Evidence map›Paper›PMID 20453917›Full record

ReviewBiochemistry and cell biology = Biochimie et biologie cellulaire2010

Fuzzy complexes of myelin basic protein: NMR spectroscopic investigations of a polymorphic organizational linker of the central nervous system.

David S Libich, Mumdooh A M Ahmed, Ligang Zhong, Vladimir V Bamm, Vladimir Ladizhansky, George Harauz

Abstract readReview
In one paragraph

Review in Biochemistry and cell biology = Biochimie et biologie cellulaire, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.6field-weighted citation impact, top 11% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

15 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
  2. Article
  3. Mapping the deformability of natural and designed cellulosomes in solution.Biotechnology for biofuels and bioproducts · 2022
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 1 institution in 2 countries.

David S LibichCentre for Structural Biology, Institute of Fundamental Sciences, Department of Physics, Massey University, Palmerston North, New Zealand. d.s.libich@massey.ac.nz
Mumdooh A M Ahmed
Ligang Zhong
Vladimir V Bamm
Vladimir Ladizhansky
George Harauz
Massey University · NZ

Funding

CIHR 74468CIHR MOP74468
6 · The paper itself

Abstract

The classic 18.5 kDa isoform of myelin basic protein (MBP) is central to maintaining the structural homeostasis of the myelin sheath of the central nervous system. It is an intrinsically disordered, promiscuous, multifunctional, peripheral membrane protein, whose conformation adapts to its particular environment. Its study requires the selective and complementary application of diverse approaches, of which solution and solid-state NMR spectroscopy are the most powerful to elucidate site-specific features. We review here several recent solution and solid-state NMR spectroscopic studies of 18.5 kDa MBP, and the induced partial disorder-to-order transitions that it has been demonstrated to undergo when complexed with calmodulin, actin, and phospholipid membranes.

Indexed as

AnimalsCentral Nervous SystemHumansMagnetic Resonance SpectroscopyMyelin Basic ProteinProtein ConformationProtein IsoformsMyelin Basic ProteinProtein Isoforms

Identifiers

PMID20453917
PMCPMC3517781
OpenAlexW650820457

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.