Pubmed abstracts for Protein-Protein Interaction search result :

Interacting proteins: P50402 and P02545	Pubmed	SVM Score :0.82788949
Mutations within LMNA , encoding A type nuclear lamins , are associated with multiple tissue specific diseases , including Emery Dreifuss ( EDMD2 / 3 ) and Limb Girdle muscular dystrophy ( LGMD1B ) . 10 linked EDMD results from mutations in emerin , a lamin A associated protein . 0.82788949^^^
Interacting proteins: P50402 and P02545	Pubmed	SVM Score :0.0
Equally remarkably , the disease is caused by mutations in widely expressed genes for the nuclear membrane / lamina proteins , emerin and lamin A / C . ^^^
Interacting proteins: P50402 and P02545	Pubmed	SVM Score :0.0
During early reassembly of the nuclear envelope at this mitotic stage emerin colocalizes with lamin A / C but not with lamin B and LAP 2 proteins . ^^^
Interacting proteins: P50402 and P02545	Pubmed	SVM Score :0.0
There is a growing body of evidence in favour of the presence of human diseases caused by mutations in genes that encode the nuclear envelope proteins emerin and lamin A / C ( lamin A and C are alternatively spliced variants of the same gene ) . ^^^ In the targeted mouse model of lamin A gene deficiency , loss of lamin A / C is associated with mislocalization of emerin . ^^^
Interacting proteins: P50402 and P02545	Pubmed	SVM Score :0.0
To compound things further , the 10 linked and dominant forms of Emery Dreifuss muscular dystrophy have recently been linked to emerin and lamin A / C , respectively , two proteins of the nuclear membrane , opening up yet another new ballpark of discovery . . ^^^
Interacting proteins: P50402 and P02545	Pubmed	SVM Score :0.0
Thus lamin A / C is , besides emerin , the first known nucleophilic protein which plays a role in human disease . ^^^
Interacting proteins: P50402 and P02545	Pubmed	SVM Score :0.0
Lamin A / C , lamin B 1 , LAP 2 , emerin , and nuclear pores all extend throughout the grooves and intranuclear inclusions of PTC . ^^^
Interacting proteins: P50402 and P02545	Pubmed	SVM Score :0.0
The results show that the loss of function of R 482 in lamin A / C in FPLD does not involve loss of ability to form a nuclear lamina or to interact with the nuclear membrane protein , emerin . . ^^^
Interacting proteins: P50402 and P02545	Pubmed	SVM Score :0.0
The 10 linked form of EDMD is caused by mutations in the emerin gene , whereas autosomal dominant EDMD is caused by mutations in the lamin A / C gene . ^^^ Emerin colocalizes with lamin A / C in interphase cells , and binds in vitro to lamin A / C . ^^^ Recent work suggests that lamin A / C might serve as a receptor for emerin . ^^^ We have undertaken a structural analysis of emerin , and in particular of its N terminal domain , which is comprised in the emerin segment critical for binding to lamin A / C . ^^^
Interacting proteins: P50402 and P02545	Pubmed	SVM Score :0.0
Mutations in the STA gene , encoding the nuclear envelope protein emerin , are responsible for 10 linked EDMD , while mutations in the LMNA gene encoding lamins A and C by alternative splicing have been found in patients with autosomal dominant , autosomal recessive , and sporadic forms of EDMD . ^^^
Interacting proteins: P50402 and P02545	Pubmed	SVM Score :0.0
We have used Western blots to detect emerin and lamin A / C in left ventricles from both nondiseased and failing DCM samples . ^^^
Interacting proteins: P50402 and P02545	Pubmed	SVM Score :0.0
The distributions of endogenous lamin A / C , lamin B 1 and lamin B 2 were also altered in cells expressing these four mutants and three of them caused a loss of emerin from the nuclear envelope . ^^^
Interacting proteins: P50402 and P02545	Pubmed	SVM Score :0.0
Interestingly the inner nuclear membrane protein emerin , thought to be a ligand of lamin A / C , is also a nonessential protein in tissue culture cells . . ^^^
Interacting proteins: P50402 and P02545	Pubmed	SVM Score :0.0
Mutations in the genes encoding the inner nuclear membrane proteins lamin A / C and emerin produce cardiomyopathy and muscular dystrophy in humans and mice . ^^^ In mature muscle , myne 1 and lamin A / C are perfectly colocalized , although colocalization with emerin is only partial . ^^^
Interacting proteins: P50402 and P02545	Pubmed	SVM Score :0.0
Thereafter , by examining the intracellular localisation of endogenously expressed lamin A / C and exogenously expressed wild type and mutant forms of emerin after a number of cell divisions , we determined that the mutant forms of emerin redistributed endogenous lamin A / C . ^^^ The extent of lamin A / C redistribution correlated with the amount of EGFP emerin that was mislocalised . ^^^ The nuclear morphology and redistribution of lamin A / C was most severely affected in the cells expressing the emerin mutant Del 236 241 . ^^^ The data presented here show that lamin A / C localisation is dominantly directed by its interaction with certain emerin mutants and perhaps wild type emerin as well . ^^^
Interacting proteins: P50402 and P02545	Pubmed	SVM Score :0.0
Seven other patients , four with the 10 linked form of Emery Dreifuss muscular dystrophy ( EDMD ) and three with an Emery Dreifuss like phenotype but no detectable mutations in either the emerin or the lamin A / C gene were also scanned as disease controls . ^^^
Interacting proteins: P50402 and P02545	Pubmed	SVM Score :0.0
Elucidation of the pathophysiology of Emery Dreifuss muscular dystrophy , caused by mutations in emerin or lamin A / C , will require deciphering the role of these proteins in the functional organization of the nuclear envelope . ^^^ Both emerin and lamin A / C interact with nuclear actin , a component of the chromatin remodeling complex associated with the nuclear matrix , suggesting that either chromatin arrangement , or gene transcription , or both , might be impaired in the disease . . ^^^
Interacting proteins: P50402 and P02545	Pubmed	SVM Score :0.0
Both emerin and lamin A / C are located in the inner surface membrane of the nucleus . ^^^
Interacting proteins: P50402 and P02545	Pubmed	SVM Score :0.0
Mutations of emerin gene cause the Emery Dreifuss muscular dystrophy , a neuromuscular disorder also linked to mutations of lamin A / C . ^^^ We demonstrate that emerin and lamin A / C are bound to actin at the late stages of myotube differentiation and in mature muscle . ^^^ On the other hand , active protein phosphatase 1 , a serine threonine phosphatase known to associate with lamin A / C , inhibits emerin actin interaction in myotube extracts . ^^^
Interacting proteins: P50402 and P02545	Pubmed	SVM Score :0.0
Mutations in two nuclear envelope associated proteins , emerin and lamin A / C cause the Emery Dreifuss muscular dystrophy ; the cellular pathology associated with the disease and the functional role of emerin and lamin A / C in muscle cells are not well established . ^^^ Moreover , chromatin remodeling complexes trigger gene expression by utilizing the nuclear matrix associated actin , which is known to interact with both emerin and lamin A / C . ^^^
Interacting proteins: P50402 and P02545	Pubmed	SVM Score :0.0
In recent years , several proteins from the sarcolemmal muscle membrane ( dystrophin , sarcoglycans , dysferlin , caveolin 3 ) , from the extracellular matrix ( alpha 2 laminin , collagen 6 ) , from the sarcomere ( telethonin , myotilin , titin , nebulin ) , from the muscle cytosol ( calpain 3 , TRIM 32 ) , from the nucleus ( emerin , lamin A / C , survival motor neuron protein ) , and from the glycosylation pathway ( fukutin , fukutin related protein ) have been identified . ^^^
Interacting proteins: P50402 and P02545	Pubmed	SVM Score :0.0
Emerin is a nuclear membrane protein that interacts with lamin A / C at the nuclear envelope . ^^^ Mutations in either emerin or lamin A / C cause Emery Dreifuss muscular dystrophy ( EDMD ) . ^^^
Interacting proteins: P50402 and P02545	Pubmed	SVM Score :0.0
The novel hypothesis suggested by the data is that EDMD / CMD1A mutations in the tail domain of lamin A / C work by direct impairment of emerin interaction , whereas mutations in the rod region cause defective lamina assembly that might or might not impair emerin capture at the nuclear rim . ^^^ Subtle effects on the function of the lamina emerin complex in EDMD / CMD1A patients might be responsible for the skeletal and / or cardiac muscle phenotype . . ^^^ Using transfection of lamin A / C deficient fibroblasts , we have studied the effects of nine pathogenic mutations on the ability of lamin A to assemble normally and to localize emerin normally at the nuclear rim . ^^^
Interacting proteins: P50402 and P02545	Pubmed	SVM Score :0.0
However , mutations in two nuclear proteins emerin and lamin A / C have also been demonstrated to give rise to a muscular dystrophy phenotype . ^^^
Interacting proteins: P50402 and P02545	Pubmed	SVM Score :0.0
Failure of lamin A / C to functionally assemble in R482L mutated familial partial lipodystrophy fibroblasts : altered intermolecular interaction with emerin and implications for gene transcription . ^^^ In addition , emerin did not colocalize with nuclear lamin A / C aggregates . ^^^
Interacting proteins: P50402 and P02545	Pubmed	SVM Score :0.0
Although conventional fluorescence microscope revealed no discernible abnormality in the distribution of emerin and lamin A / C , a serial multi layer scanning with confocal laser scanning microscope showed an attenuated and uneven distribution of lamin A / C . ^^^
Interacting proteins: P50402 and P02545	Pubmed	SVM Score :0.0
Following the immunocytochemical examination the decrease of lamin A / C in 10 EDMD and of emerin in AD EDMD was also observed . ^^^
Interacting proteins: P50402 and P02545	Pubmed	SVM Score :0.0
The downstream effect of lamin A / C silencing was investigated by immunocytochemical analysis of the cellular localization of the protein , emerin , an important component of the nuclear lamina and known to be regulated by lamin expression . ^^^ Marked displacement of emerin from the nuclear lamina to the cytoplasm was observed when lamin A / C was silenced in human endometrial stromal cells , confirming functional silencing of lamin A / C resulting in a nuclear lamina assembly defect . ^^^
Interacting proteins: P50402 and P02545	Pubmed	SVM Score :0.0
In SW 13 cells , which lack lamin A / C , nesprin 2 epitopes and emerin were both mislocalized and formed aggregates in the endoplasmic reticulum ( ER ) . ^^^
Interacting proteins: P50402 and P02545	Pubmed	SVM Score :0.0
A molecular complex in muscle cells formed by lamin A / C , emerin , and nuclear actin has been identified . ^^^
Interacting proteins: P50402 and P02545	Pubmed	SVM Score :0.0
Studies of the consequences of LMNA mutations in the skin cultured fibroblasts from the patients reveal abnormal nuclei in variable proportions , with dysmorphic nuclei exhibiting abnormal patterns of expression of B type lamins and emerin . ^^^
Interacting proteins: P50402 and P02545	Pubmed	SVM Score :0.0
To date , mutations in the genes encoding the nuclear envelope proteins emerin , MAN 1 , lamin A / C , and lamin B receptor were found to cause nuclear envelopathies . ^^^
Interacting proteins: P50402 and P02545	Pubmed	SVM Score :0.0
The causative mutation is either in the emerin gene ( 10 linked recessive EDMD ) or lamin A / C gene ( autosomal dominant EDMD 2 or LGMD1B ) . ^^^
Interacting proteins: P50402 and P02545	Pubmed	SVM Score :0.0
Using biochemical techniques , we demonstrate that Nesprin 2 binds directly to emerin and the C terminal common region of lamin A / C . ^^^
Interacting proteins: P50402 and P02545	Pubmed	SVM Score :0.0
Most of them are due to mutations in the lamin A / C gene , one to mutations in emerin gene , some are associated with mutations in Lamin B receptor gene . ^^^
Interacting proteins: P50402 and P02545	Pubmed	SVM Score :0.0
These novel skeletal muscle genes encode highly diverse proteins with different localization within or at the surface of the skeletal muscle fibre , such as the sarcolemmal muscle membrane ( dystrophin , sarcoglycans , dysferlin , caveolin 3 ) , the extracellular matrix ( alpha 2 laminin , collagen 6 ) , the sarcomere ( telethonin , myotilin , titin , nebulin and ZASP ) , the muscle cytosol ( calpain 3 , TRIM 32 ) , the nucleus ( emerin , lamin A / C ) and the glycosilation pathway enzymes ( fukutin and fukutin related proteins ) . ^^^
Interacting proteins: P50402 and P02545	Pubmed	SVM Score :0.0
Emery Dreifuss muscular dystrophy can be caused by mutations in the nuclear envelope proteins lamin A / C and emerin . ^^^
Interacting proteins: P50402 and P02545	Pubmed	SVM Score :0.0
Mutations in the GNE , dysferlin , caveolin 3 , emerin , and lamin A / C genes were excluded . ^^^
Interacting proteins: P50402 and P02545	Pubmed	SVM Score :0.0
Additionally , 3T3 L 1 pre adipocytes with stable reduction of lamin A / C or emerin were derived . ^^^
Interacting proteins: P50402 and P02545	Pubmed	SVM Score :0.0
These data identify specific functional roles for the emerin lamin C and emerin lamin A containing protein complexes and is the first report to suggest that the A type lamin mutations may be differentially dysfunctional for the same LMNA mutation . . ^^^
Interacting proteins: P50402 and P02545	Pubmed	SVM Score :0.0
Emery Dreifuss muscular dystrophy ( EDMD 1 ) is caused by mutations in either the 10 linked gene emerin ( EMD ) or the autosomal lamin A / C ( LMNA ) gene . ^^^
Interacting proteins: P50402 and P02545	Pubmed	SVM Score :0.0
We show that emerin and MAN 1 , but not LBR , are more mobile in the inner nuclear membrane of cells from Lmna / mice than in cells from wild type mice . ^^^
Interacting proteins: P50402 and P02545	Pubmed	SVM Score :0.0
EDMD is also caused by 10 linked recessive loss of function mutations of emerin , another component of the inner nuclear lamina that directly interacts with LMNA . ^^^ One model for disease pathogenesis of LMNA and emerin mutations is cell specific perturbations of the mRNA transcriptome in terminally differentiated cells . ^^^ To test this model , we studied 125 human muscle biopsies from 13 diagnostic groups ( 125 U133A , 125 U133B microarrays ) , including EDMD patients with LMNA and emerin mutations . ^^^ This showed that the two nuclear envelope defects ( EDMD LMNA , EDMD emerin ) were highly related disorders and were also related to fascioscapulohumeral muscular dystrophy ( FSHD ) . ^^^ To identify disease specific transcripts for EDMD , we applied a leave one out ( LOO ) cross validation approach using LMNA patient muscle as a test data set , with reverse transcription polymerase chain reaction ( RT PCR ) validations in both LMNA and emerin patient muscle . ^^^
Interacting proteins: P50402 and P02545	Pubmed	SVM Score :0.0
The physiologic rationale for the existence of the 2 different Lmna products lamin A and lamin C is unclear , although several reports have suggested that lamin A may have particularly important functions , for example in the targeting of emerin and lamin C to the nuclear envelope . ^^^ Lmna ( LCO / LCO ) mice were entirely healthy , and Lmna ( LCO / LCO ) cells displayed normal emerin targeting and exhibited only very minimal alterations in nuclear shape and nuclear deformability . ^^^
Interacting proteins: P50402 and P02545	Pubmed	SVM Score :0.0
Here we report evidence indicating that pre lamin A is mis localized in the nuclei of Emery Dreifuss muscular dystrophy fibroblasts , either bearing lamin A / C or emerin mutations . ^^^
Interacting proteins: P50402 and P02545	Pubmed	SVM Score :0.0
The mutated protein was not properly localized at the inner nuclear membrane and the emerin protein , which interacts with lamin A / C , was also aberrantly distributed . ^^^
Interacting proteins: P50402 and P02545	Pubmed	SVM Score :0.0
Emery Dreifuss muscular dystrophy results from mutations in either emerin or lamin A / C and is caused by loss of some unknown function of emerin lamin A / C complexes . ^^^
Interacting proteins: P50402 and P02545	Pubmed	SVM Score :0.0
We found that in IBM muscle vacuoles were immunoreactive for the inner nuclear membrane proteins emerin and lamin A / C . ^^^
Interacting proteins: P50402 and P02545	Pubmed	SVM Score :0.0
We recently identified LMNA encoding two nuclear envelope proteins , lamins A and C , to be implicated in the autosomal dominant form of EDMD . ^^^ Here , we report on the variability of the phenotype and spectrum of LMNA mutations in 53 autosomal dominant EDMD patients ( 36 members of 6 families and 17 sporadic cases ) . ^^^ Moreover , a marked inter and intra familial variability in the clinical expression of LMNA mutations exists , ranging from patients expressing the full clinical picture of EDMD to those characterized only by cardiac involvement , which points toward a significant role of possible modifier genes in the course of this disease . ^^^ In conclusion , the high proportion of de novo mutations together with the large spectrum of both LMNA mutations and the expression of the disease should now prompt screening for LMNA in familial and sporadic cases of both EDMD and dilated cardiomyopathy associated with conduction system disease . . ^^^
Interacting proteins: P50402 and P02545	Pubmed	SVM Score :0.0
Mutations in the lamin A ( LMNA ) gene are associated with the tissue specific diseases Emery Dreifuss muscular dystrophy ( EDMD ) , limb girdle muscular dystrophy ( LGMD 1B ) , dilated cardiomyopathy with conduction system disease ( DCM CD ) , and Dunnigan ' s familial partial lipodystrophy ( FPLD ) . ^^^
Interacting proteins: P50402 and P02545	Pubmed	SVM Score :0.0
Lamin A / C mutations also cause one form of dilated cardiomyopathy ( CMD1A ) and one form of limb girdle muscular dystrophy ( LGMD1B ) , both of which have clinical features in common with EDMD , as well as a rare , unrelated form of lipodystrophy ( FPLD ) . ^^^ Lamin A / C mutations also cause one form of dilated cardiomyopathy ( CMD1A ) and one form of limb girdle muscular dystrophy ( LGMD1B ) , both of which have clinical features in common with EDMD , as well as a rare , unrelated form of lipodystrophy ( FPLD ) . ^^^
Interacting proteins: P50402 and P02545	Pubmed	SVM Score :0.0
Further 50 mostly missense mutations in LMNA result in autosomal dominant EDMD , autosomal recessive EDMD , LGMD1B , DCM CD , FPLD , or CMT2B . ^^^ Phenotypically , they present as Emery Dreifuss muscular dystrophy ( EDMD ) , limb girdle muscle dystrophy 1B ( LGMD1B ) , or dilated cardiomyopathy with conduction defects ( DCM CD ) . ^^^
Interacting proteins: P50402 and P02545	Pubmed	SVM Score :0.0
Interestingly , the lamin A / C binding protein LAP2alpha was also mislocalized in 10 EDMD fibroblasts . . ^^^
Interacting proteins: P50402 and P02545	Pubmed	SVM Score :0.0
Autosomal dominantly inherited missense mutations in lamins A and C cause familial partial lipodystrophy of the Dunnigan type ( FPLD ) , and myopathies including Emery Dreifuss muscular dystrophy ( EDMD ) . ^^^ While mutations responsible for FPLD are restricted to the carboxyl terminal tails , those responsible for EDMD are spread throughout the molecules . ^^^ We observed here the same structural abnormalities in the nuclear envelope and chromatin of fibroblasts from patients with FPLD and EDMD , harboring missense mutations at codons 482 and 453 , respectively . ^^^ Transfected cells therefore develop similar phenotypes when expressing lamins mutated in the carboxyl terminal tail at sites responsible for FPLD or EDMD . . ^^^
Interacting proteins: P50402 and P02545	Pubmed	SVM Score :0.0
Patients with the autosomal dominant form of Emery Dreifuss muscular dystrophy ( EDMD ) or familial partial lipodystrophy ( FPLD ) have specific mutations in the lamin A gene . ^^^ Three such point mutations , G465D ( FPLD ) , R482L , ( FPLD ) , or R527P ( EDMD ) , were introduced by site specific mutagenesis in the C terminal tail domain of a FLAG tagged full length lamin A construct . ^^^
Interacting proteins: P50402 and P02545	Pubmed	SVM Score :0.0
Aim of the present study was to investigate the spectrum of cardiac disease in patients with an initial diagnosis of EDMD caused by a mutation in the LMNA gene . ^^^ METHODS AND RESULTS : Ten consecutive patients with EDMD and a LMNA gene mutation were evaluated with structured medical interview , physical examination , ECG , echocardiogram and 24 h Holter monitoring . ^^^ CONCLUSIONS : Cardiac disease is common in patients with an initial diagnosis of EDMD caused by a mutation in the LMNA gene and consists of arrhythmias , disorders of atrioventricular conduction , cardiomyopathies and sudden death despite pacemaker implant . . ^^^
Interacting proteins: P50402 and P02545	Pubmed	SVM Score :0.0
Autosomal dominantly inherited missense mutations in lamins A and C cause several tissue specific diseases , including Emery Dreifuss muscular dystrophy ( EDMD ) and Dunnigan type familial partial lipodystrophy ( FPLD ) . ^^^ Since clones mutated at arginine 482 ( a site responsible for FPLD ) differentiate normally , we conclude that C2C12 clones expressing R453W mutated lamin A represent a good cellular model to study the pathophysiology of EDMD . ^^^
Interacting proteins: P50402 and P02545	Pubmed	SVM Score :0.0
BACKGROUND : The autosomal dominant form of Emery Dreifuss muscular dystrophy ( AD EDMD ) is caused by mutations in the gene encoding for the lamins A and C ( LMNA ) . ^^^
Interacting proteins: P50402 and P02545	Pubmed	SVM Score :0.0
Typical features of the cardiac involvement of EDMD are presented , caused by a novel missense mutation in the splice receptor sequence of intron 6 of the LMNA gene on chromosome 1 , encoding for the lamin A / C gene , consistent with the autosomal dominant form of EDMD . . ^^^
Interacting proteins: P50402 and P02545	Pubmed	SVM Score :0.0
In search of a structural cause for the variety of inherited diseases caused by A type lamin mutations , we have studied the molecular organization of GFP tagged lamin A and lamin C mutants R453W and R386K , found in Emery Dreifuss muscular dystrophy ( EDMD ) , and lamin A and lamin C mutant R482W , found in patients with Dunnigan type familial partial lipodystrophy ( FPLD ) . ^^^
Interacting proteins: P50402 and P02545	Pubmed	SVM Score :0.0
Mutations of the LMNA gene , encoding the nuclear envelope proteins lamins A and C , give rise to Emery Dreifuss muscular dystrophy and to limb girdle muscular dystrophy 1B ( EDMD and LGMD1B ) . ^^^ With one exception , all the reported EDMD and LGMD1B mutations are confined to the first 10 exons of the gene . ^^^
Interacting proteins: P50402 and P02545	Pubmed	SVM Score :0.0
Previous histological findings , physiological data , and behavioral observations on the A type lamin knockout mouse ( Lmna ( / ) ) suggest that important aspects of this model resemble the human Emery Dreifuss muscular dystrophy ( EDMD ) phenotype . ^^^ These ECG changes resemble some aspects of the ECG records from humans with EDMD ; however , the cardiac phenotype in this Lmna ( / ) mouse model appears to be less well defined / developed . ^^^ In summary , tissues from the Lmna ( / ) mouse exhibit a number of skeletal and cardiac muscle deficiencies , some of which are similar to those which have been reported in studies of human EDMD . . ^^^
Interacting proteins: P50402 and P02545	Pubmed	SVM Score :0.0
Lamin A / C is a major component of nuclear lamina , and its gene mutations cause several human disorders including muscular dystrophy , cardiomyopathy , lipodystrophy , neuropathy , and progeria syndrome . 10 linked recessive form of EDMD is caused by mutation in EMD ( or STA ) gene encoding an integral protein of the inner nuclear membrane . ^^^
Interacting proteins: P50402 and P02545	Pubmed	SVM Score :0.0
This review focuses on laminopathies affecting the striated muscle tissue only , namely Emery Dreifuss muscular dystrophy ( EDMD ) , limb girdle muscular dystrophy type 1B ( LGMD1B ) and dilated cardiomyopathy with conduction defects ( DCM CD ) . ^^^
Interacting proteins: P50402 and P02545	Pubmed	SVM Score :0.0
As these resemble the cardiac features of patients with the autosomal dominant variant of EDMD , we examined the lamin A / C gene , identifying a de novo mutation in the propositus . ^^^
Interacting proteins: P50402 and P02545	Pubmed	SVM Score :0.0
Mutations in LMNA , which encodes nuclear lamins A and C , cause a broad range of diseases , including autosomal dominant Emery Dreifuss muscular dystrophy ( EDMD ) and related disorders with a predominant cardiomyopathy . ^^^
Interacting proteins: P50402 and P02545	Pubmed	SVM Score :0.0
The distribution of the mutations in AD EMD patients ( in the tail and in the 2A rod domain ) suggests that unique interactions between lamin A / C and other nuclear components exist that have an important role in cardiac and skeletal muscle function . . ^^^ We report here that heterozygote mutations in LMNA , the gene for AD EMD , may cause diverse phenotypes ranging from typical EMD to no phenotypic effect . ^^^
Interacting proteins: P50402 and P02545	Pubmed	SVM Score :0.0
Two main types of inheritance have been described : the 10 linked form is caused by mutations in the STA gene on locus Xq 28 and the gene for the autosomal dominant form ( LMNA gene ) has been localized on chromosome 1q11 q 23 . ^^^
Interacting proteins: P50402 and P02545	Pubmed	SVM Score :0.0
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Interacting proteins: P50402 and P02545	Pubmed	SVM Score :0.0
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