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629 Possible Causes for homodimer

  • Osteoporosis

    It is functional as a homodimer. The enzyme acts as a (lipid) membrane-bound ectophosphatase with PPi, PLP, and PEA as natural substrates. Abnormal gene product .[] Pathogenic variants may result in various consequences, sometimes cumulative: decrease or abolition of the catalytic activity; inability to form homodimers; sequestration[]

  • Paroxysmal Extreme Pain Disorder

    We have found that human prolidase, also known as peptidase D (PEPD) among several other names, binds to ErbB2 with high affinity (Kd 7 nM) and binds as a homodimer (493 amino[] The protein forms a homodimer that hydrolyzes dipeptides or tripeptides with C-terminal proline or hydroxyproline residues.[] […] as ErbB2 overexpression causes spontaneous dimerization, auto-tyrosine phosphorylation and recruitment and activation of downstream signals, PEPD rapidly binds to ErbB2 homodimers[]

  • Encephalopathy Episodic due to Thiamine Pyrophosphokinase Deficiency

    […] exists as a homodimer, which catalyzes the conversion of thiamine to thiamine pyrophosphate.[] […] thiamin pyrophosphokinase 1 From NCBI Gene : The protein encoded by this gene functions as a homodimer and catalyzes the conversion of thiamine to thiamine pyrophosphate,[] Introduction: Thiamin pyrophosphokinase 1 (TPK1) is a homodimer which catalyzes the phosphorylation of thiamine to thiamine pyrophosphate.[]

  • Hypophosphatasia

    The absence of active ALP production may be explained by the absence of a stable homodimer, while residual ALP activity may result from a deficit of functional homodimers.[] Missense mutations located in the catalytic site or in the homodimer interface were often shown by site-directed mutagenesis to have a dominant negative effect.[] In the light of our work, some particular regions of the protein appear as good candidates for further studies of GPI attachment and homodimer interactions.[]

  • Hereditary Coproporphyria

    Patients with HCP show KEYWORDS: coproporphyria; coproporphyrinogen oxidase; harderoporphyria; heterodimer; homodimer[] CPO Functions as a Homodimer. The dimensions of the dimer are 80 60 60 Å.[] Human CPO is a 76 kDa protein that is active as a homodimer in the mitochondrial intermembrane space ( 16 ).[]

  • Galactosemia

    The substitution probably disrupts both UDP-sugar binding and homodimer stability.[] The structure of the enzyme from Escherichia coli reveals a homodimer containing one zinc (II) and one iron (II) ion per subunit.[] Active site fluctuations were found to be correlated in enzyme with substrate bound to just one of the subunits in the homodimer suggesting inter-subunit communication.[]

  • Barth Syndrome

    None of the identified Taz1p complexes represents Taz1p homodimers.[] Thus, we conclude that yeast Taz1p does not form homodimers. Figure 2. Taz1p does not form homodimers.[] Taz1p Does Not Form Homodimers On the basis of migration as determined by 1D BN-PAGE, Brandner et al. (2005) suggested that Taz1p might assemble as a homodimer.[]

  • Mitochondrial Neurogastrointestinal Encephalomyopathy Type 4B

    , 25% variant homodimers, and 50% heterodimers.[] Description: Mitochondrial DNA polymerase is heterotrimeric, consisting of a homodimer of accessory subunits plus a catalytic subunit.[] Synonyms POLG1, POLGA Description DNA polymerase gamma, catalytic subunit (HGNC Symbol) Entrez gene summary Mitochondrial DNA polymerase is heterotrimeric, consisting of a homodimer[]

  • Tacrine

    The three most promising homodimers also showed a good inhibitory activity towards amyloid-β self aggregation.[] In particular, its homodimer bis(7)tacrine represents an interesting lead compound to design novel MTDLs.[] New tacrine derivatives 5a-d, 6a-d with piperazino-ethyl spacer linked with corresponding secondary amines and tacrine homodimer 8 were synthesized and tested as cholinesterase[]

  • ALK+ Histiocytosis

    Under physiological conditions, ALK monomers associate to homodimers upon ligand binding only, but this regulatory mechanism is disabled when its C-terminal residues are replaced[] In all these proliferations, the formation of X-ALK homodimers/polymers using dimerization sites at the N-terminus of ALK partners mimics ligand binding, and is responsible[]

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