DMD | ENSG00000198947 | NCBI 1756

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this specific cell.

Network Configuration

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Pathway Categories (for ONTOLOGY source):

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Node Color (Target Cell CSI, relative to current network):
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Other Information

This section provides additional information about the gene, including a description generated by an AI language model and details about associated proteins.

Description
Proteins

## Summary [DMD](/details-gene/1756) encodes dystrophin, a large, rod-shaped cytoskeletal protein essential for providing structural stability to the cell membrane, particularly in muscle fibers. It is a critical component of the dystrophin-associated glycoprotein complex (DGC), which links the internal actin cytoskeleton to the extracellular matrix, protecting cells from mechanical stress. Mutations in the [DMD](/details-gene/1756) gene are the cause of Duchenne Muscular Dystrophy ([153245](https://omim.org/entry/153245), [310200](https://omim.org/entry/310200)) and the milder Becker Muscular Dystrophy ([300377](https://omim.org/entry/300377)), both X-linked recessive disorders characterized by progressive muscle weakness and degeneration. While classically known for its role in muscle, expression data reveals significant roles in a diverse range of non-muscle cells, particularly within the central nervous system, including multiple subtypes of cortical interneurons and glial cells, as well as in [adipocytes](/details-cell/CL0000136), suggesting a broader function in cellular architecture and signaling than historically appreciated. ## Cellular Roles and Expression Landscape The expression profile of [DMD](/details-gene/1756) underscores its dual importance in both muscle and nervous tissues. **Overall**, it shows high significance in [cardiac muscle cells](/details-cell/CL0000746), consistent with its canonical function in muscle integrity. However, the most prominent significance is observed in the central nervous system and other non-muscle cell types. The gene is a highly significant marker in several classes of inhibitory neurons, including [sst GABAergic cortical interneurons](/details-cell/CL4023017), [VIP GABAergic cortical interneurons](/details-cell/CL4023016), and [pvalb GABAergic cortical interneurons](/details-cell/CL4023018). This strong expression in distinct neuronal populations suggests a crucial role in synaptic structure and function, a finding supported by research identifying specific brain-expressed isoforms of dystrophin ([Link](https://pubmed.ncbi.nlm.nih.gov/1319059/)). Furthermore, [DMD](/details-gene/1756) is also highly significant in glial cells such as [Bergmann glial cells](/details-cell/CL0000644) and [oligodendrocyte precursor cells](/details-cell/CL0002453), implying a function in maintaining the structural scaffolding and homeostasis of the nervous system. Unexpectedly, the highest significance score for [DMD](/details-gene/1756) is observed in [adipocytes](/details-cell/CL0000136), suggesting a previously underappreciated role in adipose tissue. This may relate to mechanosensing or maintaining structural integrity in cells that undergo significant volume changes. The broad cellular landscape highlights that while its absence is most catastrophic in muscle, its function extends to many other tissues where mechanical stability and cytoskeletal organization are paramount. ## Pathways and Molecular Function The molecular functions of dystrophin are centered on its role as a structural linker protein. It is a key component of the '[Dystrophin-associated glycoprotein complex](/details-cell/GO:0016010)', where it binds directly to cytoskeletal actin via its N-terminus ([GO:0003779](https://www.ebi.ac.uk/QuickGO/term/GO:0003779)) and to the transmembrane protein beta-dystroglycan at the '[Sarcolemma](/details-cell/GO:0042383)' ([GO:0002162](https://www.ebi.ac.uk/QuickGO/term/GO:0002162)) ([Link](https://doi.org/10.1074/jbc.270.45.27305)). This linkage is fundamental to the '[Muscle contraction](/details-cell/R-HSA-397014)' and '[Extracellular matrix organization](/details-cell/R-HSA-1474244)' pathways, as it dissipates the force of contraction and stabilizes the cell membrane. Beyond its structural role, [DMD](/details-gene/1756) participates in signaling. Its association with nitric oxide synthase ([GO:0050998](https://www.ebi.ac.uk/QuickGO/term/GO:0050998)) and its involvement in the '[Regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum](/details-cell/GO:0010880)' points to a function in cellular signaling cascades critical for muscle homeostasis. In the nervous system, its localization to the '[Postsynaptic membrane](/details-cell/GO:0045211)' and involvement in '[Synaptic signaling](/details-cell/GO:0099536)' are consistent with its high expression in various neuron types, where it is thought to anchor receptors and ion channels, thereby modulating neuronal communication. The protein's function is thus best described as a multi-domain scaffold that not only provides physical support but also organizes signaling complexes at the plasma membrane. ## Research Directions The expression data highlights under-explored aspects of dystrophin biology beyond its role in muscle, suggesting new avenues for research into the non-myopathic symptoms of dystrophinopathies. **Proposed Hypotheses:** 1. Given its high significance in multiple GABAergic interneuron subtypes ([sst GABAergic cortical interneuron](/details-cell/CL4023017), [VIP GABAergic cortical interneuron](/details-cell/CL4023016)), we hypothesize that dystrophin isoforms are essential for the structural anchoring of GABAA receptors and associated signaling proteins at inhibitory synapses. Their absence may lead to synaptic instability and altered inhibitory neurotransmission, contributing to the cognitive and behavioral deficits observed in patients with Duchenne Muscular Dystrophy. 2. The unexpected top ranking of [DMD](/details-gene/1756) in [adipocytes](/details-cell/CL0000136) suggests a novel function in adipose tissue. We hypothesize that dystrophin plays a role in mechanotransduction within adipocytes, helping the cells adapt to the mechanical stress associated with lipid droplet expansion and contraction, and that its absence could impair adipocyte function and systemic metabolic homeostasis. **Experimental Approach:** To test the hypothesis regarding dystrophin's role in inhibitory synapses (Hypothesis 1), a conditional knockout mouse model could be employed, using a Cre-Lox system to specifically delete [DMD](/details-gene/1756) in cortical interneurons (e.g., via a *Gad2-Cre* or *Sst-Cre* driver line). The functional consequences could be assessed using slice electrophysiology to measure inhibitory postsynaptic currents (IPSCs) in pyramidal neurons. Concurrently, super-resolution microscopy (e.g., STED or STORM) combined with immunofluorescence for dystrophin, GABAA receptor subunits, and scaffolding proteins like gephyrin could be used to directly visualize and quantify changes in the molecular architecture of inhibitory postsynapses. **Therapeutic Potential:** As a monogenic loss-of-function disorder, Duchenne Muscular Dystrophy is a prime candidate for gene replacement therapy. The therapeutic goal is **activation** or restoration of dystrophin expression. A major challenge has been the immense size of the [DMD](/details-gene/1756) gene, which exceeds the packaging capacity of conventional AAV vectors. This has led to the development of "micro-dystrophin" constructs that retain key functional domains. The data showing high significance in numerous CNS cell types underscores the critical need for therapies that can cross the blood-brain barrier to address the neurological aspects of the disease. Therefore, developing AAV serotypes with high CNS tropism or alternative delivery strategies is paramount for comprehensively treating both the muscular and neurological symptoms of dystrophinopathies.

Disclaimer: This in-silico analysis is generated by an AI language model and may contain inaccuracies or hallucinations. However, it is cross-referenced with curated gene expression data from major biological sources. Please verify the information before use.

Genular Protein ID: 2937386683

Symbol: DMD_HUMAN

Name: N/A

UniProtKB Accession Codes:

P11532 A0A075B6G3 A1L0U9 E7EQR9 E7EQS5 E7ESB2 E9PDN1 E9PDN5 F5GZY3 F8VX32 Q02295 Q14169 Q14170 Q5JYU0 Q6NSJ9 Q7KZ48 Q8N754 Q9UCW3 Q9UCW4

Database IDs:

Citations:

PubMed ID: 3282674

Title: The complete sequence of dystrophin predicts a rod-shaped cytoskeletal protein.

PubMed ID: 3282674

DOI: 10.1016/0092-8674(88)90383-2

PubMed ID: 2668885

Title: Two human cDNA molecules coding for the Duchenne muscular dystrophy (DMD) locus are highly homologous.

PubMed ID: 2668885

DOI: 10.1093/nar/17.13.5391

PubMed ID: 1319059

Title: A 71-kilodalton protein is a major product of the Duchenne muscular dystrophy gene in brain and other nonmuscle tissues.

PubMed ID: 1319059

DOI: 10.1073/pnas.89.12.5346

PubMed ID: 15772651

Title: The DNA sequence of the human X chromosome.

PubMed ID: 15772651

DOI: 10.1038/nature03440

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 3607877

Title: Complete cloning of the Duchenne muscular dystrophy (DMD) cDNA and preliminary genomic organization of the DMD gene in normal and affected individuals.

PubMed ID: 3607877

DOI: 10.1016/0092-8674(87)90504-6

PubMed ID: 2648158

Title: Alternative splicing of human dystrophin mRNA generates isoforms at the carboxy terminus.

PubMed ID: 2648158

DOI: 10.1038/338509a0

PubMed ID: 3428261

Title: Deletions of fetal and adult muscle cDNA in Duchenne and Becker muscular dystrophy patients.

PubMed ID: 3428261

DOI: 10.1002/j.1460-2075.1987.tb02646.x

PubMed ID: 3205741

Title: Deletion screening of the Duchenne muscular dystrophy locus via multiplex DNA amplification.

PubMed ID: 3205741

DOI: 10.1093/nar/16.23.11141

PubMed ID: 2569720

Title: High resolution deletion breakpoint mapping in the DMD gene by whole cosmid hybridization.

PubMed ID: 2569720

DOI: 10.1093/nar/17.14.5611

PubMed ID: 8541829

Title: Cloning and characterization of alternatively spliced isoforms of Dp71.

PubMed ID: 8541829

DOI: 10.1093/hmg/4.9.1475

PubMed ID: 2407739

Title: Detailed analysis of the repeat domain of dystrophin reveals four potential hinge segments that may confer flexibility.

PubMed ID: 2407739

DOI: 10.1016/s0021-9258(19)39599-7

PubMed ID: 7592992

Title: Identification and characterization of the dystrophin anchoring site on beta-dystroglycan.

PubMed ID: 7592992

DOI: 10.1074/jbc.270.45.27305

PubMed ID: 7844150

Title: Syntrophin binds to an alternatively spliced exon of dystrophin.

PubMed ID: 7844150

DOI: 10.1083/jcb.128.3.363

PubMed ID: 8576247

Title: The three human syntrophin genes are expressed in diverse tissues, have distinct chromosomal locations, and each bind to dystrophin and its relatives.

PubMed ID: 8576247

DOI: 10.1074/jbc.271.5.2724

PubMed ID: 9370062

Title: A splice variant of Dp71 lacking the syntrophin binding site is expressed in early stages of human neural development.

PubMed ID: 9370062

DOI: 10.1016/s0165-3806(97)00122-3

PubMed ID: 10747910

Title: Gamma1- and gamma2-syntrophins, two novel dystrophin-binding proteins localized in neuronal cells.

PubMed ID: 10747910

DOI: 10.1074/jbc.m000439200

PubMed ID: 10734266

Title: Expression and synthesis of alternatively spliced variants of Dp71 in adult human brain.

PubMed ID: 10734266

DOI: 10.1016/s0960-8966(99)00105-4

PubMed ID: 11495720

Title: The interaction of dystrophin with beta-dystroglycan is regulated by tyrosine phosphorylation.

PubMed ID: 11495720

DOI: 10.1016/s0898-6568(01)00188-7

PubMed ID: 14636778

Title: Dystrophin and mutations: one gene, several proteins, multiple phenotypes.

PubMed ID: 14636778

DOI: 10.1016/s1474-4422(03)00585-4

PubMed ID: 16000376

Title: Specific interaction of the actin-binding domain of dystrophin with intermediate filaments containing keratin 19.

PubMed ID: 16000376

DOI: 10.1091/mbc.e05-02-0112

PubMed ID: 17081983

Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.

PubMed ID: 17081983

DOI: 10.1016/j.cell.2006.09.026

PubMed ID: 16710609

Title: Role of dystrophin and utrophin for assembly and function of the dystrophin glycoprotein complex in non-muscle tissue.

PubMed ID: 16710609

DOI: 10.1007/s00018-005-5461-0

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 19413330

Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.

PubMed ID: 19413330

DOI: 10.1021/ac9004309

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 10932245

Title: Structure of a WW domain containing fragment of dystrophin in complex with beta-dystroglycan.

PubMed ID: 10932245

DOI: 10.1038/77923

PubMed ID: 10801490

Title: The structure of the N-terminal actin-binding domain of human dystrophin and how mutations in this domain may cause Duchenne or Becker muscular dystrophy.

PubMed ID: 10801490

DOI: 10.1016/s0969-2126(00)00132-5

PubMed ID: 7951253

Title: Searching for the 1 in 2,400,000: a review of dystrophin gene point mutations.

PubMed ID: 7951253

DOI: 10.1002/humu.1380040102

PubMed ID: 8045556

Title: Microlesions and polymorphisms in the Duchenne/Becker muscular dystrophy gene.

PubMed ID: 8045556

DOI: 10.1007/bf00202854

PubMed ID: 8401582

Title: A missense mutation in the dystrophin gene in a Duchenne muscular dystrophy patient.

PubMed ID: 8401582

DOI: 10.1038/ng0893-357

PubMed ID: 7981690

Title: Identification of a missense mutation, single base deletion and a polymorphism in the dystrophin exon 16.

PubMed ID: 7981690

DOI: 10.1093/hmg/3.7.1173

PubMed ID: 7849724

Title: Novel small mutations along the DMD/BMD gene associated with different phenotypes.

PubMed ID: 7849724

DOI: 10.1093/hmg/3.10.1907

PubMed ID: 8817332

Title: A cysteine 3340 substitution in the dystroglycan-binding domain of dystrophin associated with Duchenne muscular dystrophy, mental retardation and absence of the ERG b-wave.

PubMed ID: 8817332

DOI: 10.1093/hmg/5.7.973

PubMed ID: 9170407

Title: Evidence for a dystrophin missense mutation as a cause of X-linked dilated cardiomyopathy.

PubMed ID: 9170407

DOI: 10.1161/01.cir.95.10.2434

PubMed ID: 9851445

Title: A dystrophin missense mutation showing persistence of dystrophin and dystrophin-associated proteins yet a severe phenotype.

PubMed ID: 9851445

DOI: 10.1002/ana.410440619

PubMed ID: 10573008

Title: Identification of point mutations in Turkish DMD/BMD families using multiplex-single stranded conformation analysis (SSCA).

PubMed ID: 10573008

DOI: 10.1038/sj.ejhg.5200370

PubMed ID: 12354438

Title: Comprehensive mutation scanning of the dystrophin gene in patients with nonsyndromic X-linked dilated cardiomyopathy.

PubMed ID: 12354438

DOI: 10.1016/s0735-1097(02)02126-5

PubMed ID: 12359139

Title: Mutations in the dystrophin gene are associated with sporadic dilated cardiomyopathy.

PubMed ID: 12359139

DOI: 10.1016/s1096-7192(02)00153-1

PubMed ID: 12632325

Title: Rapid direct sequence analysis of the dystrophin gene.

PubMed ID: 12632325

DOI: 10.1086/374176

PubMed ID: 16959974

Title: The consensus coding sequences of human breast and colorectal cancers.

PubMed ID: 16959974

DOI: 10.1126/science.1133427

PubMed ID: 21396098

Title: Clinical and molecular characterization of a cohort of patients with novel nucleotide alterations of the Dystrophin gene detected by direct sequencing.

PubMed ID: 21396098

DOI: 10.1186/1471-2350-12-37

PubMed ID: 24302611

Title: The ZZ domain of dystrophin in DMD: making sense of missense mutations.

PubMed ID: 24302611

DOI: 10.1002/humu.22479

PubMed ID: 25340340

Title: Missense mutation Lys18Asn in dystrophin that triggers X-linked dilated cardiomyopathy decreases protein stability, increases protein unfolding, and perturbs protein structure, but does not affect protein function.

PubMed ID: 25340340

DOI: 10.1371/journal.pone.0110439

Sequence Information:

Length: 3685
Mass: 426778
Checksum: 2DBDFB589C7BDC71
Sequence:

MLWWEEVEDC YEREDVQKKT FTKWVNAQFS KFGKQHIENL FSDLQDGRRL LDLLEGLTGQ 
KLPKEKGSTR VHALNNVNKA LRVLQNNNVD LVNIGSTDIV DGNHKLTLGL IWNIILHWQV 
KNVMKNIMAG LQQTNSEKIL LSWVRQSTRN YPQVNVINFT TSWSDGLALN ALIHSHRPDL 
FDWNSVVCQQ SATQRLEHAF NIARYQLGIE KLLDPEDVDT TYPDKKSILM YITSLFQVLP 
QQVSIEAIQE VEMLPRPPKV TKEEHFQLHH QMHYSQQITV SLAQGYERTS SPKPRFKSYA 
YTQAAYVTTS DPTRSPFPSQ HLEAPEDKSF GSSLMESEVN LDRYQTALEE VLSWLLSAED 
TLQAQGEISN DVEVVKDQFH THEGYMMDLT AHQGRVGNIL QLGSKLIGTG KLSEDEETEV 
QEQMNLLNSR WECLRVASME KQSNLHRVLM DLQNQKLKEL NDWLTKTEER TRKMEEEPLG 
PDLEDLKRQV QQHKVLQEDL EQEQVRVNSL THMVVVVDES SGDHATAALE EQLKVLGDRW 
ANICRWTEDR WVLLQDILLK WQRLTEEQCL FSAWLSEKED AVNKIHTTGF KDQNEMLSSL 
QKLAVLKADL EKKKQSMGKL YSLKQDLLST LKNKSVTQKT EAWLDNFARC WDNLVQKLEK 
STAQISQAVT TTQPSLTQTT VMETVTTVTT REQILVKHAQ EELPPPPPQK KRQITVDSEI 
RKRLDVDITE LHSWITRSEA VLQSPEFAIF RKEGNFSDLK EKVNAIEREK AEKFRKLQDA 
SRSAQALVEQ MVNEGVNADS IKQASEQLNS RWIEFCQLLS ERLNWLEYQN NIIAFYNQLQ 
QLEQMTTTAE NWLKIQPTTP SEPTAIKSQL KICKDEVNRL SDLQPQIERL KIQSIALKEK 
GQGPMFLDAD FVAFTNHFKQ VFSDVQAREK ELQTIFDTLP PMRYQETMSA IRTWVQQSET 
KLSIPQLSVT DYEIMEQRLG ELQALQSSLQ EQQSGLYYLS TTVKEMSKKA PSEISRKYQS 
EFEEIEGRWK KLSSQLVEHC QKLEEQMNKL RKIQNHIQTL KKWMAEVDVF LKEEWPALGD 
SEILKKQLKQ CRLLVSDIQT IQPSLNSVNE GGQKIKNEAE PEFASRLETE LKELNTQWDH 
MCQQVYARKE ALKGGLEKTV SLQKDLSEMH EWMTQAEEEY LERDFEYKTP DELQKAVEEM 
KRAKEEAQQK EAKVKLLTES VNSVIAQAPP VAQEALKKEL ETLTTNYQWL CTRLNGKCKT 
LEEVWACWHE LLSYLEKANK WLNEVEFKLK TTENIPGGAE EISEVLDSLE NLMRHSEDNP 
NQIRILAQTL TDGGVMDELI NEELETFNSR WRELHEEAVR RQKLLEQSIQ SAQETEKSLH 
LIQESLTFID KQLAAYIADK VDAAQMPQEA QKIQSDLTSH EISLEEMKKH NQGKEAAQRV 
LSQIDVAQKK LQDVSMKFRL FQKPANFEQR LQESKMILDE VKMHLPALET KSVEQEVVQS 
QLNHCVNLYK SLSEVKSEVE MVIKTGRQIV QKKQTENPKE LDERVTALKL HYNELGAKVT 
ERKQQLEKCL KLSRKMRKEM NVLTEWLAAT DMELTKRSAV EGMPSNLDSE VAWGKATQKE 
IEKQKVHLKS ITEVGEALKT VLGKKETLVE DKLSLLNSNW IAVTSRAEEW LNLLLEYQKH 
METFDQNVDH ITKWIIQADT LLDESEKKKP QQKEDVLKRL KAELNDIRPK VDSTRDQAAN 
LMANRGDHCR KLVEPQISEL NHRFAAISHR IKTGKASIPL KELEQFNSDI QKLLEPLEAE 
IQQGVNLKEE DFNKDMNEDN EGTVKELLQR GDNLQQRITD ERKREEIKIK QQLLQTKHNA 
LKDLRSQRRK KALEISHQWY QYKRQADDLL KCLDDIEKKL ASLPEPRDER KIKEIDRELQ 
KKKEELNAVR RQAEGLSEDG AAMAVEPTQI QLSKRWREIE SKFAQFRRLN FAQIHTVREE 
TMMVMTEDMP LEISYVPSTY LTEITHVSQA LLEVEQLLNA PDLCAKDFED LFKQEESLKN 
IKDSLQQSSG RIDIIHSKKT AALQSATPVE RVKLQEALSQ LDFQWEKVNK MYKDRQGRFD 
RSVEKWRRFH YDIKIFNQWL TEAEQFLRKT QIPENWEHAK YKWYLKELQD GIGQRQTVVR 
TLNATGEEII QQSSKTDASI LQEKLGSLNL RWQEVCKQLS DRKKRLEEQK NILSEFQRDL 
NEFVLWLEEA DNIASIPLEP GKEQQLKEKL EQVKLLVEEL PLRQGILKQL NETGGPVLVS 
APISPEEQDK LENKLKQTNL QWIKVSRALP EKQGEIEAQI KDLGQLEKKL EDLEEQLNHL 
LLWLSPIRNQ LEIYNQPNQE GPFDVKETEI AVQAKQPDVE EILSKGQHLY KEKPATQPVK 
RKLEDLSSEW KAVNRLLQEL RAKQPDLAPG LTTIGASPTQ TVTLVTQPVV TKETAISKLE 
MPSSLMLEVP ALADFNRAWT ELTDWLSLLD QVIKSQRVMV GDLEDINEMI IKQKATMQDL 
EQRRPQLEEL ITAAQNLKNK TSNQEARTII TDRIERIQNQ WDEVQEHLQN RRQQLNEMLK 
DSTQWLEAKE EAEQVLGQAR AKLESWKEGP YTVDAIQKKI TETKQLAKDL RQWQTNVDVA 
NDLALKLLRD YSADDTRKVH MITENINASW RSIHKRVSER EAALEETHRL LQQFPLDLEK 
FLAWLTEAET TANVLQDATR KERLLEDSKG VKELMKQWQD LQGEIEAHTD VYHNLDENSQ 
KILRSLEGSD DAVLLQRRLD NMNFKWSELR KKSLNIRSHL EASSDQWKRL HLSLQELLVW 
LQLKDDELSR QAPIGGDFPA VQKQNDVHRA FKRELKTKEP VIMSTLETVR IFLTEQPLEG 
LEKLYQEPRE LPPEERAQNV TRLLRKQAEE VNTEWEKLNL HSADWQRKID ETLERLRELQ 
EATDELDLKL RQAEVIKGSW QPVGDLLIDS LQDHLEKVKA LRGEIAPLKE NVSHVNDLAR 
QLTTLGIQLS PYNLSTLEDL NTRWKLLQVA VEDRVRQLHE AHRDFGPASQ HFLSTSVQGP 
WERAISPNKV PYYINHETQT TCWDHPKMTE LYQSLADLNN VRFSAYRTAM KLRRLQKALC 
LDLLSLSAAC DALDQHNLKQ NDQPMDILQI INCLTTIYDR LEQEHNNLVN VPLCVDMCLN 
WLLNVYDTGR TGRIRVLSFK TGIISLCKAH LEDKYRYLFK QVASSTGFCD QRRLGLLLHD 
SIQIPRQLGE VASFGGSNIE PSVRSCFQFA NNKPEIEAAL FLDWMRLEPQ SMVWLPVLHR 
VAAAETAKHQ AKCNICKECP IIGFRYRSLK HFNYDICQSC FFSGRVAKGH KMHYPMVEYC 
TPTTSGEDVR DFAKVLKNKF RTKRYFAKHP RMGYLPVQTV LEGDNMETPV TLINFWPVDS 
APASSPQLSH DDTHSRIEHY ASRLAEMENS NGSYLNDSIS PNESIDDEHL LIQHYCQSLN 
QDSPLSQPRS PAQILISLES EERGELERIL ADLEEENRNL QAEYDRLKQQ HEHKGLSPLP 
SPPEMMPTSP QSPRDAELIA EAKLLRQHKG RLEARMQILE DHNKQLESQL HRLRQLLEQP 
QAEAKVNGTT VSSPSTSLQR SDSSQPMLLR VVGSQTSDSM GEEDLLSPPQ DTSTGLEEVM 
EQLNNSFPSS RGRNTPGKPM REDTM

Genular Protein ID: 1262659839

Symbol: Q4G0X0_HUMAN

Name: N/A

UniProtKB Accession Codes:

Q4G0X0

Database IDs:

Citations:

PubMed ID: 11237011

Title: Initial sequencing and analysis of the human genome.

PubMed ID: 11237011

DOI: 10.1038/35057062

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 15496913

Title: Finishing the euchromatic sequence of the human genome.

PubMed ID: 15496913

DOI: 10.1038/nature03001

PubMed ID: 15772651

Title: The DNA sequence of the human X chromosome.

PubMed ID: 15772651

DOI: 10.1038/nature03440

Sequence Information:

Length: 772
Mass: 88800
Checksum: 33AEE50114531EBA
Sequence:

MEDEREDVQK KTFTKWVNAQ FSKFGKQHIE NLFSDLQDGR RLLDLLEGLT GQKLPKEKGS 
TRVHALNNVN KALRVLQNNN VDLVNIGSTD IVDGNHKLTL GLIWNIILHW QVKNVMKNIM 
AGLQQTNSEK ILLSWVRQST RNYPQVNVIN FTTSWSDGLA LNALIHSHRP DLFDWNSVVC 
QQSATQRLEH AFNIARYQLG IEKLLDPEDV DTTYPDKKSI LMYITSLFQV LPQQVSIEAI 
QEVEMLPRPP KVTKEEHFQL HHQMHYSQQI TVSLAQGYER TSSPKPRFKS YAYTQAAYVT 
TSDPTRSPFP SQHLEAPEDK SFGSSLMESE VNLDRYQTAL EEVLSWLLSA EDTLQAQGEI 
SNDVEVVKDQ FHTHEGYMMD LTAHQGRVGN ILQLGSKLIG TGKLSEDEET EVQEQMNLLN 
SRWECLRVAS MEKQSNLHRV LMDLQNQKLK ELNDWLTKTE ERTRKMEEEP LGPDLEDLKR 
QVQQHKVLQE DLEQEQVRVN SLTHMVVVVD ESSGDHATAA LEEQLKVLGD RWANICRWTE 
DRWVLLQDIL LKWQRLTEEQ CLFSAWLSEK EDAVNKIHTT GFKDQNEMLS SLQKLAVLKA 
DLEKKKQSMG KLYSLKQDLL STLKNKSVTQ KTEAWLDNFA RCWDNLVQKL EKSTAQISQA 
VTTTQPSLTQ TTVMETVTTV TTREQILVKH AQEELPPPPP QKKRQITVDS EIRKRLDVDI 
TELHSWITRS EAVLQSPEFA IFRKEGNFSD LKEKVNVGYA LIFISVLILC CL

Genular Protein ID: 1747168688

Symbol: Q16484_HUMAN

Name: N/A

UniProtKB Accession Codes:

Q16484

Database IDs:

Citations:

PubMed ID: 1380160

Title: Distal transcript of the dystrophin gene initiated from an alternative first exon and encoding a 75-kDa protein widely distributed in nonmuscle tissues.

PubMed ID: 1380160

DOI: 10.1073/pnas.89.16.7506

Sequence Information:

Length: 14
Mass: 1662
Checksum: 2D5889B6976E28E8
Sequence:

MREQLKGHET QTTC

Genular Protein ID: 624637552

Symbol: A0A0S2Z3B5_HUMAN

Name: N/A

UniProtKB Accession Codes:

A0A0S2Z3B5

Database IDs:

Citations:

PubMed ID: 26871637

Title: Widespread Expansion of Protein Interaction Capabilities by Alternative Splicing.

PubMed ID: 26871637

DOI: 10.1016/j.cell.2016.01.029

Sequence Information:

Length: 617
Mass: 70375
Checksum: 660C9D904AF403B9
Sequence:

MREQLKGHET QTTCWDHPKM TELYQSLADL NNVRFSAYRT AMKLRRLQKA LCLDLLSLSA 
ACDALDQHNL KQNDQPMDIL QIINCLTTIY DRLEQEHNNL VNVPLCVDMC LNWLLNVYDT 
GRTGRIRVLS FKTGIISLCK AHLEDKYRYL FKQVASSTGF CDQRRLGLLL HDSIQIPRQL 
GEVASFGGSN IEPSVRSCFQ FANNKPEIEA ALFLDWMRLE PQSMVWLPVL HRVAAAETAK 
HQAKCNICKE CPIIGFRYRS LKHFNYDICQ SCFFSGRVAK GHKMHYPMVE YCTPTTSGED 
VRDFAKVLKN KFRTKRYFAK HPRMGYLPVQ TVLEGDNMET PVTLINFWPV DSAPASSPQL 
SHDDTHSRIE HYASRLAEME NSNGSYLNDS ISPNESIDDE HLLIQHYCQS LNQDSPLSQP 
RSPAQILISL ESEERGELER ILADLEEENR NLQAEYDRLK QQHEHKGLSP LPSPPEMMPT 
SPQSPRDAEL IAEAKLLRQH KGRLEARMQI LEDHNKQLES QLHRLRQLLE QPQAEAKVNG 
TTVSSPSTSL QRSDSSQPML LRVVGSQTSD SMGEEDLLSP PQDTSTGLEE VMEQLNNSFP 
SSRGRNTPGK PMREDTM

Genular Protein ID: 1467643553

Symbol: A7E212_HUMAN

Name: N/A

UniProtKB Accession Codes:

A7E212

Database IDs:

Citations:

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

Sequence Information:

Length: 1243
Mass: 143187
Checksum: 5CF301BCA476E93F
Sequence:

MPSSLMLEVP ALADFNRAWT ELTDWLSLLD QVIKSQRVMV GDLEDINEMI IKQKATMQDL 
EQRRPQLEEL ITAAQNLKNK TSNQEARTII TDRIERIQNQ WDEVQEHLQN RRQQLNEMLK 
DSTQWLEAKE EAEQVLGQAR AKLESWKEGP YTVDAIQKKI TETKQLAKDL RQWQTNVDVA 
NDLALKLLRD YSADDTRKVH MITENINASW RSIHKRVSER EAALEETHRL LQQFPLDLEK 
FLAWLTEAET TANVLQDATR KERLLEDSKG VKELMKQWQD LQGEIEAHTD VYHNLDENSQ 
KILRSLEGSD DAVLLQRRLD NMNFKWSELR KKSLNIRSHL EASSDQWKRL HLSLQELLVW 
LQLKDDELSR QAPIGGDFPA VQKQNDVHRA FKRELKTKEP VIMSTLETVR IFLTEQPLEG 
LEKLYQEPRE LPPEERAQNV TRLLRKQAEE VNTEWEKLNL HSADWQRKID ETLERLQELQ 
EATDELDLKL RQAEVIKGSW QPVGDLLIDS LQDHLEKVKA LRGEIAPLKE NVSHVNDLAR 
QLTTLGIQLS PYNLSTLEDL NTRWKLLQVA VEDRVRQLHE AHRDFGPASQ HFLSTSVQGP 
WERAISPNKV PYYINHETQT TCWDHPKMTE LYQSLADLNN VRFSAYRTAM KLRRLQKALC 
LDLLSLSAAC DALDQHNLKQ NDQPMDILQI INCLTTIYDR LEQEHNNLVN VPLCVDMCLN 
WLLNVYDTGR TGRIRVLSFK TGIISLCKAH LEDKYRYLFK QVASSTGFCD QRRLGLLLHD 
SIQIPRQLGE VASFGGSNIE PSVRSCFQFA NNKPEIEAAL FLDWMRLEPQ SMVWLPVLHR 
VAAAETAKHQ AKCNICKECP IIGFRYRSLK HFNYDICQSC FFSGRVAKGH KMHYPMVEYC 
TPTTSGEDVR DFAKVLKNKF RTKRYFAKHP RMGYLPVQTV LEGDNMETPV TLINFWPVDS 
APASSPQLSH DDTHSRIEHY ASRLAEMENS NGSYLNDSIS PNESIDDEHL LIQHYCQSLN 
QDSPLSQPRS PAQILISLES EERGELERIL ADLEEENRNL QAEYDRLKQQ HEHKGLSPLP 
SPPEMMPTSP QSPRDAELIA EAKLLRQHKG RLEARMQILE DHNKQLESQL HRLRQLLEQP 
QAEAKVNGTT VSSPSTSLQR SDSSQPMLLR VVGSQTSDSM GEEDLLSPPQ DTSTGLEEVM 
EQLNNSFPSS RGHNVGSLFH MADDLGRAME SLVSVMTDEE GAE

Genular Protein ID: 2478390617

Symbol: A0A0S2Z3J7_HUMAN

Name: N/A

UniProtKB Accession Codes:

A0A0S2Z3J7

Database IDs:

Citations:

PubMed ID: 26871637

Title: Widespread Expansion of Protein Interaction Capabilities by Alternative Splicing.

PubMed ID: 26871637

DOI: 10.1016/j.cell.2016.01.029

Sequence Information:

Length: 635
Mass: 72191
Checksum: 5EB1E49C45CF34EC
Sequence:

MREQLKGHET QTTCWDHPKM TELYQSLADL NNVRFSAYRT AMKLRRLQKA LCLDLLSLSA 
ACDALDQHNL KQNDQPMDIL QIINCLTTIY DRLEQEHNNL VNVPLCVDMC LNWLLNVYDT 
GRTGRIRVLS FKTGIISLCK AHLEDKYRYL FKQVASSTGF CDQRRLGLLL HDSIQIPRQL 
GEVASFGGSN IEPSVRSCFQ FANNKPEIEA ALFLDWMRLE PQSMVWLPVL HRVAAAETAK 
HQAKCNICKE CPIIGFRYRS LKHFNYDICQ SCFFSGRVAK GHKMHYPMVE YCTPTTSGED 
VRDFAKVLKN KFRTKRYFAK HPRMGYLPVQ TVLEGDNMET PVTLINFWPV DSAPASSPQL 
SHDDTHSRIE HYASRLAEME NSNGSYLNDS ISPNESIDDE HLLIQHYCQS LNQDSPLSQP 
RSPAQILISL ESEERGELER ILADLEEENR NLQAEYDRLK QQHEHKGLSP LPSPPEMMPT 
SPQSPRDAEL IAEAKLLRQH KGRLEARMQI LEDHNKQLES QLHRLRQLLE QPQAEAKVNG 
TTVSSPSTSL QRSDSSQPML LRVVGSQTSD SMGEEDLLSP PQDTSTGLEE VMEQLNNSFP 
SSRGHNVGSL FHMADDLGRA MESLVSVMTD EEGAE

	Overall overall
	Alzheimer disease MONDO0004975
	Amyotrophic lateral sclerosis MONDO0004976
	Basal cell carcinoma MONDO0020804
	Bipolar disorder MONDO0004985
	Bipolar I disorder MONDO0001866
	Brain UBERON0000955
	\|— Brain Healthy UBERON0000955_PATO0000461
	Breast UBERON0000310
	\|— Breast cancer MONDO0007254
	Caudate lobe of liver UBERON0001117
	Cerebellum UBERON0002037
	\|— Cerebellum Healthy UBERON0002037_PATO0000461
	Cerebral cortex UBERON0000956
	\|— Cerebral cortex Healthy UBERON0000956_PATO0000461
	Choroid plexus UBERON0001886
	Chronic kidney disease MONDO0005300
	Colon UBERON0001155
	\|— Colon Healthy UBERON0001155_PATO0000461
	Cortex of kidney UBERON0001225
	\|— Cortex of kidney Healthy UBERON0001225_PATO0000461
	COVID-19 MONDO0100096
	Crohn disease MONDO0005011
	Dementia MONDO0001627
	Dental pulp UBERON0001754
	Dorsolateral prefrontal cortex UBERON0009834
	\|— Dorsolateral prefrontal cortex Bipolar disorder UBERON0009834_MONDO0004985
	\|— Dorsolateral prefrontal cortex Bipolar I disorder UBERON0009834_MONDO0001866
	\|— Dorsolateral prefrontal cortex Dementia UBERON0009834_MONDO0001627
	\|— Dorsolateral prefrontal cortex Healthy UBERON0009834_PATO0000461
	\|— Dorsolateral prefrontal cortex Schizophrenia UBERON0009834_MONDO0005090
	\|— Dorsolateral prefrontal cortex Vascular dementia UBERON0009834_MONDO0004648
	Entorhinal cortex UBERON0002728
	Fovea centralis UBERON0001786
	\|— Fovea centralis Healthy UBERON0001786_PATO0000461
	Frontal cortex UBERON0001870
	Glioblastoma MONDO0018177
	Healthy PATO0000461
	Heart left ventricle UBERON0002084
	\|— Heart left ventricle Healthy UBERON0002084_PATO0000461
	Heart right ventricle UBERON0002080
	\|— Heart right ventricle Healthy UBERON0002080_PATO0000461
	Hippocampal formation UBERON0002421
	\|— Hippocampal formation Healthy UBERON0002421_PATO0000461
	Hypothalamus UBERON0001898
	\|— Hypothalamus Healthy UBERON0001898_PATO0000461
	Ileum UBERON0002116
	\|— Ileum Healthy UBERON0002116_PATO0000461
	Interventricular septum UBERON0002094
	Isolated focal cortical dysplasia type II MONDO0011818
	Kidney UBERON0002113
	\|— Kidney Healthy UBERON0002113_PATO0000461
	Leukoencephalopathy, diffuse hereditary, with spheroids 1 MONDO0800027
	Liver UBERON0002107
	Lung UBERON0002048
	\|— Lung Healthy UBERON0002048_PATO0000461
	Lymph node UBERON0000029
	Medial orbital frontal cortex UBERON0022352
	Midbrain UBERON0001891
	\|— Midbrain Healthy UBERON0001891_PATO0000461
	Nasopharynx UBERON0001728
	Neocortex UBERON0001950
	\|— Neocortex Healthy UBERON0001950_PATO0000461
	Neuroblastoma MONDO0005072
	Occipital cortex UBERON0016540
	Peripheral region of retina UBERON0013682
	\|— Peripheral region of retina Healthy UBERON0013682_PATO0000461
	Pons UBERON0000988
	\|— Pons Healthy UBERON0000988_PATO0000461
	Prefrontal cortex UBERON0000451
	\|— Prefrontal cortex Healthy UBERON0000451_PATO0000461
	Primary motor cortex UBERON0001384
	Renal medulla UBERON0000362
	\|— Renal medulla Healthy UBERON0000362_PATO0000461
	Retina UBERON0000966
	\|— Retina Healthy UBERON0000966_PATO0000461
	Right atrium auricular region UBERON0006631
	Right cardiac atrium UBERON0002078
	\|— Right cardiac atrium Healthy UBERON0002078_PATO0000461
	Schizophrenia MONDO0005090
	Sclera UBERON0001773
	\|— Sclera Healthy UBERON0001773_PATO0000461
	Sigmoid colon UBERON0001159
	Substantia nigra pars compacta UBERON0001965
	Telencephalon UBERON0001893
	\|— Telencephalon Healthy UBERON0001893_PATO0000461
	Thalamic complex UBERON0010225
	\|— Thalamic complex Healthy UBERON0010225_PATO0000461
	UBERON0005290 UBERON0005290
	\|— UBERON0005290 Healthy UBERON0005290_PATO0000461
	UBERON8440012 UBERON8440012
	\|— UBERON8440012 Healthy UBERON8440012_PATO0000461
	Vascular dementia MONDO0004648

Details for: DMD

Cell Significance Landscape

Associated with

Significant Cells

Network Configuration

Legend:

Other Information

The complete sequence of dystrophin predicts a rod-shaped cytoskeletal protein. PubMed ID: 3282674

Two human cDNA molecules coding for the Duchenne muscular dystrophy (DMD) locus are highly homologous. PubMed ID: 2668885

A 71-kilodalton protein is a major product of the Duchenne muscular dystrophy gene in brain and other nonmuscle tissues. PubMed ID: 1319059

The DNA sequence of the human X chromosome. PubMed ID: 15772651

The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). PubMed ID: 15489334

Complete cloning of the Duchenne muscular dystrophy (DMD) cDNA and preliminary genomic organization of the DMD gene in normal and affected individuals. PubMed ID: 3607877

Alternative splicing of human dystrophin mRNA generates isoforms at the carboxy terminus. PubMed ID: 2648158

Deletions of fetal and adult muscle cDNA in Duchenne and Becker muscular dystrophy patients. PubMed ID: 3428261

Deletion screening of the Duchenne muscular dystrophy locus via multiplex DNA amplification. PubMed ID: 3205741

High resolution deletion breakpoint mapping in the DMD gene by whole cosmid hybridization. PubMed ID: 2569720

Cloning and characterization of alternatively spliced isoforms of Dp71. PubMed ID: 8541829

Detailed analysis of the repeat domain of dystrophin reveals four potential hinge segments that may confer flexibility. PubMed ID: 2407739

Identification and characterization of the dystrophin anchoring site on beta-dystroglycan. PubMed ID: 7592992

Syntrophin binds to an alternatively spliced exon of dystrophin. PubMed ID: 7844150

The three human syntrophin genes are expressed in diverse tissues, have distinct chromosomal locations, and each bind to dystrophin and its relatives. PubMed ID: 8576247

A splice variant of Dp71 lacking the syntrophin binding site is expressed in early stages of human neural development. PubMed ID: 9370062

Gamma1- and gamma2-syntrophins, two novel dystrophin-binding proteins localized in neuronal cells. PubMed ID: 10747910

Expression and synthesis of alternatively spliced variants of Dp71 in adult human brain. PubMed ID: 10734266

The interaction of dystrophin with beta-dystroglycan is regulated by tyrosine phosphorylation. PubMed ID: 11495720

Dystrophin and mutations: one gene, several proteins, multiple phenotypes. PubMed ID: 14636778

Specific interaction of the actin-binding domain of dystrophin with intermediate filaments containing keratin 19. PubMed ID: 16000376

Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. PubMed ID: 17081983

Role of dystrophin and utrophin for assembly and function of the dystrophin glycoprotein complex in non-muscle tissue. PubMed ID: 16710609

A quantitative atlas of mitotic phosphorylation. PubMed ID: 18669648

Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. PubMed ID: 19413330

Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. PubMed ID: 20068231

Initial characterization of the human central proteome. PubMed ID: 21269460

Toward a comprehensive characterization of a human cancer cell phosphoproteome. PubMed ID: 23186163

An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. PubMed ID: 24275569

Structure of a WW domain containing fragment of dystrophin in complex with beta-dystroglycan. PubMed ID: 10932245

The structure of the N-terminal actin-binding domain of human dystrophin and how mutations in this domain may cause Duchenne or Becker muscular dystrophy. PubMed ID: 10801490

Searching for the 1 in 2,400,000: a review of dystrophin gene point mutations. PubMed ID: 7951253

Microlesions and polymorphisms in the Duchenne/Becker muscular dystrophy gene. PubMed ID: 8045556

A missense mutation in the dystrophin gene in a Duchenne muscular dystrophy patient. PubMed ID: 8401582

Identification of a missense mutation, single base deletion and a polymorphism in the dystrophin exon 16. PubMed ID: 7981690

Novel small mutations along the DMD/BMD gene associated with different phenotypes. PubMed ID: 7849724

A cysteine 3340 substitution in the dystroglycan-binding domain of dystrophin associated with Duchenne muscular dystrophy, mental retardation and absence of the ERG b-wave. PubMed ID: 8817332

Evidence for a dystrophin missense mutation as a cause of X-linked dilated cardiomyopathy. PubMed ID: 9170407

A dystrophin missense mutation showing persistence of dystrophin and dystrophin-associated proteins yet a severe phenotype. PubMed ID: 9851445

Identification of point mutations in Turkish DMD/BMD families using multiplex-single stranded conformation analysis (SSCA). PubMed ID: 10573008

Comprehensive mutation scanning of the dystrophin gene in patients with nonsyndromic X-linked dilated cardiomyopathy. PubMed ID: 12354438

Mutations in the dystrophin gene are associated with sporadic dilated cardiomyopathy. PubMed ID: 12359139

Rapid direct sequence analysis of the dystrophin gene. PubMed ID: 12632325

The consensus coding sequences of human breast and colorectal cancers. PubMed ID: 16959974

Clinical and molecular characterization of a cohort of patients with novel nucleotide alterations of the Dystrophin gene detected by direct sequencing. PubMed ID: 21396098

The ZZ domain of dystrophin in DMD: making sense of missense mutations. PubMed ID: 24302611

Missense mutation Lys18Asn in dystrophin that triggers X-linked dilated cardiomyopathy decreases protein stability, increases protein unfolding, and perturbs protein structure, but does not affect protein function. PubMed ID: 25340340

Initial sequencing and analysis of the human genome. PubMed ID: 11237011

The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). PubMed ID: 15489334

Finishing the euchromatic sequence of the human genome. PubMed ID: 15496913

The DNA sequence of the human X chromosome. PubMed ID: 15772651

Distal transcript of the dystrophin gene initiated from an alternative first exon and encoding a 75-kDa protein widely distributed in nonmuscle tissues. PubMed ID: 1380160

Widespread Expansion of Protein Interaction Capabilities by Alternative Splicing. PubMed ID: 26871637

The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). PubMed ID: 15489334

Widespread Expansion of Protein Interaction Capabilities by Alternative Splicing. PubMed ID: 26871637

PubMed ID: 3282674

PubMed ID: 2668885

PubMed ID: 1319059

PubMed ID: 15772651

PubMed ID: 15489334

PubMed ID: 3607877

PubMed ID: 2648158

PubMed ID: 3428261

PubMed ID: 3205741

PubMed ID: 2569720

PubMed ID: 8541829

PubMed ID: 2407739

PubMed ID: 7592992

PubMed ID: 7844150

PubMed ID: 8576247

PubMed ID: 9370062

PubMed ID: 10747910

PubMed ID: 10734266

PubMed ID: 11495720

PubMed ID: 14636778

PubMed ID: 16000376

PubMed ID: 17081983

PubMed ID: 16710609

PubMed ID: 18669648

PubMed ID: 19413330

PubMed ID: 20068231

PubMed ID: 21269460

PubMed ID: 23186163

PubMed ID: 24275569

PubMed ID: 10932245

PubMed ID: 10801490

PubMed ID: 7951253

PubMed ID: 8045556

PubMed ID: 8401582

PubMed ID: 7981690

PubMed ID: 7849724

PubMed ID: 8817332

PubMed ID: 9170407

PubMed ID: 9851445

PubMed ID: 10573008

PubMed ID: 12354438

PubMed ID: 12359139

PubMed ID: 12632325

PubMed ID: 16959974

PubMed ID: 21396098

PubMed ID: 24302611

PubMed ID: 25340340

PubMed ID: 11237011

PubMed ID: 15489334

PubMed ID: 15496913

PubMed ID: 15772651

PubMed ID: 1380160

PubMed ID: 26871637

PubMed ID: 15489334

PubMed ID: 26871637