Intrinsically disordered protein from a pathogenic mesophile Mycobacterium tuberculosis adopts structured conformation at high temperature

scientific article published in May 2008

Intrinsically disordered protein from a pathogenic mesophile Mycobacterium tuberculosis adopts structured conformation at high temperature is …
instance of (P31):
scholarly articleQ13442814

External links are
P356DOI10.1002/PROT.21798
P698PubMed publication ID18004752

P50authorSouvik MaitiQ18217615
P2093author name stringSrinivasan Ramachandran
Sanjiv Kumar
Uma Chaudhry
Niti Kumar
Anju Suryawanshi
Swati Shukla
P2860cites workMassive gene decay in the leprosy bacillusQ22122381
Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequenceQ22122411
Pyruvate carboxylase from Mycobacterium smegmatis: stabilization, rapid purification, molecular and biochemical characterization and regulation of the cellular level.Q30889482
Spectrofluorimetric assessment of the surface hydrophobicity of proteinsQ42792990
Alzheimer's disease in Down's syndrome: clinicopathologic studiesQ43697583
P433issue3
P407language of work or nameEnglishQ1860
P921main subjectMycobacterium tuberculosisQ130971
P304page(s)1123-1133
P577publication date2008-05-01
P1433published inProteinsQ7251514
P1476titleIntrinsically disordered protein from a pathogenic mesophile Mycobacterium tuberculosis adopts structured conformation at high temperature
P478volume71

Reverse relations

cites work (P2860)
Q42796919Allotment of carbon is responsible for disorders in proteins
Q86275590Effect of temperature on the conformation of natively unfolded protein 4E-BP1 in aqueous and mixed solutions containing trifluoroethanol and hexafluoroisopropanol
Q37891686Novel Strategies for Drug Discovery Based on Intrinsically Disordered Proteins (IDPs)
Q42170092Phytolacca americana lectin (Pa-2; pokeweed mitogen): an intrinsically unordered protein and its conversion into partial order at low pH.
Q47401954Structural disorder and induced folding within two cereal, ABA stress and ripening (ASR) proteins.
Q41925625The Henipavirus V protein is a prevalently unfolded protein with a zinc-finger domain involved in binding to DDB1.
Q33811264Thermostability in endoglucanases is fold-specific

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