associated with alpha-tubulin

Structure of the alpha beta tubulin dimer by electron crystallography

SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling

Rapid and efficient site-specific mutagenesis without phenotypic selection

A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae

Genetically essential and nonessential alpha-tubulin genes specify functionally interchangeable proteins

Mitotic spindle positioning in Saccharomyces cerevisiae is accomplished by antagonistically acting microtubule motor proteins.

Defining protein interactions with yeast actin in vivo.

D-Erythroascorbic acid is an important antioxidant molecule in Saccharomyces cerevisiae.

Two functional alpha-tubulin genes of the yeast Saccharomyces cerevisiae encode divergent proteins.

P304

1887-1903

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1091/MBC.11.5.1887

http://www.w3.org/2001/XMLSchema#string

P433

5

http://www.w3.org/2001/XMLSchema#string

P478

11

http://www.w3.org/2001/XMLSchema#string

P50

P577

2000-05-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

12524534

http://www.w3.org/2001/XMLSchema#string

P698

10793159

http://www.w3.org/2001/XMLSchema#string

P932

14891

http://www.w3.org/2001/XMLSchema#string