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Journal ArticleDOI

Isolation and characterization of libraries of monoclonal antibodies directed against various forms of tubulin in Paramecium.

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TLDR
Analysis of tubulin heterogeneity in Paramecium through extensive isolation and characterization of monoclonal antibodies using various antigens and several immunization protocols and the results are discussed in terms of identification and accessibility of the epitopes and immunogenicity of ciliate tubulin with reference to mammalian and ciliate Tubulin sequences.
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This article is published in Biology of the Cell.The article was published on 1994-01-01. It has received 62 citations till now. The article focuses on the topics: Polyglycylation & Tubulin.

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Journal ArticleDOI

Polyglycylation of tubulin: a posttranslational modification in axonemal microtubules

TL;DR: A posttranslational modification was detected in the carboxyl-terminal region of axonemal tubulin from Paramecium, present in one of the most stable microtubular systems, may influence microtubule stability or axoneme function, or both.
Journal ArticleDOI

TTLL3 Is a Tubulin Glycine Ligase that Regulates the Assembly of Cilia

TL;DR: It is proposed that tubulin glycylation regulates the assembly and dynamics of axonemal microtubules and acts either directly or indirectly by inhibiting tubulin glutamylation.
Journal ArticleDOI

Axonemal tubulin polyglycylation probed with two monoclonal antibodies: widespread evolutionary distribution, appearance during spermatozoan maturation and possible function in motility

TL;DR: Two monoclonal antibodies, AXO 49 and TAP 952, are found to recognize differently tubulin polyglycylation, the most recently identified posttranslational modification discovered in Paramecium axonemal tubulin, and show that tubulinPolyglycylated tubulin is widely distributed in organisms ranging from ciliated protozoa to mammals.
Journal ArticleDOI

Kinesin-II Is Preferentially Targeted to Assembling Cilia and Is Required for Ciliogenesis and Normal Cytokinesis inTetrahymena

TL;DR: The cell division arrests observed in kinesin-II knockout cells appear to be induced by the loss of cilia and resulting cell paralysis.
Journal ArticleDOI

Polyglycylation of Tubulin Is Essential and Affects Cell Motility and Division in Tetrahymena thermophila

TL;DR: It is the total amount of polyglycylation on both α- and β-tubulin that is essential for survival, indicating the essential function of poly glycylation of the COOH terminus of β- Tubulin can be transferred to α-tubul.
References
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Journal ArticleDOI

Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

TL;DR: Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products.
Journal Article

Cleavage of structural proteins during the assemble of the head of bacterio-phage T4

U. K. Laemmli
- 01 Jan 1970 - 
TL;DR: Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products as mentioned in this paper.
Journal ArticleDOI

Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications.

TL;DR: A method has been devised for the electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets that results in quantitative transfer of ribosomal proteins from gels containing urea.
Journal ArticleDOI

Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis.

TL;DR: A rapid and convenient method for peptide mapping of proteins has been developed that involves partial enzymatic proteolysis in the presence of sodium dodecyl sulfate and analysis of the cleavage products by polyacrylamide gel electrophoresis.
Journal ArticleDOI

Ultrasensitive stain for proteins in polyacrylamide gels shows regional variation in cerebrospinal fluid proteins

TL;DR: A new silver stain for electrophoretically separated polypeptides can be rapidly and easily used and can detect as little as 0.01 nanogram of protein per square millimeter when employed with two-dimensional electrophoresis.
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