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August 17, 1992FEBS LettersOpen Access

Glycoprotein‐binding site of dystrophin is confined to the cysteine‐rich domain and the first half of the carboxy‐terminal domain

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Population

Dystrophin protein and glycoprotein complex (biochemical model)

Design

Preclinical

Authors

ASAtsushi SuzukiHiroshima UniversityMYMikiharu YoshidaNational Center of Neurology and PsychiatryHYHideko YamamotoTokyo Institute of Psychiatry

Discussion

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Implication

May guide DMD mutation analysis; leaves open therapeutic targeting pending human validation.

Structured PICO

P
Population
Dystrophin protein and glycoprotein complex (biochemical model)
I
Intervention
Biochemical analysis of dystrophin binding sites
O
Outcome
Identification of the glycoprotein-binding site of dystrophinsurrogate

The study identifies the specific glycoprotein-binding site on dystrophin, providing a molecular basis for severe phenotypes in Duchenne muscular dystrophy when this region is missing.

Cite This Study

Suzuki et al. (1992) studied this question.

synapsesocial.com/papers/6a1017bd8090e499da609ae7https://doi.org/10.1016/0014-5793(92)81265-n
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Also Consider

Synapse has enriched 4 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1Are cysteine-rich and COOH-terminal domains of dystrophin critical for sarcolemmal localization?1992 · 48 citations
  2. 2Detailed analysis of the repeat domain of dystrophin reveals four potential hinge segments that may confer flexibility.1990 · 400 citations
  3. 3Is the carboxyl‐terminus of dystrophin required for membrane association? A novel, severe case of duchenne muscular dystrophy1991 · 87 citations
  4. 4Glycoprotein Complex Anchoring Dystrophin to Sarcolemma11990 · 503 citations