208:. The integrins contain multiple divalent cation binding sites in the extracellular domain ). The integrin cation binding sites can be occupied by Ca2+ or by Mn2+ ions. Cations are necessary but not sufficient for integrins to convert from the inactive bent conformation into the active extended conformation. Both the presence of cations bound to the multiple cation binding sites is required, along with the direct physical association with ECM ligands for integrins to attain the extended structure and concomitant activation. Thus, rise in extracellular Ca2+ ions may serve to prime the integrin heterodimer. The release of intracellular Ca2+ have been shown to be important for integrin inside-out activation. However, extracellular Ca2+ binding may exert different effects depending on the type of integrin and the cation concentration. Integrins regulate their activity within the body by changing conformation. Most exist at rest in a low
45:. In essence, CAMs help cells stick to each other and to their surroundings. CAMs are crucial components in maintaining tissue structure and function. In fully developed animals, these molecules play an integral role in generating force and movement and consequently ensuring that organs are able to execute their functions normally. In addition to serving as "molecular glue", CAMs play important roles in the cellular mechanisms of growth, contact inhibition, and apoptosis. Aberrant expression of CAMs may result in a wide range of pathologies, ranging from frostbite to cancer.
409:. Lymphocyte homing is a key process occurring in a strong immune system. It controls the process of circulating lymphocytes adhering to particular regions and organs of the body. The process is highly regulated by cell adhesion molecules, particularly, the addressin also known as MADCAM1. This antigen is known for its role in tissue-specific adhesion of lymphocytes to high endothelium venules. Through these interactions they play a crucial role in orchestrating circulating lymphocytes.
425:
200:, as they consist of an alpha and beta subunit. There are currently 18 alpha subunits and 8 beta subunits, which combine to make up 24 different integrin combinations. Within each of the alpha and beta subunits there is a large extracellular domain, a transmembrane domain and a short cytoplasmic domain. The extracellular domain is where the
108:
One classification system involves the distinction between calcium-independent CAMs and calcium-dependent CAMs. The Ig-superfamily CAMs do not depend on Ca while integrins, cadherins and selectins depend on Ca. In addition, integrins participate in cell–matrix interactions, while other CAM families
412:
CAM function in cancer metastasis, inflammation, and thrombosis makes it a viable therapeutic target that is currently being considered. For example, they block the metastatic cancer cells' ability to extravasate and home to secondary sites. This has been successfully demonstrated in metastatic
1334:
Berg, Ellen Lakey; Goldstein, Leslie A.; Jimla, Mark A.; Nakache, Maurice; Picker, Louis J.; Streeter, Philip R.; Wu, Nora W.; Zhou, David; Butcher, Eugene C. (1 April 1989). "Homing
Receptors and Vascular Addressins: Cell Adhesion Molecules that Direct Lymphocyte Traffic".
397:), which is a mucin-type glycoprotein expressed on all white blood cells. Selectins have been implicated in several roles but they are especially important in the immune system by helping white blood cell homing and trafficking.
315:. Each cadherin exhibits a unique pattern of tissue distribution that is carefully controlled by calcium. The diverse family of cadherins include epithelial (E-cadherins), placental (P-cadherins), neural (N-cadherins), retinal (
311:. Cadherins also contribute significantly to the development of the nervous system. The distinct temporal and spatial localization of cadherins implicates these molecules as major players in the process of
413:
melanoma that hones to the lungs. In mice, when antibodies directed against CAMs in the lung endothelium were used as treatment there was a significant reduction in the number of metastatic sites.
131:
CAMs (IgSF CAMs) is regarded as the most diverse superfamily of CAMs. This family is characterized by their extracellular domains containing Ig-like domains. The Ig domains are then followed by
135:
repeats and IgSFs are anchored to the membrane by a GPI moiety. This family is involved in both homophilic or heterophilic binding and has the ability to bind integrins or different IgSF CAMs.
405:
The variety in CAMs leads to diverse functionality of these proteins in the biological setting. One of the CAMS that are particularly important in the lymphocyte homing is
212:
state, which can be altered to high affinity through an external agonist which causes a conformational change within the integrin, increasing their affinity.
1531:
61:, a transmembrane domain, and an extracellular domain. These proteins can interact in several different ways. The first method is through
2075:
94:
1680:
16:
This article is about cell adhesion molecules. For the role of CAMs in the formation and stabilization of neural synapses, see
1524:
1497:
585:
Korthuis RJ, Anderson DC, Granger DN (March 1994). "Role of neutrophil-endothelial cell adhesion in inflammatory disorders".
319:), brain (B-cadherins and T-cadherins), and muscle (M-cadherins). Many cell types express combinations of cadherin types.
1486:
Andreoli, Thomas E.; Brown, A. M.; Fambrough, D. M.; Hoffman, Joseph F.; Schultz, Stanley G.; Welsh, Michael J. (2013).
760:
Lodish, Harvey; Berk, Arnold; Zipursky, S. Lawrence; Matsudaira, Paul; Baltimore, David; Darnell, James (2000-01-01).
2049:
209:
2070:
1517:
1579:
972:"Crystal Structure of the Extracellular Segment of Integrin alpha Vbeta 3 in Complex with an Arg-Gly-Asp Ligand"
1283:
Cavallaro U, Christofori G (February 2004). "Cell adhesion and signalling by cadherins and Ig-CAMs in cancer".
1025:
Dai, Aguang; Ye, Feng; Taylor, Dianne W.; Hu, Guiqing; Ginsberg, Mark H.; Taylor, Kenneth A. (November 2015).
1569:
132:
1997:
128:
174:
782:
2029:
476:
472:
190:
182:
1197:
Buxton RS, Magee AI (June 1992). "Structure and interactions of desmosomal and other cadherins".
186:
312:
54:
17:
393:). The best-characterized ligand for the three selectins is P-selectin glycoprotein ligand-1 (
1736:
1509:
1487:
769:
703:"Distinct calcium-independent and calcium-dependent adhesion systems of chicken embryo cells"
448:
57:
and are composed of three conserved domains: an intracellular domain that interacts with the
326:
domain has major repeats called extracellular cadherin domains (ECD). Sequences involved in
1708:
1694:
1027:"The Structure of a Full-length Membrane-embedded Integrin Bound to a Physiological Ligand"
983:
714:
177:
and the intracellular signalling pathways, which can play roles in cell behaviours such as
157:, one of the major classes of receptors within the ECM, mediate cell–ECM interactions with
38:
8:
1573:
646:
987:
718:
1463:
1430:
1368:
1348:
1316:
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1233:
1169:
1136:
1112:
1077:
1053:
1026:
1007:
907:
851:
826:
683:
253:
1210:
1078:"The Calcium-Sensing Receptor and Integrins in Cellular Differentiation and Migration"
971:
809:
737:
702:
554:
537:
295:
Cadherins are notable in embryonic development. For example, cadherins are crucial in
1493:
1468:
1450:
1411:
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1308:
1300:
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1156:
1117:
1099:
1058:
999:
952:
947:
930:
911:
894:
GarcĂa AJ (December 2005). "Get a grip: integrins in cell-biomaterial interactions".
856:
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671:
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518:
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506:
281:
34:
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942:
903:
846:
838:
805:
732:
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687:
667:
594:
549:
502:
796:
Brown, K; Yamada, K (1995), "The Role of
Integrins during Vertebrae Development",
658:
Chothia C, Jones EY (1997). "The molecular structure of cell adhesion molecules".
205:
69:
binding, meaning a CAM on one cell will bind with different CAMs on another cell.
1446:
761:
443:
430:
78:
2064:
1856:
1454:
1407:
1356:
1304:
1160:
1103:
1094:
606:
563:
538:"Cell adhesion: the molecular basis of tissue architecture and morphogenesis"
514:
438:
338:
323:
265:
102:
42:
1043:
995:
1827:
1823:
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1815:
1608:
1472:
1312:
1269:
1178:
1121:
1062:
1003:
915:
860:
628:
490:
453:
362:
341:. The cytoplasmic domain has specific regions where catenin proteins bind.
296:
58:
1415:
1364:
1218:
956:
746:
727:
679:
614:
571:
522:
227:
trigger the integrin into its high affinity state, which causes increased
1900:
1833:
1793:
1783:
1250:
374:
277:
269:
197:
170:
166:
2006:
1977:
1972:
1967:
1890:
1811:
1431:"Role of beta7 integrins in intestinal lymphocyte homing and retention"
1234:"The Function of E-Cadherin in Stem Cell Pluripotency and Self-Renewal"
386:
378:
370:
228:
162:
1152:
842:
65:
binding, where CAMs bind with the same CAMs. They are also capable of
1803:
1603:
406:
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2012:
1959:
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1672:
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308:
304:
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247:
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158:
154:
149:
123:
90:
86:
289:
33:) are a subset of cell surface proteins that are involved in the
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2017:
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1635:
1618:
1613:
1587:
1485:
1386:
Picker, Louis (1 June 1994). "Control of lymphocyte homing".
700:
366:
285:
82:
759:
629:"Single-pass transmembrane adhesion and structural proteins"
2039:
2034:
2001:
1940:
1910:
1905:
1895:
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1730:
1716:
1702:
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1598:
316:
273:
288:
filament network through specific linking proteins called
77:
There are four major superfamilies or groups of CAMs: the
1333:
1137:"The regulation of integrin function by divalent cations"
701:
Brackenbury R, Rutishauser U, Edelman GM (January 1981).
361:
are a family of heterophilic CAMs that are dependent on
824:
584:
1428:
1282:
1076:
Tharmalingam, Sujeenthar; Hampson, David R. (2016).
825:
Humphries JD, Byron A, Humphries MJ (October 2006).
491:"The molecular structure of cell adhesion molecules"
420:
1075:
1429:Gorfu G, Rivera-Nieves J, Ley K (September 2009).
1489:Molecular Biology of Membrane Transport Disorders
795:
2062:
820:
818:
173:. Integrins provide essential links between the
874:
872:
870:
400:
1525:
1192:
1190:
1188:
1024:
815:
635:. College of Pharmacy, University of Michigan
1422:
1276:
657:
488:
1196:
1135:Zhang, Kun; Chen, JianFeng (January 2012).
922:
867:
337:binding between the ECDs are necessary for
105:are also considered to be a class of CAMs.
1532:
1518:
1231:
1185:
928:
887:
694:
651:
578:
369:for binding. The three family members are
1492:. Springer Science & Business Media.
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1168:
1134:
1111:
1093:
1052:
1042:
946:
893:
850:
736:
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553:
475:at the U.S. National Library of Medicine
215:An example of this is the aggregation of
81:super family of cell adhesion molecules (
1552:
789:
535:
878:
231:binding, causing platelet aggregation.
109:participate in cell–cell interactions.
2063:
1759:
1385:
762:"Cell–Cell Adhesion and Communication"
112:
95:C-type of lectin-like domains proteins
37:of cells with other cells or with the
1513:
969:
138:
72:
13:
2076:Single-pass transmembrane proteins
1349:10.1111/j.1600-065X.1989.tb00010.x
908:10.1016/j.biomaterials.2005.05.029
489:Chothia, C.; Jones, E. Y. (1997).
204:binds through the use of divalent
14:
2087:
935:Eur J Obstet Gynecol Reprod Biol
672:10.1146/annurev.biochem.66.1.823
507:10.1146/annurev.biochem.66.1.823
423:
53:CAMs are typically single-pass
23:Subset of cell adhesion proteins
1479:
1379:
1327:
1232:Soncin, F.; Ward, M.C. (2011).
1225:
1128:
1069:
1031:Journal of Biological Chemistry
1018:
963:
881:Integrin, Adhesion/cell-matrix
827:"Integrin ligands at a glance"
753:
621:
536:Gumbiner, B. M. (1996-02-09).
529:
482:
466:
1:
1388:Current Opinion in Immunology
1211:10.1016/s1043-4682(10)80012-1
1141:Cell Adhesion & Migration
810:10.1016/s1044-5781(06)80016-2
555:10.1016/s0092-8674(00)81279-9
495:Annual Review of Biochemistry
459:
1400:10.1016/0952-7915(94)90118-X
948:10.1016/0028-2243(94)01987-I
931:"Integrins and reproduction"
707:Proc. Natl. Acad. Sci. U.S.A
599:10.1016/0883-9441(94)90032-9
344:
234:
143:
117:
48:
7:
970:Xiong, J.-P. (2002-04-05).
416:
401:Biological function of CAMs
282:intermediate cell junctions
133:Fibronectin type III domain
41:(ECM), in a process called
10:
2092:
1998:Lymphocyte homing receptor
1447:10.2174/156652409789105525
348:
280:) are concentrated at the
238:
147:
129:Immunoglobulin superfamily
121:
15:
1990:
1958:
1883:
1855:
1802:
1776:
1767:
1758:
1671:
1560:
1551:
929:Vinatier D (March 1995).
299:for the formation of the
268:. The classic cadherins (
175:extracellular environment
93:, and the Superfamily of
2030:Carcinoembryonic antigen
1884:Unconventional/ungrouped
1095:10.3389/fphys.2016.00190
477:Medical Subject Headings
2071:Cell adhesion molecules
1545:cell adhesion molecules
1082:Frontiers in Physiology
1044:10.1074/jbc.M115.682377
996:10.1126/science.1069040
473:Cell+Adhesion+Molecules
55:transmembrane receptors
27:Cell adhesion molecules
777:Cite journal requires
313:synaptic stabilization
18:Synaptic stabilization
1737:Glycoprotein IIb/IIIa
1337:Immunological Reviews
798:Developmental Biology
728:10.1073/pnas.78.1.387
449:Immunological synapse
365:carbohydrates, e.g.,
1709:Macrophage-1 antigen
1695:Integrin alphaXbeta2
1251:10.3390/genes2010229
883:. Seattle: Elsevier.
284:, which link to the
39:extracellular matrix
1574:Myelin protein zero
1553:Calcium-independent
1037:(45): 27168–27175.
988:2002Sci...296..151X
879:Schnapp, L (2006).
719:1981PNAS...78..387B
647:Membranome database
219:; Agonists such as
113:Calcium-independent
660:Annu. Rev. Biochem
2058:
2057:
1986:
1985:
1954:
1953:
1760:Calcium-dependent
1754:
1753:
1541:Membrane proteins
1499:978-1-4613-1143-0
1153:10.4161/cam.18702
982:(5565): 151–155.
843:10.1242/jcs.03098
837:(Pt 19): 3901–3.
139:Calcium-dependent
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73:Families of CAMs
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251:are homophilic
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183:differentiation
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24:
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11:
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1435:Curr. Mol. Med
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1394:(3): 394–406.
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902:(36): 7525–9.
886:
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548:(3): 345–357.
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444:Cell migration
441:
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431:Biology portal
418:
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349:Main article:
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239:Main article:
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196:Integrins are
148:Main article:
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122:Main article:
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79:immunoglobulin
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1857:Protocadherin
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1448:
1444:
1441:(7): 836–50.
1440:
1436:
1432:
1425:
1417:
1413:
1409:
1405:
1401:
1397:
1393:
1389:
1382:
1374:
1370:
1366:
1362:
1358:
1354:
1350:
1346:
1342:
1338:
1330:
1322:
1318:
1314:
1310:
1306:
1302:
1298:
1294:
1291:(2): 118–32.
1290:
1286:
1279:
1271:
1267:
1262:
1257:
1252:
1247:
1243:
1239:
1235:
1228:
1220:
1216:
1212:
1208:
1205:(3): 157–67.
1204:
1200:
1193:
1191:
1189:
1180:
1176:
1171:
1166:
1162:
1158:
1154:
1150:
1146:
1142:
1138:
1131:
1123:
1119:
1114:
1109:
1105:
1101:
1096:
1091:
1087:
1083:
1079:
1072:
1064:
1060:
1055:
1050:
1045:
1040:
1036:
1032:
1028:
1021:
1013:
1009:
1005:
1001:
997:
993:
989:
985:
981:
977:
973:
966:
958:
954:
949:
944:
940:
936:
932:
925:
917:
913:
909:
905:
901:
897:
890:
882:
875:
873:
871:
862:
858:
853:
848:
844:
840:
836:
832:
828:
821:
819:
811:
807:
803:
799:
792:
784:
771:
763:
756:
748:
744:
739:
734:
729:
724:
720:
716:
713:(1): 387–91.
712:
708:
704:
697:
689:
685:
681:
677:
673:
669:
665:
661:
654:
648:
634:
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581:
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569:
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508:
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500:
496:
492:
485:
478:
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469:
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455:
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445:
442:
440:
439:Cell membrane
437:
436:
432:
426:
421:
414:
410:
408:
398:
396:
392:
388:
384:
380:
376:
372:
368:
364:
360:
359:
352:
342:
340:
339:cell adhesion
325:
324:extracellular
320:
318:
314:
310:
306:
302:
298:
293:
291:
287:
283:
279:
275:
271:
267:
266:glycoproteins
262:
250:
249:
242:
232:
230:
226:
222:
218:
213:
211:
207:
203:
199:
198:heterodimeric
194:
192:
191:transcription
188:
184:
180:
176:
172:
168:
164:
160:
156:
151:
136:
134:
130:
125:
110:
106:
104:
103:Proteoglycans
100:
96:
92:
88:
84:
80:
70:
68:
64:
60:
56:
46:
44:
43:cell adhesion
40:
36:
32:
28:
19:
2011:
1544:
1488:
1481:
1438:
1434:
1424:
1391:
1387:
1381:
1340:
1336:
1329:
1288:
1284:
1278:
1241:
1237:
1227:
1202:
1198:
1147:(1): 20–29.
1144:
1140:
1130:
1085:
1081:
1071:
1034:
1030:
1020:
979:
975:
965:
941:(1): 71–81.
938:
934:
924:
899:
896:Biomaterials
895:
889:
880:
834:
830:
804:(2): 69–77,
801:
797:
791:
770:cite journal
755:
710:
706:
696:
663:
659:
653:
637:. Retrieved
632:
623:
593:(1): 47–71.
590:
586:
580:
545:
541:
531:
498:
494:
484:
468:
454:Trogocytosis
411:
404:
356:
354:
321:
297:gastrulation
294:
246:
244:
214:
195:
153:
127:
107:
98:
76:
67:heterophilic
66:
62:
59:cytoskeleton
52:
30:
26:
25:
1834:Desmocollin
1343:(1): 5–18.
831:J. Cell Sci
639:October 20,
587:J Crit Care
501:: 823–862.
375:endothelial
363:fucosylated
317:R-cadherins
264:-dependent
171:vitronectin
167:fibronectin
2065:Categories
2007:L-selectin
1978:P-selectin
1973:L-selectin
1968:E-selectin
1891:T-cadherin
1812:Desmoglein
1804:Desmosomal
666:: 823–62.
633:membranome
460:References
387:P-selectin
379:L-selectin
371:E-selectin
229:fibrinogen
163:fibrinogen
63:homophilic
1960:Selectins
1777:Classical
1769:Cadherins
1673:Integrins
1604:L1 family
1455:1566-5240
1408:0952-7915
1357:1600-065X
1305:1474-1768
1161:1933-6918
1104:1664-042X
607:0883-9441
564:0092-8674
515:0066-4154
407:addressin
383:leukocyte
358:selectins
345:Selectins
248:cadherins
235:Cadherins
217:platelets
179:apoptosis
155:Integrins
144:Integrins
118:IgSF CAMs
91:Integrins
87:Cadherins
49:Structure
2013:integrin
1562:IgSF CAM
1473:19860663
1373:37831094
1321:18383054
1313:14964308
1270:24710147
1179:22647937
1122:27303307
1063:26391523
1012:24339086
1004:11884718
916:16002137
861:16988024
417:See also
391:platelet
351:Selectin
309:ectoderm
305:endoderm
301:mesoderm
290:catenins
241:Cadherin
225:collagen
221:thrombin
210:affinity
187:survival
159:collagen
150:Integrin
124:IgSF CAM
1464:2770881
1416:7917107
1365:2670744
1261:3924836
1219:1623205
1170:3364134
1113:4880553
1088:: 190.
1054:4646401
984:Bibcode
976:Science
957:7781865
852:3380273
747:6165990
715:Bibcode
688:6298053
680:9242926
615:8199653
572:8608588
523:9242926
385:), and
206:cations
35:binding
1875:PCDH19
1870:PCDH15
1741:ITGA2B
1631:Nectin
1609:L1-CAM
1599:PE-CAM
1594:VCAM-1
1496:
1471:
1461:
1453:
1414:
1406:
1371:
1363:
1355:
1319:
1311:
1303:
1268:
1258:
1217:
1177:
1167:
1159:
1120:
1110:
1102:
1061:
1051:
1010:
1002:
955:
914:
859:
849:
745:
738:319058
735:
686:
678:
613:
605:
570:
562:
521:
513:
479:(MeSH)
395:PSGL-1
367:mucins
307:, and
202:ligand
189:, and
169:, and
83:IgCAMs
2050:EpCAM
2045:CD146
2022:LFA-1
2018:VLA-4
1991:Other
1946:CDH10
1936:CDH17
1931:CDH16
1926:CDH15
1921:CDH12
1916:CDH11
1865:PCDH1
1745:ITGB3
1727:CD49d
1723:VLA-4
1713:CD11b
1699:CD11c
1685:CD11a
1681:LFA-1
1661:CD155
1656:CADM3
1651:CADM1
1646:PVRL3
1641:PVRL2
1636:PVRL1
1619:NFASC
1614:NRCAM
1570:N-CAM
1369:S2CID
1317:S2CID
1238:Genes
1008:S2CID
684:S2CID
286:actin
99:CTLDs
2040:CD44
2035:CD24
2002:CD44
1941:CDH9
1911:CDH8
1906:CDH6
1901:CDH5
1896:CDH4
1846:DSC3
1842:DSC2
1838:DSC1
1828:DSG4
1824:DSG3
1820:DSG2
1816:DSG1
1794:CDH3
1789:CDH2
1784:CDH1
1731:CD29
1717:CD18
1703:CD18
1689:CD18
1624:CHL1
1580:ICAM
1494:ISBN
1469:PMID
1451:ISSN
1412:PMID
1404:ISSN
1361:PMID
1353:ISSN
1309:PMID
1301:ISSN
1266:PMID
1215:PMID
1175:PMID
1157:ISSN
1118:PMID
1100:ISSN
1059:PMID
1000:PMID
953:PMID
912:PMID
857:PMID
783:help
743:PMID
676:PMID
641:2018
611:PMID
603:ISSN
568:PMID
560:ISSN
542:Cell
519:PMID
511:ISSN
355:The
322:The
276:and
245:The
31:CAMs
1459:PMC
1443:doi
1396:doi
1345:doi
1341:108
1293:doi
1256:PMC
1246:doi
1207:doi
1165:PMC
1149:doi
1108:PMC
1090:doi
1049:PMC
1039:doi
1035:290
992:doi
980:296
943:doi
904:doi
847:PMC
839:doi
835:119
806:doi
733:PMC
723:doi
668:doi
645:in
595:doi
550:doi
503:doi
377:),
223:or
101:).
85:),
2067::
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328:Ca
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278:P-
274:N-
272:,
270:E-
254:Ca
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