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Conserved domains on  [gi|442618286|ref|NP_001262428|]
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uncharacterized protein Dmel_CG8312, isoform D [Drosophila melanogaster]

Protein Classification

FAM43A/B family PTB domain-containing protein( domain architecture ID 10631605)

FAM43A/B family (phosphotyrosine-binding) domain-containing protein similar to mammalian proteins FAM43A and FAM43B

CATH:  2.30.29.30
Gene Ontology:  GO:0005515
PubMed:  15567406|8987385|10610414
SCOP:  4002427

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PID_2 pfam14719
Phosphotyrosine interaction domain (PTB/PID);
263-441 5.14e-106

Phosphotyrosine interaction domain (PTB/PID);


:

Pssm-ID: 405418  Cd Length: 184  Bit Score: 324.42  E-value: 5.14e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618286  263 EFKVSYLGNVLTGWAKGEGCVEKQLNTLWRNYTQHsKPDVIMRLKVCASGLKATTRQHGLTEYWAHRITYCCAPKNYPRV 342
Cdd:pfam14719   1 TYKVVYLGNVLTIHAKGEGCTDKPLGTIWKNYCQG-KSGTKMKLTVTRSGLKATTKEHGLTEYWSHRITYCSAPPNYPRV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618286  343 FCWIYRHEGRKLKHELRCHAVLCSKEKIAQDICDTLRENLESALREFKREKIL---KQNARLSLANAVYDNPSLPRRKIM 419
Cdd:pfam14719  80 FCWVYRHEGRKLKVELRCHAVLCKKEEKARAMALLLYQTLRAALQEFKREKLCarhAQNARLSLGNAAYDPPSVPRRKLL 159

                         170       180
                  ....*....|....*....|..
gi 442618286  420 LSVggNNYRPPLERSKSAPKLM 441
Cdd:pfam14719 160 TGT--CNYRPPVERSKSAPKLG 179
 
Name Accession Description Interval E-value
PID_2 pfam14719
Phosphotyrosine interaction domain (PTB/PID);
263-441 5.14e-106

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 405418  Cd Length: 184  Bit Score: 324.42  E-value: 5.14e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618286  263 EFKVSYLGNVLTGWAKGEGCVEKQLNTLWRNYTQHsKPDVIMRLKVCASGLKATTRQHGLTEYWAHRITYCCAPKNYPRV 342
Cdd:pfam14719   1 TYKVVYLGNVLTIHAKGEGCTDKPLGTIWKNYCQG-KSGTKMKLTVTRSGLKATTKEHGLTEYWSHRITYCSAPPNYPRV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618286  343 FCWIYRHEGRKLKHELRCHAVLCSKEKIAQDICDTLRENLESALREFKREKIL---KQNARLSLANAVYDNPSLPRRKIM 419
Cdd:pfam14719  80 FCWVYRHEGRKLKVELRCHAVLCKKEEKARAMALLLYQTLRAALQEFKREKLCarhAQNARLSLGNAAYDPPSVPRRKLL 159

                         170       180
                  ....*....|....*....|..
gi 442618286  420 LSVggNNYRPPLERSKSAPKLM 441
Cdd:pfam14719 160 TGT--CNYRPPVERSKSAPKLG 179
PTB_FAM43A cd01214
Family with sequence similarity 43, member A (FAM43A) Phosphotyrosine-binding (PTB) domain; ...
 257-381 3.22e-85

Family with sequence similarity 43, member A (FAM43A) Phosphotyrosine-binding (PTB) domain; The function of FAM43A is currently unknown. Human FAM43A is located on chromosome 3 at location 3q29. It encodes a 3182 base pair mRNA which possesses one Pleckstrin homology-like domain. The mRNA translates into LOC131583, a hydrophilic protein that is predicted to localize in the nucleus. The FAM43A gene is conserved through a broad range of vertebrates. It is highly conserved from chimpanzees to zebrafish. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains.


Pssm-ID: 269925  Cd Length: 125  Bit Score: 267.62  E-value: 3.22e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618286 257 ISTPDPEFKVSYLGNVLTGWAKGEGCVEKQLNTLWRNYTQHSKPDVIMRLKVCASGLKATTRQHGLTEYWAHRITYCCAP 336
Cdd:cd01214    1 ITEEDPTYTVVYLGNVLTIWAKGEGCTDKPLATIWRNYTQGKKPDVKMKLTVTPSGLKATTKQHGLTEYWLHRITYCSAP 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 442618286 337 KNYPRVFCWIYRHEGRKLKHELRCHAVLCSKEKIAQDICDTLREN 381
Cdd:cd01214   81 PNYPRVFCWIYRHEGRKLKVELRCHAVLCSKESKARAIALLLYQR 125
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 260-393 1.10e-19

Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain structure similar to those of pleckstrin homology (PH) and IRS-1-like PTB domains.


Pssm-ID: 214675  Cd Length: 134  Bit Score: 85.83  E-value: 1.10e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618286   260 PDPEFKVSYLGNVLTGWAKGEGCVEKQLNTLWRNYTQHSKPDVIMRLKVCASGLKATTRQHG--LTEYWAHRITYCCAPK 337
Cdd:smart00462   2 SGVSFRVKYLGSVEVPEARGLQVVQEAIRKLRAAQGSEKKEPQKVILSISSRGVKLIDEDTKavLHEHPLRRISFCAVGP 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 442618286   338 NYPRVFCWIYRHEGrklKHELRCHAVLCSKEkiAQDICDTLRENLESALREFKREK 393
Cdd:smart00462  82 DDLDVFGYIARDPG---SSRFACHVFRCEKA--AEDIALAIGQAFQLAYELKLKAR 132
 
Name Accession Description Interval E-value
PID_2 pfam14719
Phosphotyrosine interaction domain (PTB/PID);
263-441 5.14e-106

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 405418  Cd Length: 184  Bit Score: 324.42  E-value: 5.14e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618286  263 EFKVSYLGNVLTGWAKGEGCVEKQLNTLWRNYTQHsKPDVIMRLKVCASGLKATTRQHGLTEYWAHRITYCCAPKNYPRV 342
Cdd:pfam14719   1 TYKVVYLGNVLTIHAKGEGCTDKPLGTIWKNYCQG-KSGTKMKLTVTRSGLKATTKEHGLTEYWSHRITYCSAPPNYPRV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618286  343 FCWIYRHEGRKLKHELRCHAVLCSKEKIAQDICDTLRENLESALREFKREKIL---KQNARLSLANAVYDNPSLPRRKIM 419
Cdd:pfam14719  80 FCWVYRHEGRKLKVELRCHAVLCKKEEKARAMALLLYQTLRAALQEFKREKLCarhAQNARLSLGNAAYDPPSVPRRKLL 159

                         170       180
                  ....*....|....*....|..
gi 442618286  420 LSVggNNYRPPLERSKSAPKLM 441
Cdd:pfam14719 160 TGT--CNYRPPVERSKSAPKLG 179
PTB_FAM43A cd01214
Family with sequence similarity 43, member A (FAM43A) Phosphotyrosine-binding (PTB) domain; ...
 257-381 3.22e-85

Family with sequence similarity 43, member A (FAM43A) Phosphotyrosine-binding (PTB) domain; The function of FAM43A is currently unknown. Human FAM43A is located on chromosome 3 at location 3q29. It encodes a 3182 base pair mRNA which possesses one Pleckstrin homology-like domain. The mRNA translates into LOC131583, a hydrophilic protein that is predicted to localize in the nucleus. The FAM43A gene is conserved through a broad range of vertebrates. It is highly conserved from chimpanzees to zebrafish. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains.


Pssm-ID: 269925  Cd Length: 125  Bit Score: 267.62  E-value: 3.22e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618286 257 ISTPDPEFKVSYLGNVLTGWAKGEGCVEKQLNTLWRNYTQHSKPDVIMRLKVCASGLKATTRQHGLTEYWAHRITYCCAP 336
Cdd:cd01214    1 ITEEDPTYTVVYLGNVLTIWAKGEGCTDKPLATIWRNYTQGKKPDVKMKLTVTPSGLKATTKQHGLTEYWLHRITYCSAP 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 442618286 337 KNYPRVFCWIYRHEGRKLKHELRCHAVLCSKEKIAQDICDTLREN 381
Cdd:cd01214   81 PNYPRVFCWIYRHEGRKLKVELRCHAVLCSKESKARAIALLLYQR 125
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
 262-381 2.95e-22

Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to bind peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains.


Pssm-ID: 269911  Cd Length: 120  Bit Score: 92.96  E-value: 2.95e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618286 262 PEFKVSYLGNVLTGWAKGEGCVEKQLNTLWRNYTQHSKPDVIMRLKVCASGLKATTRQHG--LTEYWAHRITYCCAPKNY 339
Cdd:cd00934    1 ASFQVKYLGSVEVGSSRGVDVVEEALKALAAALKSSKRKPGPVLLEVSSKGVKLLDLDTKelLLRHPLHRISYCGRDPDN 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 442618286 340 PRVFCWIYRHEGRKlkhELRCHAVLCSKEKIAQDICDTLREN 381
Cdd:cd00934   81 PNVFAFIAGEEGGS---GFRCHVFQCEDEEEAEEILQAIGQA 119
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 260-393 1.10e-19

Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain structure similar to those of pleckstrin homology (PH) and IRS-1-like PTB domains.


Pssm-ID: 214675  Cd Length: 134  Bit Score: 85.83  E-value: 1.10e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618286   260 PDPEFKVSYLGNVLTGWAKGEGCVEKQLNTLWRNYTQHSKPDVIMRLKVCASGLKATTRQHG--LTEYWAHRITYCCAPK 337
Cdd:smart00462   2 SGVSFRVKYLGSVEVPEARGLQVVQEAIRKLRAAQGSEKKEPQKVILSISSRGVKLIDEDTKavLHEHPLRRISFCAVGP 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 442618286   338 NYPRVFCWIYRHEGrklKHELRCHAVLCSKEkiAQDICDTLRENLESALREFKREK 393
Cdd:smart00462  82 DDLDVFGYIARDPG---SSRFACHVFRCEKA--AEDIALAIGQAFQLAYELKLKAR 132
PTB_LDLRAP-mammal-like cd13159
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in mammals and similar proteins ...
 263-374 5.61e-12

Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in mammals and similar proteins Phosphotyrosine-binding (PTB) PH-like fold; The null mutations in the LDL receptor adaptor protein 1 (LDLRAP1) gene, which serves as an adaptor for LDLR endocytosis in the liver, causes autosomal recessive hypercholesterolemia (ARH). LDLRAP1 contains a single PTB domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd contains mammals, insects, and sponges.


Pssm-ID: 269981  Cd Length: 123  Bit Score: 63.50  E-value: 5.61e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618286 263 EFKVSYLGNVLTGWAKGEGCVE----------KQLNTLWRNYTqhskpdvimrLKVCASGLKAT--TRQHGLTEYWAHRI 330
Cdd:cd13159    4 TFYLKYLGSTLVEKPKGEGATAeavktiiamaKASGKKLQKVT----------LTVSPKGIKVTdsATNETILEVSIYRI 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 442618286 331 TYCCAPKNYPRVFCWIyrheGRKLKHE-LRCHAVLCSKEKIAQDI 374
Cdd:cd13159   74 SYCTADANHDKVFAFI----ATNQDNEkLECHAFLCAKRKMAQAV 114
PTB_P-CLI1 cd13167
PTB-containing, cubilin and LRP1-interacting protein Phosphotyrosine-binding (PTB) PH-like ...
 264-384 2.55e-09

PTB-containing, cubilin and LRP1-interacting protein Phosphotyrosine-binding (PTB) PH-like fold; P-CLI1 (also called Phosphotyrosine interaction domain-containing protein 1) increases proliferation of preadipocytes without affecting adipocytic differentiation. It forms a complex with PID1/PCLI1, LRP1 and CUBNI. It is found in subcutaneous fat, heart, skeletal muscle, brain, colon, thymus, spleen, kidney, liver, small intestine, placenta, lung and peripheral blood leukocyte. P-CLI1 contains a single PTB domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains.


Pssm-ID: 269988  Cd Length: 139  Bit Score: 56.54  E-value: 2.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618286 264 FKVSYLGNV-LTGWAKGEGCVEKQLNTLWRNYTQhSKPDVI----------MRLKVCASGLKATTRQHgLTEYWAHRITY 332
Cdd:cd13167    3 YKVTYLGKVsTTGTQFLSGCTESPVIELWKKHTL-AREDIFpsnalleirpFQVRLHHLDLRGEATVH-MDTFQVARIAY 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 442618286 333 CCAPKNY-PRVFCWIYRHEGRKLKHELRCHAVLC-SK---EKIAQDICDTLRENLES 384
Cdd:cd13167   81 CTADHNIsPNIFAWVYREINDDLSFQMDCHAVECeSKleaKKLAHAMMEAFKKTFHS 137
PTB_LDLRAP_insect-like cd13160
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in insects and similar proteins ...
 262-374 9.65e-08

Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in insects and similar proteins Phosphotyrosine-binding (PTB) PH-like fold; The null mutations in the LDL receptor adaptor protein 1 (LDLRAP1) gene, which serves as an adaptor for LDLR endocytosis in the liver, causes autosomal recessive hypercholesterolemia (ARH). LDLRAP1 contains a single PTB domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd contains insects, ticks, sea urchins, and nematodes.


Pssm-ID: 269982  Cd Length: 125  Bit Score: 51.57  E-value: 9.65e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618286 262 PEFKVSYLGNvltGWAKGegcvekqlntLW-RNYTqhSKPDV-------------IMRLKVCASGLK-----ATTRQHGL 322
Cdd:cd13160    1 PVFTVKYLGR---MPARG----------LWgIKHT--RKPLVdalknlpkgktlpKTKLEVSSDGVKleelrGGFGSSKT 65

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 442618286 323 TEYWAHRITYCCAPKNYPRVFCWIYRHEGRKLKHELRCHAVLCSKEKIAQDI 374
Cdd:cd13160   66 VFFPIHTISYGVQDLVHTRVFSMIVVGEQDSSNHPFECHAFVCDSRADARNL 117
PTB_CED-6 cd01273
Cell death protein 6 homolog (CED-6/GULP1) Phosphotyrosine-binding (PTB) domain; CED6 (also ...
 257-389 2.00e-03

Cell death protein 6 homolog (CED-6/GULP1) Phosphotyrosine-binding (PTB) domain; CED6 (also known as GULP1: engulfment adaptor PTB domain containing 1) is an adaptor protein involved in the specific recognition and engulfment of apoptotic cells. CED6 has been shown to interact with the cytoplasmic tail of another protein involved in the engulfment of apoptotic cells, CED1. CED6 has a C-terminal PTB domain, which can bind to NPXY motifs. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.


Pssm-ID: 269971  Cd Length: 144  Bit Score: 39.57  E-value: 2.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618286 257 ISTPDP------EFKVSYLGNVLTGWAKGEGCVEKQLNTLwrNYTQHSK-------PDV-----IMRLKVCASGLKATTR 318
Cdd:cd01273    1 IHPPEAlikghvAYLVKFLGCTEVEQPKGTEVVKEAIRKL--KFARQLKksegaklPKVelqisIDGVKIQDPKTKVIMH 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442618286 319 QHGLteywaHRITYCCAPKNYPRVFCWIYRHEGRKlKHElrCHAVLCskEKIAQDICDTLRENLESALREF 389
Cdd:cd01273   79 QFPL-----HRISFCADDKTDKRIFSFIAKDSESE-KHL--CFVFDS--EKLAEEITLTIGQAFDLAYRRF 139
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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